|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-438 |
1.37e-92 |
|
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: 289.88 E-value: 1.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLIEL----------PMKYDELIVDP 70
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIsgevlldgrdLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 LSGVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKT 150
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 151 LFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEIILQKYVHLLSEyg 228
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVM-DDGRIVEDGPPEEILAAPQALAAV-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 229 vwhPRAWEFAPSRVDFPTTNSHLLQFKN-----GRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK- 302
Cdd:COG1123 241 ---PRLGAARGRAAPAAAAAEPLLEVRNlskryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRp 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 303 YQGDVYFENQRLTKIKHA-----AKHMYLVYQNPELQFI-TNSVYDEI----NIHfNHLSKDQSDDETIQLLKLLDL-EN 371
Cdd:COG1123 318 TSGSILFDGKDLTKLSRRslrelRRRVQMVFQDPYSSLNpRMTVGDIIaeplRLH-GLLSRAERRERVAELLERVGLpPD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 372 VKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQK-RINLGQSIFMVTHD 438
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHD 464
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-202 |
1.12e-64 |
|
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: 207.70 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 3 KVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP------NLIELPMKYDEL-IVDPLSGVI 75
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGptsgevLVDGKDLTKLSLkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 FQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDE 155
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 612672732 156 PTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIWNHVDRVILMD 202
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
261-455 |
5.84e-59 |
|
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: 192.68 E-value: 5.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTK--IKHAAKHMYLVYQNPELQFIT 337
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGKDLTKlsLKELRRKVGLVFQNPDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 338 NSVYDEINIHFNHLSKDQSDDETI--QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:cd03225 91 PTVEEEVAFGLENLGLPEEEIEERveEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 416 FQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03225 171 RELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-223 |
5.85e-54 |
|
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: 180.22 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielPMK----YDELIVDPLS----- 72
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK-----PTSgevlVDGKDITKKNlrelr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ---GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSK 149
Cdd:COG1122 75 rkvGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 150 TLFLDEPTAMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQKYVHL 223
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLD-DGRIVADGTPREVFSDYELL 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
271-464 |
1.06e-43 |
|
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: 153.26 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTK--IKHAAKHMYLVYQNPELQFITNSVYDEI--- 344
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKpTSGEVLVDGKDITKknLRELRRKVGLVFQNPDDQLFAPTVEEDVafg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 --NIHfnhLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLF 422
Cdd:COG1122 101 peNLG---LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 612672732 423 QKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLdCDGDT 464
Cdd:COG1122 178 KRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV-ADGTP 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
277-457 |
1.25e-43 |
|
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: 152.41 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLtKIKHAAKHMYLVYQNPELQFITNSVYDEINIHFNHLSKDQ 355
Cdd:cd03226 26 GEIIALTGKNGAGKTTLAKILAGLIKeSSGSILLNGKPI-KAKERRKSIGYVMQDVDYQLFTDSVREELLLGLKELDAGN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 356 SDDETIqlLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMV 435
Cdd:cd03226 105 EQAETV--LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI 182
|
170 180
....*....|....*....|..
gi 612672732 436 THDDEIIERYPSRRLKISDGAL 457
Cdd:cd03226 183 THDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
271-457 |
9.57e-37 |
|
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: 134.54 E-value: 9.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHA------AKHMYLVYQNPELqfITN-SVYD 342
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKelaafrRRHIGFVFQSFNL--LPDlTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 eiNI----HFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:cd03255 102 --NVelplLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 419 IKLFQKrIN--LGQSIFMVTHDDEIIERYpSRRLKISDGAL 457
Cdd:cd03255 180 MELLRE-LNkeAGTTIVVVTHDPELAEYA-DRIIELRDGKI 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-228 |
1.54e-35 |
|
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: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpMKYDE--LIVDPLS------- 72
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--------LLPTSgkVTVDGLDtldeenl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -------GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtpETYIKD----LSGGMKQKLAIV 141
Cdd:TIGR04520 73 weirkkvGMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGM----EDFRDRephlLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 142 ETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIwNHVDRVILMDyNGNIIADECPEIILQK 219
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMN-KGKIVAEGTPREIFSQ 226
|
....*....
gi 612672732 220 yVHLLSEYG 228
Cdd:TIGR04520 227 -VELLKEIG 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
271-457 |
3.14e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.55 E-value: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAA------KHMYLVYQN----PELqfitnS 339
Cdd:COG1136 28 SLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGQDISSLSERElarlrrRHIGFVFQFfnllPEL-----T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 340 VYDeiNI----HFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:COG1136 103 ALE--NValplLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 612672732 416 FQLIKLFQkRIN--LGQSIFMVTHDDEIIErYPSRRLKISDGAL 457
Cdd:COG1136 181 EEVLELLR-ELNreLGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
4.76e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 130.98 E-value: 4.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPS--GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielP----MKYDELIVDPLS-- 72
Cdd:COG1116 7 ALELRGVSKRFPTggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEK-----PtsgeVLVDGKPVTGPGpd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQDPDSqfcMP--KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSK 149
Cdd:COG1116 82 rGVVFQEPAL---LPwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 150 TLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHkvkhiwnHV-------DRVILMDYN-GNIIAD 210
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTH-------DVdeavflaDRVVVLSARpGRIVEE 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
271-459 |
1.58e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA-----KHMYLVYQnpELQFITN-SVYDe 343
Cdd:COG2884 22 SLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERpTSGQVLVNGQDLSRLKRREipylrRRIGVVFQ--DFRLLPDrTVYE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 iNIHF----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLI 419
Cdd:COG2884 99 -NVALplrvTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 420 KLFqKRIN-LGQSIFMVTHDDEIIERYPSRRLKISDGALLD 459
Cdd:COG2884 178 ELL-EEINrRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-220 |
2.93e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.26 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-----------NLIELPMKYDELIvdp 70
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRptsgevrvlgeDVARDPAEVRRRI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 lsGVIFQDP--DSQFcmpKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQS 148
Cdd:COG1131 76 --GYVPQEPalYPDL---TVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 149 KTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVehkVKHIWNHV----DRVILMDyNGNIIADECPEIILQKY 220
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLL---STHYLEEAerlcDRVAIID-KGRIVADGTPDELKARL 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-186 |
1.11e-33 |
|
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: 126.05 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQR--KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielP----MKYDELIVDPLS--- 72
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER-----PtsgeVLVDGEPVTGPGpdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 GVIFQDPDSqfcMP--KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKT 150
Cdd:cd03293 76 GYVFQQDAL---LPwlTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 612672732 151 LFLDEPTAMLDVQATEDLWTKLIELWED--QTVVIVEH 186
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTH 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
250-456 |
2.62e-30 |
|
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: 116.42 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 250 HLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIK-HAAKHMYLV 327
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpSAGEVLWNGEPIRDAReDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 328 YQNPELqfitnsvYDEI----NIHF-NHLSKDQSDDETI-QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADII 401
Cdd:COG4133 81 GHADGL-------KPELtvreNLRFwAALYGLRADREAIdEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 402 FLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIEryPSRRLKISDGA 456
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
251-457 |
3.73e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 122.70 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRI--IRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLI----KYQGDVYFENQRLTKIKHA--AK 322
Cdd:COG1123 4 LLEVRDLSVryPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggRISGEVLLDGRDLLELSEAlrGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 323 HMYLVYQNPELQFITNSVYDEIN--IHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADI 400
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 401 IFLDEPTFGLDSHNTFQLIKLFQK-RINLGQSIFMVTHDDEIIERYPSRRLKISDGAL 457
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
1.88e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.24 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIELpmKYDELIVDPLS------- 72
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGEI--KIDGITISKENlkeirkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtpETYIK----DLSGGMKQKLAIVETILQQ 147
Cdd:PRK13632 85 iGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM----EDYLDkepqNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 148 SKTLFLDEPTAMLDVQATEDLWTKLIELWE--DQTVVIVEHKVKHIWNhVDRVILMDyNGNIIADECPEIIL 217
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAIL-ADKVIVFS-EGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-218 |
2.16e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.27 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP---NLIELP-MKYDELIVDPLS---GV 74
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpeaGTITVGgMVLSEETVWDVRrqvGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 75 IFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtpETYIKD----LSGGMKQKLAIVETILQQSKT 150
Cdd:PRK13635 86 VFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM----EDFLNRephrLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 151 LFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNhVDRVILMDyNGNIIADECPEIILQ 218
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQ-ADRVIVMN-KGEILEEGTPEEIFK 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
252-440 |
4.20e-29 |
|
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: 113.38 E-value: 4.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHMYLVYQN 330
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 331 PELqFITNSVYDeiNIHF----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEP 406
Cdd:cd03259 81 YAL-FPHLTVAE--NIAFglklRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 612672732 407 TFGLDSHNTFQLIKLFQKRI-NLGQSIFMVTHDDE 440
Cdd:cd03259 158 LSALDAKLREELREELKELQrELGITTIYVTHDQE 192
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-202 |
8.75e-29 |
|
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: 110.80 E-value: 8.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 3 KVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDPDS 81
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK---------------PTSGeILIDGKDI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 qfcmpkvyeelafvlenRQVPREDMDALIInalnmvnlnvtpetYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLD 161
Cdd:cd00267 64 -----------------AKLPLEELRRRIG--------------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 612672732 162 VQATEDLWTKLIELWEDQ-TVVIVEHKVKHIWNHVDRVILMD 202
Cdd:cd00267 113 PASRERLLELLRELAEEGrTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-209 |
1.60e-28 |
|
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: 112.21 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPN------LIELPMKYDELIVDPLSGVI 75
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtsgtayINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 FQDpDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDE 155
Cdd:cd03263 81 PQF-DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 612672732 156 PTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNHVDRVILMdYNGNIIA 209
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIM-SDGKLRC 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
271-438 |
3.34e-28 |
|
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: 111.44 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKI-----KHAAKHMYLVYQNPELQF-----ITNS 339
Cdd:cd03257 25 SFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLsrrlrKIRRKEIQMVFQDPMSSLnprmtIGEQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 340 VYDEINIHFNHLSKDQSDDETIQLLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:cd03257 105 IAEPLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQI 184
|
170 180
....*....|....*....|.
gi 612672732 419 IKLFQK-RINLGQSIFMVTHD 438
Cdd:cd03257 185 LDLLKKlQEELGLTLLFITHD 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-207 |
3.74e-28 |
|
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: 109.79 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIF---QD 78
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK---------------PDSGEIKvlgKD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 PDSQFcmPKVYEELAFVLENRQVPRedmdaliinalnmvnlNVTPETYIKdLSGGMKQKLAIVETILQQSKTLFLDEPTA 158
Cdd:cd03230 64 IKKEP--EEVKRRIGYLPEEPSLYE----------------NLTVRENLK-LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 612672732 159 MLDVQATEDLWTKLIELWEDQ-TVVIVEHKVKHIWNHVDRVILMDyNGNI 207
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILN-NGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-209 |
4.27e-28 |
|
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: 110.69 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielPMKYDELI-------VDPLS-- 72
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER-----PDSGEILIdgrdvtgVPPERrn 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQDPdSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:cd03259 74 iGMVFQDY-ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 152 FLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIA 209
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMN-EGRIVQ 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
5.27e-28 |
|
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: 111.12 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLIELP---------MKYDELIVDPLS 72
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPdegevlldgKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -----GVIFQDPdSQFCMPkVYEELAFVLENRQV-PREDMDALIINALNMVNL--NVTPETYIKDLSGGMKQKLAIVETI 144
Cdd:cd03260 79 lrrrvGMVFQKP-NPFPGS-IYDNVAYGLRLHGIkLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 145 LQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEII 216
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFL-LNGRLVEFGPTEQI 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-218 |
7.37e-28 |
|
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: 110.84 E-value: 7.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielPMK----YDELIVDPLS---- 72
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-----PDSgeilVDGQDITGLSekel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -------GVIFQDP---DSqfcMPkVYEELAFVL-ENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIV 141
Cdd:COG1127 78 yelrrriGMLFQGGalfDS---LT-VFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 142 ETILQQSKTLFLDEPTAMLDVQATEDLwTKLI-ELWEDQ--TVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEIILQ 218
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVI-DELIrELRDELglTSVVVTHDLDSAFAIADRVAVL-ADGKIIAEGTPEELLA 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
271-461 |
1.41e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.15 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAK-HMYLVYQNPEL-QFITnsVYDeiNIH 347
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDVARDPAEVRrRIGYVPQEPALyPDLT--VRE--NLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 348 F----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQ 423
Cdd:COG1131 96 FfarlYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLR 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 612672732 424 KRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDCD 461
Cdd:COG1131 176 ELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
251-438 |
1.63e-27 |
|
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: 110.13 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHA--AKHMYLV 327
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRelARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 328 YQNPELQF-ITnsVYDEI----NIHFNHLSKDQSDDETI--QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADI 400
Cdd:COG1120 81 PQEPPAPFgLT--VRELValgrYPHLGLFGRPSAEDREAveEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 401 IFLDEPTFGLDSHNTFQLIKLFqKRIN--LGQSIFMVTHD 438
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELL-RRLAreRGRTVVMVLHD 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-207 |
2.51e-27 |
|
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: 108.73 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIF--DHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpMKYD--ELIVD--PLS--- 72
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL--------DRPTsgEVRVDgtDISkls 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ------------GVIFQD----PD-SqfcmpkVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMK 135
Cdd:cd03255 73 ekelaafrrrhiGFVFQSfnllPDlT------ALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIEL--WEDQTVVIVEHKVKhIWNHVDRVILMDyNGNI 207
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPE-LAEYADRIIELR-DGKI 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-226 |
3.67e-27 |
|
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: 114.93 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPN-----LI-ELPMKYdeliVDPLS--- 72
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPtsgriLIdGIDLRQ----IDPASlrr 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 --GVIFQDP----DSqfcmpkVYEELAfvLENRQVPREDmdalIINALNMVNL----NVTP---ETYIKD----LSGGMK 135
Cdd:COG2274 550 qiGVVLQDVflfsGT------IRENIT--LGDPDATDEE----IIEAARLAGLhdfiEALPmgyDTVVGEggsnLSGGQR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNIIADECPEI 215
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI-RLADRIIVLD-KGRIVEDGTHEE 695
|
250
....*....|....
gi 612672732 216 ILQK---YVHLLSE 226
Cdd:COG2274 696 LLARkglYAELVQQ 709
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
253-455 |
3.76e-27 |
|
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: 106.56 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 253 QFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA--KHMYLVYQ 329
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 330 npelqfitnsvydeinihfnhlskdqsddetiqllklldlenvkdqhpyeLSIGQKRRLSVATALSSKADIIFLDEPTFG 409
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 612672732 410 LDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
5.95e-27 |
|
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: 113.71 E-value: 5.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlielpmkydelIVDPLSGVIFQD--P 79
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR---------------FLDPQSGSITLGgvD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFCMPKVYEELAFV-----------LENRQVPREDM-DALIINALNMVNLnvtpETYIKD---------------LSG 132
Cdd:COG4987 399 LRDLDEDDLRRRIAVVpqrphlfdttlRENLRLARPDAtDEELWAALERVGL----GDWLAAlpdgldtwlgeggrrLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 133 GMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNIIADEC 212
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL-ERMDRILVLE-DGRIVEQGT 552
|
250
....*....|....*.
gi 612672732 213 PEIILQK---YVHLLS 225
Cdd:COG4987 553 HEELLAQngrYRQLYQ 568
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
271-407 |
6.02e-27 |
|
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: 105.81 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTK--IKHAAKHMYLVYQNPELqFITNSVYDEI--N 345
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQL-FPRLTVRENLrlG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 346 IHFNHLSKDQSDDETIQLLKLLDLENVKDQH----PYELSIGQKRRLSVATALSSKADIIFLDEPT 407
Cdd:pfam00005 84 LLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-229 |
7.94e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 7.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlieLPMKYDE--LIVDPLS------- 72
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL-----LPDDNPNskITVDGITltaktvw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ------GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQ 146
Cdd:PRK13640 81 direkvGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 147 QSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIwNHVDRVILMDyNGNIIADECPEIILQKyVHLL 224
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEA-NMADQVLVLD-DGKLLAQGSPVEIFSK-VEML 237
|
....*
gi 612672732 225 SEYGV 229
Cdd:PRK13640 238 KEIGL 242
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-222 |
9.28e-27 |
|
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: 108.02 E-value: 9.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG-IVPN----------LIELPMKYDELIvd 69
Cdd:COG4555 1 MIEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDsgsilidgedVRKEPREARRQI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 plsGVIFQDPDSQFCMpKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSK 149
Cdd:COG4555 77 ---GVLPDERGLYDRL-TVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 150 TLFLDEPTAMLDVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQKYVH 222
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILH-KGKVVAQGSLDELREEIGE 225
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
271-455 |
1.03e-26 |
|
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: 106.95 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESI-MQLIKYQGDVYFENQRLTKIKHAA-----KHMYLVYQNPELqFITNSVYDEI 344
Cdd:TIGR02673 22 SLHIRKGEFLFLTGPSGAGKTTLLKLLyGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVVFQDFRL-LPDRTVYENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 NI--HFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLF 422
Cdd:TIGR02673 101 ALplEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLL 180
|
170 180 190
....*....|....*....|....*....|...
gi 612672732 423 QKRINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:TIGR02673 181 KRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
252-461 |
1.28e-26 |
|
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: 107.20 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIK-----HAAKHMY 325
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGLSeaelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 326 LVYQNPELqFITNSVYDeiNIHFN---H--LSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADI 400
Cdd:cd03261 81 MLFQSGAL-FDSLTVFE--NVAFPlreHtrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 401 IFLDEPTFGLD---SHNTFQLIKLFQKRINLgqSIFMVTHDDEIIERYPSRRLKISDGALLDCD 461
Cdd:cd03261 158 LLYDEPTAGLDpiaSGVIDDLIRSLKKELGL--TSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-438 |
3.24e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 111.31 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKY--PSGQRKIFDHLNITIQDKEKVLLLGPSGCGKS-TLLNVLsGIVPNLIELP---MKYD--ELIVDPLS 72
Cdd:COG4172 6 LLSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAAHPsgsILFDgqDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ----------GVIFQDPdsqfcM----P--KVYEELAFVLE-NRQVPREDMDALIINALNMVNLNvTPETYIKD----LS 131
Cdd:COG4172 85 elrrirgnriAMIFQEP-----MtslnPlhTIGKQIAEVLRlHRGLSGAAARARALELLERVGIP-DPERRLDAyphqLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 132 GGMKQKLAIVETILQQSKTLFLDEPTAMLDV--QAtedlwtKLIELWED-QT-----VVIVEHK---VKHIwnhVDRVIL 200
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVtvQA------QILDLLKDlQRelgmaLLLITHDlgvVRRF---ADRVAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 201 MdYNGNII-ADECPEIILQ---KYV-HLL-SEYGVWHPRAWEFAPS-------RVDFPTtNSHLLQFKNG--RIIRGKSt 265
Cdd:COG4172 230 M-RQGEIVeQGPTAELFAApqhPYTrKLLaAEPRGDPRPVPPDAPPlleardlKVWFPI-KRGLFRRTVGhvKAVDGVS- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 266 llsfsdLEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVYFENQRLTKIKHAA-----KHMYLVYQ------NPELq 334
Cdd:COG4172 307 ------LTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQdpfgslSPRM- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 335 fitnSVYDEI----NIHFNHLSKDQSDDETIQLLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFG 409
Cdd:COG4172 380 ----TVGQIIaeglRVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
490 500 510
....*....|....*....|....*....|..
gi 612672732 410 LDSHNTFQLIKLF---QKRINLGQsIFmVTHD 438
Cdd:COG4172 456 LDVSVQAQILDLLrdlQREHGLAY-LF-ISHD 485
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-202 |
4.07e-26 |
|
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: 104.00 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlielpmkydelivDPLSGVIFQD--P 79
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY---------------DPTSGEILIDgvD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFCMPKVYEELAFVLENRQVpredMDALIINalnmvNLnvtpetyikdLSGGMKQKLAIVETILQQSKTLFLDEPTAM 159
Cdd:cd03228 66 LRDLDLESLRKNIAYVPQDPFL----FSGTIRE-----NI----------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 160 LDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMD 202
Cdd:cd03228 127 LDPETEALILEALRALAKGKTVIVIAHRLSTI-RDADRIIVLD 168
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-218 |
4.27e-26 |
|
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: 106.05 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 4 VSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PN----LIE----LPMKYDELIVDPL-SG 73
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDsgevLIDgediSGLSEAELYRLRRrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 74 VIFQDP---DSqfcMpKVYEELAFVL-ENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSK 149
Cdd:cd03261 81 MLFQSGalfDS---L-TVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 150 TLFLDEPTAMLDVQATEDLwTKLIELWEDQ---TVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEIILQ 218
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVI-DDLIRSLKKElglTSIMVTHDLDTAFAIADRIAVL-YDGKIVAEGTPEELRA 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-229 |
5.58e-26 |
|
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: 105.90 E-value: 5.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIF---- 76
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK---------------PSSGEVLldgr 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 ------------------QDPDSQFCMpKVYEelaFVLENR-------QVPREDMDALIINALNMVNLNVTPETYIKDLS 131
Cdd:COG1120 64 dlaslsrrelarriayvpQEPPAPFGL-TVRE---LVALGRyphlglfGRPSAEDREAVEEALERTGLEHLADRPVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 132 GGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIA 209
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLK-DGRIVA 218
|
250 260
....*....|....*....|.
gi 612672732 210 DECPEIILQKyvHLLSE-YGV 229
Cdd:COG1120 219 QGPPEEVLTP--ELLEEvYGV 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
271-438 |
1.09e-25 |
|
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: 104.68 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA-----KHMYLVYQNPELqFITNSVYDei 344
Cdd:COG1127 25 SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpDSGEILVDGQDITGLSEKElyelrRRIGMLFQGGAL-FDSLTVFE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 NIHF-----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SHNTF 416
Cdd:COG1127 102 NVAFplrehTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVID 181
|
170 180
....*....|....*....|..
gi 612672732 417 QLIKLFQKRinLGQSIFMVTHD 438
Cdd:COG1127 182 ELIRELRDE--LGLTSVVVTHD 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-219 |
1.76e-25 |
|
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: 109.46 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP--------NLIELpmkyDELIVDPLSG 73
Cdd:COG4988 337 IELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPpysgsiliNGVDL----SDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 74 VIF---QDP----DSqfcmpkVYEELAFVleNRQVPREDMDAliinALNMVNL----NVTP---ETYIKD----LSGGMK 135
Cdd:COG4988 412 QIAwvpQNPylfaGT------IRENLRLG--RPDASDEELEA----ALEAAGLdefvAALPdglDTPLGEggrgLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNIIADECPEI 215
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLD-DGRIVEQGTHEE 557
|
....
gi 612672732 216 ILQK 219
Cdd:COG4988 558 LLAK 561
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
247-464 |
2.09e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.02 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 247 TNSHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQrltKIKHAAKHMY 325
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGK---PPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 326 LVYQNPEL--QF-ITnsVYD--------EINIhFNHLSKdqSDDETI-QLLKLLDLENVKDQHPYELSIGQKRRLSVATA 393
Cdd:COG1121 79 YVPQRAEVdwDFpIT--VRDvvlmgrygRRGL-FRRPSR--ADREAVdEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 394 LSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALldCDGDT 464
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPP 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-201 |
2.14e-25 |
|
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: 103.70 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 20 DHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI-VPNLIELPMKYDELIV-DPLSGVIFQDPdSQFCMPKVYEELAFVLE 97
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGKQITEpGPDRMVVFQNY-SLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 98 --NRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIEL 175
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180
....*....|....*....|....*...
gi 612672732 176 WEDQ--TVVIVEHKVKHIWNHVDRVILM 201
Cdd:TIGR01184 161 WEEHrvTVLMVTHDVDEALLLSDRVVML 188
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-463 |
2.33e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 4 VSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlielpmkydelIVDPLSGVIF------- 76
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG---------------ELEPDSGEVSipkglri 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 ----QDPDS-------QFCMP------KVYEELAFVLENRQVPREDMDAL-----IINALN-----------MVNLNVTP 123
Cdd:COG0488 64 gylpQEPPLdddltvlDTVLDgdaelrALEAELEELEAKLAEPDEDLERLaelqeEFEALGgweaearaeeiLSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 124 ETY---IKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEdlwtklielW-EDQ------TVVIVEHK------ 187
Cdd:COG0488 144 EDLdrpVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE---------WlEEFlknypgTVLVVSHDryfldr 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 188 -VKHIWnHVDRVILMDYNGN-------------IIADECpEIILQKYVHLLseygvwhprAW--EF---------APSRV 242
Cdd:COG0488 215 vATRIL-ELDRGKLTLYPGNysayleqraerleQEAAAY-AKQQKKIAKEE---------EFirRFrakarkakqAQSRI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 243 ---------DFPTTNSHL-LQFKNGRIIrGKSTL----LSFS----------DLEIGLGEWITITGANGSGKTTLLESIM 298
Cdd:COG0488 284 kaleklereEPPRRDKTVeIRFPPPERL-GKKVLelegLSKSygdktllddlSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 299 QLIK-YQGDV---------YFenqrltkikhAAKHMYLvyqNPELqfitnSVYDEInihfNHLSKDQSDDETIQLLKLLD 368
Cdd:COG0488 363 GELEpDSGTVklgetvkigYF----------DQHQEEL---DPDK-----TVLDEL----RDGAPGGTEQEVRGYLGRFL 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 369 ------LENVKDqhpyeLSIGQKRRLSVATALSSKADIIFLDEPTFGLDSH---------NTFQliklfqkrinlGqSIF 433
Cdd:COG0488 421 fsgddaFKPVGV-----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIEtlealeealDDFP-----------G-TVL 483
|
570 580 590
....*....|....*....|....*....|
gi 612672732 434 MVTHDDEIIERYPSRRLKISDGALLDCDGD 463
Cdd:COG0488 484 LVSHDRYFLDRVATRILEFEDGGVREYPGG 513
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
255-442 |
3.80e-25 |
|
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: 101.74 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 255 KNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHA--AKHMYLVyqnP 331
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKelARKIAYV---P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 332 elqfitnsvydeinihfnhlskdqsddetiQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:cd03214 80 ------------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 412 SHNTFQLIKLFQK-RINLGQSIFMVTHD--------DEII 442
Cdd:cd03214 130 IAHQIELLELLRRlARERGKTVVMVLHDlnlaaryaDRVI 169
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-208 |
4.18e-25 |
|
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: 102.97 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQR--KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-----------NLIELPMKYDELI 67
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiifdgkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 68 VDPLsGVIFQDPDSQFCmP--KVYEELAFVLENRQVPREDMDALIINALNMVNLNvTPETYIK----DLSGGMKQKLAIV 141
Cdd:cd03257 81 RKEI-QMVFQDPMSSLN-PrmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVG-LPEEVLNryphELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 142 ETILQQSKTLFLDEPTAMLDV--QA-TEDLWTKLIELwEDQTVVIVEHK---VKHIwnhVDRVILMdYNGNII 208
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVsvQAqILDLLKKLQEE-LGLTLLFITHDlgvVAKI---ADRVAVM-YAGKIV 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
253-448 |
5.52e-25 |
|
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: 102.23 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 253 QFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHaakHMYLVYQNP 331
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGKPLEKERK---RIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 332 E---------LQFITNSVYDEINiHFNHLSKDQSDDeTIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:cd03235 78 SidrdfpisvRDVVLMGLYGHKG-LFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 612672732 403 LDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSR 448
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR 201
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-158 |
7.54e-25 |
|
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: 100.03 E-value: 7.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 19 FDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP------NLIELPMKYDELIVDPLS-GVIFQDPdSQFCMPKVYEE 91
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSptegtiLLDGQDLTDDERKSLRKEiGYVFQDP-QLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 92 LAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKD----LSGGMKQKLAIVETILQQSKTLFLDEPTA 158
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-209 |
1.11e-24 |
|
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: 101.46 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 3 KVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNL---IEL----PMKYDELIvdplsGVI 75
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTsgsIRVfgkpLEKERKRI-----GYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 FQDPDSQFCMP-KVYEelaFVLENR--------QVPREDMDAlIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQ 146
Cdd:cd03235 74 PQRRSIDRDFPiSVRD---VVLMGLyghkglfrRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 147 QSKTLFLDEPTAMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVDRVILMdyNGNIIA 209
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLL--NRTVVA 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQrKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIEL-----PMKYDE---LIVDPL 71
Cdd:PRK13639 1 ILETRDLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVlikgePIKYDKkslLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 72 SGVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:PRK13639 80 VGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 152 FLDEPTAMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEII 216
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVM-SDGKIIKEGTPKEV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-186 |
2.73e-24 |
|
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: 99.86 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDP 79
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP---------------PSAGeVLWNGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFCMPKVYEELAF------------VLEN---------RQVPREDMDAliinALNMVNLNVTPETYIKDLSGGMKQKL 138
Cdd:COG4133 65 PIRDAREDYRRRLAYlghadglkpeltVRENlrfwaalygLRADREAIDE----ALEAVGLAGLADLPVRQLSAGQKRRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 612672732 139 AIVETILQQSKTLFLDEPTAMLDVQATEDLWTkLIELWEDQ--TVVIVEH 186
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAE-LIAAHLARggAVLLTTH 189
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-211 |
3.30e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 100.50 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSG--QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpMKYD--ELIVD--PLS-- 72
Cdd:COG1136 4 LLELRNLTKSYGTGegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGL--------DRPTsgEVLIDgqDISsl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -------------GVIFQDPdsqFCMPK--VYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQK 137
Cdd:COG1136 76 serelarlrrrhiGFVFQFF---NLLPEltALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 138 LAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED--QTVVIVEHKvKHIWNHVDRVILMDyNGNIIADE 211
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHD-PELAARADRVIRLR-DGRIVSDE 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-210 |
3.75e-24 |
|
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: 99.96 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGqrKIFDHLNITIQDKEKVLLlGPSGCGKSTLLNVLSGIVP---NLIEL--------PMKYDELIvdp 70
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPpssGTIRIdgqdvlkqPQKLRRRI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 lsGVIFQDPD--SQFcmpKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQS 148
Cdd:cd03264 75 --GYLPQEFGvyPNF---TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 149 KTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIAD 210
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLN-KGKLVFE 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-455 |
4.77e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 105.28 E-value: 4.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 31 KVL-LLGPSGCGKSTLLNVLSG-IVPNL--IELPMKYDElIVDPLSGVIFQD---------------PdsQFC--MPKVY 89
Cdd:PRK13409 100 KVTgILGPNGIGKTTAVKILSGeLIPNLgdYEEEPSWDE-VLKRFRGTELQNyfkklyngeikvvhkP--QYVdlIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 90 -----EELAFVLEnrqvpREDMDALIiNALNMVNLnvtPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVqa 164
Cdd:PRK13409 177 kgkvrELLKKVDE-----RGKLDEVV-ERLGLENI---LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI-- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 165 TEDLWT-KLI-ELWEDQTVVIVEHkvkhiwnhvDRVILmDYngniIADecpeiilqkYVHLL----SEYGVW-HPRAwef 237
Cdd:PRK13409 246 RQRLNVaRLIrELAEGKYVLVVEH---------DLAVL-DY----LAD---------NVHIAygepGAYGVVsKPKG--- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 238 apSRVDFpttNSHL---LQFKNGRI----IR----------GKSTLLSFSDL--------------EIGLGEWITITGAN 286
Cdd:PRK13409 300 --VRVGI---NEYLkgyLPEENMRIrpepIEfeerpprdesERETLVEYPDLtkklgdfsleveggEIYEGEVIGIVGPN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 287 GSGKTTLLESIMQLIK-YQGDVyfenqrLTKIKHAAKHMYLVYQNPElqfitnSVYDeinihFNHLSKDQSDDETIQ--L 363
Cdd:PRK13409 375 GIGKTTFAKLLAGVLKpDEGEV------DPELKISYKPQYIKPDYDG------TVED-----LLRSITDDLGSSYYKseI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 364 LKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRI-NLGQSIFMVTHDDEII 442
Cdd:PRK13409 438 IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDHDIYMI 517
|
490
....*....|...
gi 612672732 443 ErYPSRRLKISDG 455
Cdd:PRK13409 518 D-YISDRLMVFEG 529
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
267-464 |
5.84e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 5.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSDLEIGLGEWITITGANGSGKTTLLESIMQL-IKYQGDV--YFENQ------------------------RLTKIKH 319
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALlLPDTGTIewIFKDEknkkktkekekvleklviqktrfkKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 320 AAKHMYLVYQNPELQFITNSVydEINIHFNHLSKDQSDDETIQL----LKLLDL-ENVKDQHPYELSIGQKRRLSVATAL 394
Cdd:PRK13651 103 IRRRVGVVFQFAEYQLFEQTI--EKDIIFGPVSMGVSKEEAKKRaakyIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 395 SSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDcDGDT 464
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK-DGDT 249
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
261-457 |
5.88e-24 |
|
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: 99.96 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAA-----KHMYLVYQNPELq 334
Cdd:cd03258 15 GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPtSGSVLVDGTDLTLLSGKElrkarRRIGMIFQHFNL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 335 FITNSVYDeiNIHF----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGL 410
Cdd:cd03258 94 LSSRTVFE--NVALpleiAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 411 DSHNTFQLIKLFqKRIN--LGQSIFMVTHDDEIIERYPSRRLKISDGAL 457
Cdd:cd03258 172 DPETTQSILALL-RDINreLGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
7.11e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIEL-----PMKYDELIVDPLS-- 72
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKG-ININIKKGEVTAILGGNGAGKSTLFQNLNGILkPSSGRIlfdgkPIDYSRKGLMKLRes 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:PRK13636 84 vGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 152 FLDEPTAMLDVQATEDLWTKLIELWE--DQTVVIVEHKVKHIWNHVDRVILMDYNGNIIADECPEIILQKYV 221
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
271-440 |
7.45e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.16 E-value: 7.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIkhAAKHMYlVYQNPELqfitnSVYDeiNIHF- 348
Cdd:COG1116 31 SLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKpTSGEVLVDGKPVTGP--GPDRGV-VFQEPALlp-wlTVLD--NVALg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 ---NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPtFG-LDSHNTFQ----LIK 420
Cdd:COG1116 105 lelRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP-FGaLDALTRERlqdeLLR 183
|
170 180
....*....|....*....|.
gi 612672732 421 LFQKRinlGQSIFMVTHD-DE 440
Cdd:COG1116 184 LWQET---GKTVLFVTHDvDE 201
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
7.55e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.78 E-value: 7.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIF---Q 77
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP---------------PTSGTVRlfgK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 78 DP----------------DSQFCMpKVYEelaFVLENRQ--------VPREDMDAlIINALNMVNLnvtpETY----IKD 129
Cdd:COG1121 69 PPrrarrrigyvpqraevDWDFPI-TVRD---VVLMGRYgrrglfrrPSRADREA-VDEALERVGL----EDLadrpIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 130 LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLwTKLIELW--EDQTVVIVEHKVKHIWNHVDRVILMdyNGNI 207
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL-YELLRELrrEGKTILVVTHDLGAVREYFDRVLLL--NRGL 216
|
250
....*....|.
gi 612672732 208 IADECPEIILQ 218
Cdd:COG1121 217 VAHGPPEEVLT 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
271-442 |
8.11e-24 |
|
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: 98.26 E-value: 8.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQG--------DVYFENQRLTKIKhaaKHMYLVYQNPELQFITNSVYD 342
Cdd:TIGR01166 12 NFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSgavlidgePLDYSRKGLLERR---QRVGLVFQDPDDQLFAADVDQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EINihFNHLSKDQSDDETI----QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:TIGR01166 89 DVA--FGPLNLGLSEAEVErrvrEALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQM 166
|
170 180
....*....|....*....|....
gi 612672732 419 IKLFQKRINLGQSIFMVTHDDEII 442
Cdd:TIGR01166 167 LAILRRLRAEGMTVVISTHDVDLA 190
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
258-444 |
8.83e-24 |
|
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: 98.46 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 258 RIIRGKSTLLSFSdLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAAKHMYL------VYQN 330
Cdd:TIGR03608 6 KKFGDKVILDDLN-LTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFdSGQVYLNGQETPPLNSKKASKFRreklgyLFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 331 PELqfITN-SVYDEINIHFNH--LSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPT 407
Cdd:TIGR03608 85 FAL--IENeTVEENLDLGLKYkkLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 408 FGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIER 444
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ 199
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-213 |
1.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.51 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSG---QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG--------IVPNLIELPMKYDELI-VD 69
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkptsgkIIIDGVDITDKKVKLSdIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 PLSGVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVtpETYiKD-----LSGGMKQKLAIVETI 144
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDY--EDY-KDkspfeLSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 145 LQQSKTLFLDEPTAMLDVQATEDLWTKLIELWE--DQTVVIVEHKVKHIWNHVDRVILMdYNGNIIADECP 213
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVM-NKGKCELQGTP 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
271-455 |
1.17e-23 |
|
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: 97.08 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAK-HMYLVYQNPELqfitnsvYDEINIHf 348
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIKVLGKDIKKEPEEVKrRIGYLPEEPSL-------YENLTVR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 nhlskdqsddetiqllklldlENVKdqhpyeLSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINL 428
Cdd:cd03230 92 ---------------------ENLK------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE 144
|
170 180
....*....|....*....|....*..
gi 612672732 429 GQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03230 145 GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
247-438 |
2.50e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.06 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 247 TNSHLLQFKNGRIIRGKSTLLSFSDLEIGL--GEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTK--IKHAA 321
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIpkGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAITDdnFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 322 KHMYLVYQNPELQFITNSV-YDeinIHF---NHL-SKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSS 396
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVkYD---VAFgleNHAvPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 397 KADIIFLDEPTFGLDSHNTFQLIKLFQK-RINLGQSIFMVTHD 438
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKvKSEHNITIISITHD 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-210 |
2.64e-23 |
|
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: 96.35 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 3 KVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIFQD--PD 80
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK---------------PSSGEILLDgkDL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 SQFCMPKVYEELAFVLEnrqvpredmdaliinALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAML 160
Cdd:cd03214 64 ASLSPKELARKIAYVPQ---------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 612672732 161 DVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIAD 210
Cdd:cd03214 129 DIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLK-DGRIVAQ 179
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
271-440 |
3.96e-23 |
|
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: 97.16 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKikhAAKHMYLVYQNPELqFITNSVYDeiNIHF- 348
Cdd:cd03293 24 SLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGEPVTG---PGPDRGYVFQQDAL-LPWLTVLD--NVALg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 ---NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPtFG-LDSH--NTFQ--LIK 420
Cdd:cd03293 98 lelQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP-FSaLDALtrEQLQeeLLD 176
|
170 180
....*....|....*....|.
gi 612672732 421 LFQKRinlGQSIFMVTHD-DE 440
Cdd:cd03293 177 IWRET---GKTVLLVTHDiDE 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-455 |
4.06e-23 |
|
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: 102.17 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 31 KVL-LLGPSGCGKSTLLNVLSG-IVPNL--IELPMKYDElIVDPLSGVIFQDpdsqfCMPKVYE-ELAFVLENRQV---P 102
Cdd:COG1245 100 KVTgILGPNGIGKSTALKILSGeLKPNLgdYDEEPSWDE-VLKRFRGTELQD-----YFKKLANgEIKVAHKPQYVdliP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 103 ----------------REDMDAlIINALNMVNLnvtPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ--- 163
Cdd:COG1245 174 kvfkgtvrellekvdeRGKLDE-LAEKLGLENI---LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrl 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 164 ATEDLWTKLIElwEDQTVVIVEHkvkhiwnhvDRVILmDYngniIADecpeiilqkYVHLL----SEYGVW-HPRawefa 238
Cdd:COG1245 250 NVARLIRELAE--EGKYVLVVEH---------DLAIL-DY----LAD---------YVHILygepGVYGVVsKPK----- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 239 PSRVDFpttNSHL---LQFKNGRI----IR----------GKSTLLSFSDL--------------EIGLGEWITITGANG 287
Cdd:COG1245 300 SVRVGI---NQYLdgyLPEENVRIrdepIEfevhaprrekEEETLVEYPDLtksyggfsleveggEIREGEVLGIVGPNG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 288 SGKTTLLESIMQLIK-YQGDVYfenqrlTKIKHAAKHMYLVYQNPEL--QFITNSVYDEINIH-FNHlskdqsddetiQL 363
Cdd:COG1245 377 IGKTTFAKILAGVLKpDEGEVD------EDLKISYKPQYISPDYDGTveEFLRSANTDDFGSSyYKT-----------EI 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 364 LKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRI-NLGQSIFMVTHDDEII 442
Cdd:COG1245 440 IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHDIYLI 519
|
490
....*....|...
gi 612672732 443 ErYPSRRLKISDG 455
Cdd:COG1245 520 D-YISDRLMVFEG 531
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
272-455 |
5.54e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLT----KIKHAAKHMYLVYQNPELQFITNSVYDEI-- 344
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQYPEYQLFEETIEKDIaf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 ---NIHfnhLSKDQSDDETIQLLKL--LDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SHNTF 416
Cdd:PRK13637 108 gpiNLG---LSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgRDEIL 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 612672732 417 QLIKLFQKRINLgqSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:PRK13637 185 NKIKELHKEYNM--TIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-188 |
6.00e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.46 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSgqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP---NLIELpmkyDELIVDPLS---GV 74
Cdd:PRK11248 1 MLQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhGSITL----DGKPVEGPGaerGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 75 IFQDpDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLD 154
Cdd:PRK11248 75 VFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 612672732 155 EPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKV 188
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDI 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-442 |
6.82e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.32 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSG--QRKIFDHLNITIQDKEKVLLLGPSGCGKS-TLLNVLSGIVPNLIELP-----------MKYDEL 66
Cdd:PRK15134 5 LLAIENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVVYPsgdirfhgeslLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 67 IVDPLSG----VIFQDP-DSQFCMPKVYEELAFVLE-NRQVPREDMDALIINALNMVNLNvTPETYIKD----LSGGMKQ 136
Cdd:PRK15134 85 TLRGVRGnkiaMIFQEPmVSLNPLHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIR-QAAKRLTDyphqLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 137 KLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWE--DQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPE 214
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQ-NGRCVEQNRAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 215 IILQKYVH------LLSE-YGVWHPRAWEFAPS------RVDFPTTNShLLQfkngRIIRGKSTL--LSFSdleIGLGEW 279
Cdd:PRK15134 243 TLFSAPTHpytqklLNSEpSGDPVPLPEPASPLldveqlQVAFPIRKG-ILK----RTVDHNVVVknISFT---LRPGET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 280 ITITGANGSGKTTLLESIMQLIKYQGDVYFENQRLTKIKHAA-----KHMYLVYQNPE---------LQFITNSvydeIN 345
Cdd:PRK15134 315 LGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQDPNsslnprlnvLQIIEEG----LR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHFNHLSKDQSDDETIQLLKLLDLE-NVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDshNTFQ-----LI 419
Cdd:PRK15134 391 VHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD--KTVQaqilaLL 468
|
490 500
....*....|....*....|...
gi 612672732 420 KLFQKRINLGQsIFmVTHDDEII 442
Cdd:PRK15134 469 KSLQQKHQLAY-LF-ISHDLHVV 489
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-188 |
6.82e-23 |
|
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: 95.57 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 11 YPSGQRkIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PN--LIEL---PMKYDE---LIVDPLSGVIFQDPDS 81
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLrPQsgAVLIdgePLDYSRkglLERRQRVGLVFQDPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLD 161
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*...
gi 612672732 162 VQATEDLWTKLIELWED-QTVVIVEHKV 188
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEgMTVVISTHDV 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
241-438 |
7.00e-23 |
|
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: 98.59 E-value: 7.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 241 RVDFPTTNSHLlqfkngRIIRGkstlLSFSdleIGLGEWITITGANGSGKTTLLESIMQLIKYQ----GDVYFENQRLTK 316
Cdd:COG0444 8 KVYFPTRRGVV------KAVDG----VSFD---VRRGETLGLVGESGSGKSTLARAILGLLPPPgitsGEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 317 IKHAA------KHMYLVYQNPE-----LQFITNSVYDEINIHfNHLSKDQSDDETIQLLKLLDL---ENVKDQHPYELSI 382
Cdd:COG0444 75 LSEKElrkirgREIQMIFQDPMtslnpVMTVGDQIAEPLRIH-GGLSKAEARERAIELLERVGLpdpERRLDRYPHELSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 383 GQKRRLSVATALSSKADIIFLDEPTFGLDShnTFQ-----LIKLFQKRINLgqSIFMVTHD 438
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDV--TIQaqilnLLKDLQRELGL--AILFITHD 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
262-438 |
1.06e-22 |
|
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: 95.78 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAAKHMYLVYQNPELqFITNSV 340
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTDLPPKDRDIAMVFQNYAL-YPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 341 YDeiNIHFN----HLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTF 416
Cdd:cd03301 90 YD--NIAFGlklrKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRV 167
|
170 180
....*....|....*....|....*
gi 612672732 417 QL---IKLFQKRinLGQSIFMVTHD 438
Cdd:cd03301 168 QMraeLKRLQQR--LGTTTIYVTHD 190
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-211 |
1.71e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.50 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlIELP--------------MKYDEL 66
Cdd:COG2884 1 MIRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG-----EERPtsgqvlvngqdlsrLKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 67 ------IvdplsGVIFQD----PDsqfcMPkVYEELAFVLENRQVPREDMDALIINALNMVNL----NVTPETyikdLSG 132
Cdd:COG2884 75 pylrrrI-----GVVFQDfrllPD----RT-VYENVALPLRVTGKSRKEIRRRVREVLDLVGLsdkaKALPHE----LSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 133 GMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ-TVVIVEHkVKHIWNHVD-RVILMDyNGNIIAD 210
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGtTVLIATH-DLELVDRMPkRVLELE-DGRLVRD 218
|
.
gi 612672732 211 E 211
Cdd:COG2884 219 E 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-207 |
3.26e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 94.11 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQD-P 79
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP---------------PTSGeIYLDGkP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFCMPK------------------VYEELAFVLENRQvPREDMDALIiNALNMVNLnvtPETY----IKDLSGGMKQK 137
Cdd:COG4619 64 LSAMPPPEwrrqvayvpqepalwggtVRDNLPFPFQLRE-RKFDRERAL-ELLERLGL---PPDIldkpVERLSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 138 LAIVETILQQSKTLFLDEPTAMLDvQATEDLWTKLIELW---EDQTVVIVEHKVKHIWNHVDRVILMDyNGNI 207
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALD-PENTRRVEELLREYlaeEGRAVLWVSHDPEQIERVADRVLTLE-AGRL 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-202 |
3.41e-22 |
|
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: 93.41 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP---NLIEL---PMKYDELIVDPL---S 72
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpdsGSILIdgeDLTDLEDELPPLrrrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 GVIFQDPdsqfcmpKVYEELAfVLENRQVPredmdaliinalnmvnlnvtpetyikdLSGGMKQKLAIVETILQQSKTLF 152
Cdd:cd03229 79 GMVFQDF-------ALFPHLT-VLENIALG---------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 612672732 153 LDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMD 202
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
3.58e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 93.15 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlielpmkydelivDPLSGVIFQDPDS 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL---------------KPQQGEITLDGVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFCMPKVYEELAFVLENRqvpredmdALIINALNMVNLNvtpetyiKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLD 161
Cdd:cd03247 66 VSDLEKALSSLISVLNQR--------PYLFDTTLRNNLG-------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 162 VQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNIIAD 210
Cdd:cd03247 131 PITERQLLSLIFEVLKDKTLIWITHHLTGI-EHMDKILFLE-NGKIIMQ 177
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
277-441 |
4.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTK-----IKHaakHMYLVYQNPELQFITNSVYDEINIHFNH 350
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEenvwdIRH---KIGMVFQNPDNQFVGATVEDDVAFGLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 351 --LSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQK-RIN 427
Cdd:PRK13650 110 kgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGiRDD 189
|
170
....*....|....*
gi 612672732 428 LGQSIFMVTHD-DEI 441
Cdd:PRK13650 190 YQMTVISITHDlDEV 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
272-457 |
6.32e-22 |
|
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: 93.63 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA-----KHMYLVYQNPELqFITNSVYDeiN 345
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDLRGRAipylrRKIGVVFQDFRL-LPDRNVYE--N 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHFNHLSKDQSDDE----TIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKL 421
Cdd:cd03292 99 VAFALEVTGVPPREirkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNL 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 612672732 422 FQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGAL 457
Cdd:cd03292 179 LKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
271-466 |
7.97e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLT------KIKHAAKHMYLVYQNPELQFITNSVYDE 343
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQFPESQLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INIHFNH--LSKDQSDDETIQLLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIK 420
Cdd:PRK13643 106 VAFGPQNfgIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 612672732 421 LFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDCDGDTNV 466
Cdd:PRK13643 186 LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
271-445 |
1.24e-21 |
|
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: 93.27 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIK-HAAKHMYLV--YQNPELqFITNSVYDEI-- 344
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRpTSGSVLFDGEDITGLPpHEIARLGIGrtFQIPRL-FPELTVLENVmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 --------NIHFNHLSKDQSD--DETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHN 414
Cdd:cd03219 99 aaqartgsGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEE 178
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 415 TFQLIKLFQKRINLGQSIFMVTHDDEIIERY 445
Cdd:cd03219 179 TEELAELIRELRERGITVLLVEHDMDVVMSL 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
271-460 |
1.29e-21 |
|
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: 92.95 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYF-ENQRLTKIKHAAKHMYLVYQN----PELqfitnSVYDEI 344
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTsGTAYInGYSIRTDRKAARQSLGYCPQFdalfDEL-----TVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 NIH--FNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS---HNTFQLI 419
Cdd:cd03263 97 RFYarLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPasrRAIWDLI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 420 KLFQKrinlGQSIFMVTHDDEIIERYPSRRLKISDGALLDC 460
Cdd:cd03263 177 LEVRK----GRSIILTTHSMDEAEALCDRIAIMSDGKLRCI 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-459 |
1.40e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.18 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG----------IVPNL--------IELPMKY 63
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgrIIYHValcekcgyVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 64 DELIvdPLSGVIFQDPDSQFCMP------KVYEELAFVLENRQVPREDMDAL--IINALN------------------MV 117
Cdd:TIGR03269 79 GEPC--PVCGGTLEPEEVDFWNLsdklrrRIRKRIAIMLQRTFALYGDDTVLdnVLEALEeigyegkeavgravdlieMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 118 NLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELW--EDQTVVIVEHKVKHIWNHV 195
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 196 DRVILMDyNGNIIADECPEIILQKYVHLLSEYgvwhPRAWEFapsRVDFPTTNSHLLQFKNGRIIRGKSTLLSFSDLEIG 275
Cdd:TIGR03269 237 DKAIWLE-NGEIKEEGTPDEVVAVFMEGVSEV----EKECEV---EVGEPIIKVRNVSKRYISVDRGVVKAVDNVSLEVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 276 LGEWITITGANGSGKTTLLESIMQLIK-YQGDVYF----ENQRLTKIK-----HAAKHMYLVYQNPEL---QFITNSVYD 342
Cdd:TIGR03269 309 EGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVrvgdEWVDMTKPGpdgrgRAKRYIGILHQEYDLyphRTVLDNLTE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EINIhfnHLSKDQSDDETIQLLKLLDL-----ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQ 417
Cdd:TIGR03269 389 AIGL---ELPDELARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVD 465
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 612672732 418 LIK-LFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLD 459
Cdd:TIGR03269 466 VTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-207 |
2.00e-21 |
|
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: 92.69 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnliELPMKYDELI----VDPL------SGVIFQDPdSQF 83
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-----ETPTSGEILLdgkdITNLpphkrpVNTVFQNY-ALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 84 CMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ 163
Cdd:cd03300 85 PHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 164 ATEDLwtkLIELWEDQ-----TVVIVEHKVKHIWNHVDRVILMDyNGNI 207
Cdd:cd03300 165 LRKDM---QLELKRLQkelgiTFVFVTHDQEEALTMSDRIAVMN-KGKI 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-217 |
2.60e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.51 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIfDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielPMKYDELI------------- 67
Cdd:PRK13644 1 MIRLENVSYSYPDGTPAL-ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR-----PQKGKVLVsgidtgdfsklqg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 68 VDPLSGVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQ 147
Cdd:PRK13644 75 IRKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 148 SKTLFLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIwNHVDRVILMDyNGNIIADECPEIIL 217
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEEL-HDADRIIVMD-RGKIVLEGEPENVL 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
249-455 |
3.06e-21 |
|
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: 92.45 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 249 SHLLQFKNGRIIRGKSTLLSFSDLEIGLGE-WItITGANGSGKTTLLesimQLI------KYQGDVY-FENQR----LTK 316
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEhWA-ILGPNGAGKSTLL----SLItgdlppTYGNDVRlFGERRggedVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 317 IKhaaKHMYLVyqNPELQ-FITNSV----------YDEINIhFNHLSKDQsDDETIQLLKLLDLENVKDQHPYELSIGQK 385
Cdd:COG1119 76 LR---KRIGLV--SPALQlRFPRDEtvldvvlsgfFDSIGL-YREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 386 RRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQ-SIFMVTHD-DEIIERYpSRRLKISDG 455
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHvEEIPPGI-THVLLLKDG 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
271-440 |
3.67e-21 |
|
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: 91.91 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHMYLVYQNPELqFITNSVYDeiNIHF- 348
Cdd:cd03300 20 SLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETpTSGEILLDGKDITNLPPHKRPVNTVFQNYAL-FPHLTVFE--NIAFg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 ---NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDshntFQLIKLFQ-- 423
Cdd:cd03300 97 lrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD----LKLRKDMQle 172
|
170 180
....*....|....*....|
gi 612672732 424 -KRI--NLGQSIFMVTHDDE 440
Cdd:cd03300 173 lKRLqkELGITFVFVTHDQE 192
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
271-439 |
4.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTllesIMQL-----IKYQGDVYFENQRLT------KIKHAAKHMYLVYQNPELQFITNS 339
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKST----IMQLlnglhVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 340 VYDEINIHFNHLSKDQSDDETIQLLKLLDL---ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTF 416
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAREKLALVgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180
....*....|....*....|....*
gi 612672732 417 QLIKLFQKRINLGQSIFMVTH--DD 439
Cdd:PRK13649 183 ELMTLFKKLHQSGMTIVLVTHlmDD 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-210 |
4.12e-21 |
|
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: 92.17 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSG--QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNlielpmkyD--ELIVD--PLSG- 73
Cdd:COG1124 1 MLEVRNLSVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP--------WsgEVTFDgrPVTRr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 74 ----------VIFQDPDSQFcMPK--VYEELAFVLENRQVPreDMDALIINALNMVNLnvTPET---YIKDLSGGMKQKL 138
Cdd:COG1124 73 rrkafrrrvqMVFQDPYASL-HPRhtVDRILAEPLRIHGLP--DREERIAELLEQVGL--PPSFldrYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 139 AIVETILQQSKTLFLDEPTAMLD--VQA-TEDLWTKLIELwEDQTVVIVEH---KVKHIwnhVDRVILMDyNGNIIAD 210
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDvsVQAeILNLLKDLREE-RGLTYLFVSHdlaVVAHL---CDRVAVMQ-NGRIVEE 220
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
263-457 |
5.54e-21 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 90.93 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 263 KSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAAK----HMYLVYQNPELQFIT 337
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLdSGSLTLAGKEVTNLSYSQKiilrRELIGYIFQSFNLIP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 338 N-SVYDEINI--HFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHN 414
Cdd:NF038007 97 HlSIFDNVALplKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 612672732 415 TFQLIKLFqKRIN-LGQSIFMVTHDDEiIERYPSRRLKISDGAL 457
Cdd:NF038007 177 ARAVLQQL-KYINqKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-238 |
5.80e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKY----PSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpNLIELPMKYDELIVDPLS---- 72
Cdd:PRK13643 1 MIKFEKVNYTYqpnsPFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL-QPTEGKVTVGDIVVSSTSkqke 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 --------GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvTPETYIK---DLSGGMKQKLAIV 141
Cdd:PRK13643 79 ikpvrkkvGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKspfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 142 ETILQQSKTLFLDEPTAMLDVQATedlwTKLIELWED-----QTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEII 216
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKAR----IEMMQLFESihqsgQTVVLVTHLMDDVADYADYVYLLE-KGHIISCGTPSDV 231
|
250 260
....*....|....*....|..
gi 612672732 217 LQKyVHLLSEYGVWHPRAWEFA 238
Cdd:PRK13643 232 FQE-VDFLKAHELGVPKATHFA 252
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
253-444 |
6.90e-21 |
|
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: 91.46 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 253 QFKNGRIIRGKStllsfsdLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTK-IKHAAKHMYLVYQN 330
Cdd:COG4555 10 KYGKVPALKDVS-------FTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpDSGSILIDGEDVRKePREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 331 PELqFITNSVYDEINIH--FNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTF 408
Cdd:COG4555 83 RGL-YDRLTVRENIRYFaeLYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 612672732 409 GLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIER 444
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEA 197
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-210 |
8.19e-21 |
|
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: 90.73 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpmkYDelivdPLSGVIFQD--P 79
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL----------YK-----PTSGSVLLDgtD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFCMPKVYEELAFVLENRQV----PREDM--------DALIINALNMVNLNvtpeTYIKD---------------LSG 132
Cdd:cd03245 68 IRQLDPADLRRNIGYVPQDVTLfygtLRDNItlgapladDERILRAAELAGVT----DFVNKhpngldlqigergrgLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 133 GMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKhIWNHVDRVILMDyNGNIIAD 210
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS-LLDLVDRIIVMD-SGRIVAD 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
271-443 |
8.81e-21 |
|
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: 91.72 E-value: 8.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFEN------QRLTKIKhaaKHMYLVYQNPELQFITNSVYDE 343
Cdd:TIGR04520 22 SLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTsGKVTVDGldtldeENLWEIR---KKVGMVFQNPDNQFVGATVEDD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 I-----NIHFNHlskdqsdDETIQ----LLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHN 414
Cdd:TIGR04520 99 VafgleNLGVPR-------EEMRKrvdeALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG 171
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 415 TFQLIKLFQK-RINLGQSIFMVTHD-DEIIE 443
Cdd:TIGR04520 172 RKEVLETIRKlNKEEGITVISITHDmEEAVL 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
266-458 |
9.98e-21 |
|
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: 90.05 E-value: 9.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 266 LLSFSdLEIGL---GEWITITGANGSGKTTLLESIMQL-------IKYQGDVYFENQRLTKIKHAAKHMYLVYQNPELqF 335
Cdd:cd03297 10 LPDFT-LKIDFdlnEEVTGIFGASGAGKSTLLRCIAGLekpdggtIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYAL-F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 336 ITNSVYDEINIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 612672732 416 FQLIKLFQKRI-NLGQSIFMVTHDDEIIERYPSRRLKISDGALL 458
Cdd:cd03297 168 LQLLPELKQIKkNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
271-459 |
1.00e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTK------IKHAAKHMYLVYQNPELQFITNSVYDE 343
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQFPESQLFEDTVERE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INI---HFNhLSKDQSDDETIQLLKLLDLE-NVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLI 419
Cdd:PRK13646 107 IIFgpkNFK-MNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVM 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 420 KLFQK-RINLGQSIFMVTHDDEIIERYPSRRLKISDGALLD 459
Cdd:PRK13646 186 RLLKSlQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-238 |
1.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.69 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKY---PSGQRKI-FDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlieLPMKyDELIVDPLS---- 72
Cdd:PRK13633 4 MIKCKNVSYKYesnEESTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL-----IPSE-GKVYVDGLDtsde 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ----------GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVE 142
Cdd:PRK13633 78 enlwdirnkaGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 143 TILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNhVDRVILMDyNGNIIADECPEIILQKy 220
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMD-SGKVVMEGTPKEIFKE- 234
|
250
....*....|....*...
gi 612672732 221 VHLLSEYGVWHPRAWEFA 238
Cdd:PRK13633 235 VEMMKKIGLDVPQVTELA 252
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-186 |
1.79e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.44 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlIELP----MKYDELIVDPLS---- 72
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-----LEDPtsgeILIGGRDVTDLPpkdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 --GVIFQDPD-----SqfcmpkVYEELAFVLENRQVPREDMDALIINALNMVN----LNVTPetyiKDLSGGMKQKLAIV 141
Cdd:COG3839 76 niAMVFQSYAlyphmT------VYENIAFPLKLRKVPKAEIDRRVREAAELLGledlLDRKP----KQLSGGQRQRVALG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 612672732 142 ETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED--QTVVIVEH 186
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlgTTTIYVTH 192
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
261-452 |
1.82e-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: 89.09 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLI-KYQGDVYFENQRLTKIK--HAAKHMYLVYQNPelqfIT 337
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGPLDFQRdsIARGLLYLGHAPG----IK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 338 NSVYDEINIHFNHlsKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQ 417
Cdd:cd03231 86 TTLSVLENLRFWH--ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 612672732 418 LIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKI 452
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
267-466 |
2.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFsdlEIGLGEWITITGANGSGKTTLLESIMQLIK----------YQGDVYFENQRLTKIKhaaKHMYLVYQNPELQFI 336
Cdd:PRK13641 26 ISF---ELEEGSFVALVGHTGSGKSTLMQHFNALLKpssgtitiagYHITPETGNKNLKKLR---KKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 337 TNSVYDEI-----NIHFnhlSKDQSDDETIQLLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGL 410
Cdd:PRK13641 100 ENTVLKDVefgpkNFGF---SEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 411 DSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDCDGDTNV 466
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-161 |
2.23e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.08 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLIELP--MKYDELIVDPLS------ 72
Cdd:COG4136 1 MLSLENLTITL--GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASgeVLLNGRRLTALPaeqrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 GVIFQDpDSQFCMPKVYEELAFVLENRqVPREDMDALIINALNMVNL----NVTPETyikdLSGGMKQKLAIVETILQQS 148
Cdd:COG4136 79 GILFQD-DLLFPHLSVGENLAFALPPT-IGRAQRRARVEQALEEAGLagfaDRDPAT----LSGGQRARVALLRALLAEP 152
|
170
....*....|...
gi 612672732 149 KTLFLDEPTAMLD 161
Cdd:COG4136 153 RALLLDEPFSKLD 165
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-217 |
2.36e-20 |
|
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: 89.80 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDPD 80
Cdd:cd03219 1 LEVRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR---------------PTSGsVLFDGED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 SQ---------------FCMPKVYEELAfVLENRQV-----------------PREDMDALIINALNMVNL----NVTPE 124
Cdd:cd03219 64 ITglppheiarlgigrtFQIPRLFPELT-VLENVMVaaqartgsglllararrEEREARERAEELLERVGLadlaDRPAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 125 TyikdLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWE-DQTVVIVEHKVKHIWNHVDRVILMDY 203
Cdd:cd03219 143 E----LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
250
....*....|....
gi 612672732 204 nGNIIADECPEIIL 217
Cdd:cd03219 219 -GRVIAEGTPDEVR 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
271-411 |
2.82e-20 |
|
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: 88.74 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAA----KHMYLVYQN----PELQFITNSVY 341
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKLTDDKKNInelrQKVGMVFQQfnlfPHLTVLENITL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DEINIHfnHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:cd03262 100 APIKVK--GMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
271-444 |
2.94e-20 |
|
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: 93.75 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA--KHMYLVYQNPELqfITNSVYDeiNIH 347
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFL--FSGTIRE--NIT 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 348 FNHlsKDQSDDETIQLLKLLDLENVKDQHP--YE---------LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTF 416
Cdd:COG2274 571 LGD--PDATDEEIIEAARLAGLHDFIEALPmgYDtvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
170 180
....*....|....*....|....*...
gi 612672732 417 QLIKLFQKRINlGQSIFMVTHDDEIIER 444
Cdd:COG2274 649 IILENLRRLLK-GRTVIIIAHRLSTIRL 675
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-208 |
3.93e-20 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 89.32 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnliELPMKYDELI-------VDPLS-- 72
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-----ERPDSGTILFggedatdVPVQErn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQDPdSQFCMPKVYEELAFVLENRQV----PREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQ 147
Cdd:cd03296 76 vGFVFQHY-ALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 148 SKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNII 208
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEVADRVVVMN-KGRIE 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
271-457 |
5.02e-20 |
|
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: 92.91 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAA--KHMYLVYQNPELqFITnSVYDeiNIH 347
Cdd:COG4987 355 SLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSITLGGVDLRDLDEDDlrRRIAVVPQRPHL-FDT-TLRE--NLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 348 fnhLSKDQ-SDDETIQLLKLLDLENVKDQHPY-------E----LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:COG4987 431 ---LARPDaTDEELWAALERVGLGDWLAALPDgldtwlgEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE 507
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 612672732 416 FQLIKLFQKRINlGQSIFMVTHDDEIIERYpSRRLKISDGAL 457
Cdd:COG4987 508 QALLADLLEALA-GRTVLLITHRLAGLERM-DRILVLEDGRI 547
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
271-444 |
5.45e-20 |
|
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: 87.05 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA--KHMYLVYQNPELqfitnsvydeinih 347
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDpTSGEILIDGVDLRDLDLESlrKNIAYVPQDPFL-------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 348 FNhlskdqsddETIqllklldLENVkdqhpyeLSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRIN 427
Cdd:cd03228 88 FS---------GTI-------RENI-------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK 144
|
170
....*....|....*..
gi 612672732 428 lGQSIFMVTHDDEIIER 444
Cdd:cd03228 145 -GKTVIVIAHRLSTIRD 160
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
252-455 |
6.62e-20 |
|
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: 86.86 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTK----IKHAAKHMYL 326
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLTDledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 327 VYQNPELqfitnsvydeinihFNHLSKdqsddetiqllklldLENVKdqhpYELSIGQKRRLSVATALSSKADIIFLDEP 406
Cdd:cd03229 81 VFQDFAL--------------FPHLTV---------------LENIA----LGLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 612672732 407 TFGLDSHNTFQLIKLFQK-RINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03229 128 TSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-411 |
1.08e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 34 LLGPSGCGKSTLLNVLSGIVPnlielpmkYD--ELIVDplsG--VIFQDP-DSQ-----FcmpkVYEELAF-----VLEN 98
Cdd:COG1129 35 LLGENGAGKSTLMKILSGVYQ--------PDsgEILLD---GepVRFRSPrDAQaagiaI----IHQELNLvpnlsVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 99 RQVPREDMDALIIN----------ALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDL 168
Cdd:COG1129 100 IFLGREPRRGGLIDwramrrrareLLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 169 WtKLIELWEDQ--TVVIVEHKVKHIWNHVDRV-ILMDynGNIIAD-ECPEIILQKYVHL-----LSEygvwhprawEFAP 239
Cdd:COG1129 180 F-RIIRRLKAQgvAIIYISHRLDEVFEIADRVtVLRD--GRLVGTgPVAELTEDELVRLmvgreLED---------LFPK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 240 SRVDFPTTnshLLQFKN---GRIIRGkstlLSFsDL---EIgLGewitITGANGSGKTTLLESIMQLIK-YQGDVYFENQ 312
Cdd:COG1129 248 RAAAPGEV---VLEVEGlsvGGVVRD----VSF-SVragEI-LG----IAGLVGAGRTELARALFGADPaDSGEIRLDGK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 313 --RLTKIKHAAKH-MYLVyqnPE------LqFITNSVYDEINI-------HFNHLSKDQSDDETIQLLKLLdleNVK--- 373
Cdd:COG1129 315 pvRIRSPRDAIRAgIAYV---PEdrkgegL-VLDLSIRENITLasldrlsRGGLLDRRRERALAEEYIKRL---RIKtps 387
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 612672732 374 -DQHPYELSIG--QKrrLSVATALSSKADIIFLDEPTFGLD 411
Cdd:COG1129 388 pEQPVGNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGID 426
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
273-459 |
1.17e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 273 EIGLGEWITITGANGSGKTTLLESIMQL-IKYQGDVYFENQRLTKIKHAAKHMYlvyQNPELQFItnsvydeinIHFNHL 351
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAKAEL---RNQKLGFI---------YQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 352 SKD-------------------QSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:PRK11629 99 LPDftalenvamplligkkkpaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 612672732 413 HNT---FQLIKLFQKRinLGQSIFMVTHDDEIIERYpSRRLKISDGALLD 459
Cdd:PRK11629 179 RNAdsiFQLLGELNRL--QGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-208 |
1.24e-19 |
|
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: 89.34 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIF--DHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP--------------NLIELPMKyd 64
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgitsgeilfdgeDLLKLSEK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 65 EL-------IvdplsGVIFQDPDSQF--CMpKVYEELAFVLE-NRQVPREDMDALIINALNMVNLNvTPETYIKD----L 130
Cdd:COG0444 79 ELrkirgreI-----QMIFQDPMTSLnpVM-TVGDQIAEPLRiHGGLSKAEARERAIELLERVGLP-DPERRLDRypheL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 131 SGGMKQKLAIVETILQQSKTLFLDEPTAMLDV--QA-TEDLwtkLIELWEDQ--TVVIVEHK---VKHIwnhVDRVILMd 202
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVtiQAqILNL---LKDLQRELglAILFITHDlgvVAEI---ADRVAVM- 224
|
....*.
gi 612672732 203 YNGNII 208
Cdd:COG0444 225 YAGRIV 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-208 |
1.38e-19 |
|
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: 86.54 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 4 VSDLRLKYPsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI---VPNLIEL---PMKYDELIvdPLSGVIFQ 77
Cdd:cd03226 2 IENISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLikeSSGSILLngkPIKAKERR--KSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 78 DPDSQFCMPKVYEELAFVLENRQVPREDMDALiinaLNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPT 157
Cdd:cd03226 79 DVDYQLFTDSVREELLLGLKELDAGNEQAETV----LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 612672732 158 AMLDVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRVILMDyNGNII 208
Cdd:cd03226 155 SGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVCDRVLLLA-NGAIV 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
1.43e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.32 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIELPMKYDELI------VDPLSG 73
Cdd:PRK13652 3 LIETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILkPTSGSVLIRGEPITkenireVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 74 VIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFL 153
Cdd:PRK13652 82 LVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 154 DEPTAMLDVQATEDLWTKLIELWED--QTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECP-EIILQ 218
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMD-KGRIVAYGTVeEIFLQ 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
255-439 |
1.60e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 255 KNGRIIRGKSTLlsFSDLEIGL--GEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHMYLVYQN- 330
Cdd:PRK13539 6 EDLACVRGGRVL--FSGLSFTLaaGEALVLTGPNGSGKTTLLRLIAGLLPpAAGTIKLDGGDIDDPDVAEACHYLGHRNa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 331 --PELqfitnSVYDeiNIHF--NHLSKDQSD-DETIQLLKLLDLENVkdqhPY-ELSIGQKRRLSVATALSSKADIIFLD 404
Cdd:PRK13539 84 mkPAL-----TVAE--NLEFwaAFLGGEELDiAAALEAVGLAPLAHL----PFgYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 612672732 405 EPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDD 439
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
12-243 |
1.62e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.26 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 12 PSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI-VPNliELPMKYDELIVDPLS------------GVIFQD 78
Cdd:PRK13649 17 PFEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPT--QGSVRVDDTLITSTSknkdikqirkkvGLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 PDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNlnVTPETYIK---DLSGGMKQKLAIVETILQQSKTLFLDE 155
Cdd:PRK13649 94 PESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVG--ISESLFEKnpfELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 156 PTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQKyVHLLSEYGVWHPRA 234
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLE-KGKLVLSGKPKDIFQD-VDFLEEKQLGVPKI 249
|
....*....
gi 612672732 235 WEFAPSRVD 243
Cdd:PRK13649 250 TKFAQRLAD 258
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-218 |
1.63e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLL---NVLSGIVPNlielpmkydELIVDPLS---------------GVI 75
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSG---------DLIVDGLKvndpkvderlirqeaGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 FQdpdsQFCM-PKV--YEELAF-VLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:PRK09493 83 FQ----QFYLfPHLtaLENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 152 FLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQ 218
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFID-KGRIAEDGDPQVLIK 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-186 |
1.87e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.78 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI---VPNL-----IELpmkYDELI----VD 69
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlIPGArvegeILL---DGEDIydpdVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 PLS-----GVIFQDPDSqFcmPK-VYEELAFVLE-NRQVPREDMDALIINALNMVNL--NVtpetyiKD--------LSG 132
Cdd:COG1117 87 VVElrrrvGMVFQKPNP-F--PKsIYDNVAYGLRlHGIKSKSELDEIVEESLRKAALwdEV------KDrlkksalgLSG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 133 GMKQKLAIVETILQQSKTLFLDEPTAMLDVQAT---EDLwtkLIELWEDQTVVIVEH 186
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTakiEEL---ILELKKDYTIVIVTH 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-207 |
2.07e-19 |
|
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: 86.54 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnliELPMKYDELI-------VDPLS---GVIFQD----P 79
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-----EEPTSGRIYIggrdvtdLPPKDrdiAMVFQNyalyP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DsqfcMpKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAM 159
Cdd:cd03301 86 H----M-TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 612672732 160 LDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNI 207
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLgtTTIYVTHDQVEAMTMADRIAVMN-DGQI 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
2.84e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.48 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIfDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnliELPMK------------YDELIVD 69
Cdd:PRK13647 5 IEVEDLHFRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI-----YLPQRgrvkvmgrevnaENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 PLSGVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSK 149
Cdd:PRK13647 79 SKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 150 TLFLDEPTAMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQKyvHLLSEYG 228
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLK-EGRVLAEGDKSLLTDE--DIVEQAG 235
|
....
gi 612672732 229 VWHP 232
Cdd:PRK13647 236 LRLP 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-214 |
2.94e-19 |
|
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: 86.27 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 4 VSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlieLPMKYDELIVDPLS----------- 72
Cdd:cd03265 3 VENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL------LKPTSGRATVAGHDvvreprevrrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQDP--DSQFcmpKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSK 149
Cdd:cd03265 75 iGIVFQDLsvDDEL---TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 150 TLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPE 214
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIID-HGRIIAEGTPE 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
261-442 |
3.05e-19 |
|
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: 86.59 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA--KHMYLVYQNPELqFIT 337
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDIREQDPVElrRKIGYVIQQIGL-FPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 338 NSVYDEINI--HFNHLSKDQSDDETIQLLKLLDLE--NVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPtFG-LDS 412
Cdd:cd03295 90 MTVEENIALvpKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP-FGaLDP 168
|
170 180 190
....*....|....*....|....*....|...
gi 612672732 413 HNTFQLIKLFqKRIN--LGQSIFMVTHD-DEII 442
Cdd:cd03295 169 ITRDQLQEEF-KRLQqeLGKTIVFVTHDiDEAF 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
10-238 |
4.98e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.00 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 10 KYPSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PN---------LIELPMKYDELivDPLS---GVIF 76
Cdd:PRK13634 15 KTPFERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTsgtvtigerVITAGKKNKKL--KPLRkkvGIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 QDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtPETYIK----DLSGGMKQKLAIVETILQQSKTLF 152
Cdd:PRK13634 92 QFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGL---PEELLArspfELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 153 LDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQKyVHLLSEYGVW 230
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYADQIVVMH-KGTVFLQGTPREIFAD-PDELEAIGLD 246
|
....*...
gi 612672732 231 HPRAWEFA 238
Cdd:PRK13634 247 LPETVKFK 254
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
252-440 |
5.45e-19 |
|
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: 85.85 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAAKHMYLVYQN 330
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 331 PELqFITNSVYDeiNIHF--------NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:cd03296 83 YAL-FRHMTVFD--NVAFglrvkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 403 LDEPTFGLDSHNTFQL---IKLFQKRINLgQSIFmVTHDDE 440
Cdd:cd03296 160 LDEPFGALDAKVRKELrrwLRRLHDELHV-TTVF-VTHDQE 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-213 |
5.82e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQrkIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIEL-----PMKYDE---LIVDPL 71
Cdd:PRK13638 1 MLATSDLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVlwqgkPLDYSKrglLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 72 SGVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:PRK13638 79 VATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 152 FLDEPTAMLDVQATedlwTKLIEL-----WEDQTVVIVEHKVKHIWNHVDRVILMdYNGNIIADECP 213
Cdd:PRK13638 159 LLDEPTAGLDPAGR----TQMIAIirrivAQGNHVIISSHDIDLIYEISDAVYVL-RQGQILTHGAP 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
271-455 |
7.88e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRL----TKIKHAAKHMYLVYQNPELQFITNSVYDEIN 345
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKPIdysrKGLMKLRESVGMVFQDPDNQLFSASVYQDVS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHFNH--LSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQ 423
Cdd:PRK13636 106 FGAVNlkLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLV 185
|
170 180 190
....*....|....*....|....*....|...
gi 612672732 424 KRIN-LGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:PRK13636 186 EMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-219 |
1.00e-18 |
|
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: 85.08 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIfdhLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-----------NLIEL-PMKYDelivd 69
Cdd:cd03299 1 LKVENLSKDWKEFKLKN---VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpdsgkillngkDITNLpPEKRD----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 plSGVIFQDpDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVN----LNVTPETyikdLSGGMKQKLAIVETIL 145
Cdd:cd03299 73 --ISYVPQN-YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGidhlLNRKPET----LSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 146 QQSKTLFLDEPTAMLDVQATEDLwTKLIELWEDQ---TVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEIILQK 219
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKL-REELKKIRKEfgvTVLHVTHDFEEAWALADKVAIM-LNGKLIQVGKPEEVFKK 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-208 |
1.04e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 87.08 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielP----MKYDELIVDPLS---- 72
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET-----PdsgrILLDGRDVTGLPpekr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 --GVIFQDPD-----SqfcmpkVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETIL 145
Cdd:COG3842 78 nvGMVFQDYAlfphlT------VAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 146 QQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHkvkhiwNHV------DRVILMDyNGNII 208
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTH------DQEealalaDRIAVMN-DGRIE 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
252-438 |
1.22e-18 |
|
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: 84.54 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ------GDVYFENQRLTKIKHAA---- 321
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdeGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 322 KHMYLVYQNPELqfITNSVYDeiNIHFN---HLSKDQSDDETI--QLLKLLDL-ENVKDQ-HPYELSIGQKRRLSVATAL 394
Cdd:cd03260 81 RRVGMVFQKPNP--FPGSIYD--NVAYGlrlHGIKLKEELDERveEALRKAALwDEVKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 612672732 395 SSKADIIFLDEPTFGLDSHNTF---QLIKLFQKRInlgqSIFMVTHD 438
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAkieELIAELKKEY----TIVIVTHN 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-186 |
1.36e-18 |
|
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: 88.19 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRkIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNL---IEL----PMKYDELIVDPLSGV 74
Cdd:TIGR02868 335 LELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLqgeVTLdgvpVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 75 IFQDP---DSQfcmpkvyeelafVLENRQVPREDM-DALIINALNMVNLnvtpETYIKDL---------------SGGMK 135
Cdd:TIGR02868 414 CAQDAhlfDTT------------VRENLRLARPDAtDEELWAALERVGL----ADWLRALpdgldtvlgeggarlSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEH 186
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-199 |
1.46e-18 |
|
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: 84.00 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 6 DLRLKYPSGQrKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnliELPMKyDELIVD--PLS----------- 72
Cdd:cd03292 5 NVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTS-GTIRVNgqDVSdlrgraipylr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ---GVIFQD----PDSQfcmpkVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETIL 145
Cdd:cd03292 78 rkiGVVFQDfrllPDRN-----VYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 146 QQSKTLFLDEPTAMLDVQATedlwTKLIELWED-----QTVVIVEHKVKHIWNHVDRVI 199
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTT----WEIMNLLKKinkagTTVVVATHAKELVDTTRHRVI 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
267-459 |
1.46e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ------GDVYFEN--QRLTKIKHAAKHMYLVYQNPELQFITN 338
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivGDYAIPAnlKKIKEVKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 339 SVYDEINIHFNHLSKDQSD--DETIQLLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEayKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 612672732 416 FQLIKLFQK-RINLGQSIFMVTHDDEIIERYPSRRLKISDGALLD 459
Cdd:PRK13645 187 EDFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-208 |
1.53e-18 |
|
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: 84.55 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKI--FDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIELP----MKYDELIVDPLS-- 72
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-----NGLERPtsgsVLVDGTDLTLLSgk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ---------GVIFQdpdsQFCM---PKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAI 140
Cdd:cd03258 76 elrkarrriGMIFQ----HFNLlssRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 141 VETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWE--DQTVVIVEHK---VKHIwnhVDRVILMDyNGNII 208
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEmevVKRI---CDRVAVME-KGEVV 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
271-458 |
1.58e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTL---LESIMQ------LIKYQgDVYFENQRLTKIKhaaKHMYLVYQNPELQFITNSVY 341
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLflhFNGILKptsgevLIKGE-PIKYDKKSLLEVR---KTVGIVFQNPDDQLFAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DEI-----NIHfnhLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTF 416
Cdd:PRK13639 98 EDVafgplNLG---LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 612672732 417 QLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALL 458
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
271-445 |
1.62e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.46 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLT------KIKHAAKHMYLVYQNPELQFITNSVydE 343
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIGERVITagkknkKLKPLRKKVGIVFQFPEHQLFEETV--E 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INIHFNHLSKDQSDDETIQ----LLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:PRK13634 105 KDICFGPMNFGVSEEDAKQkareMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM 184
|
170 180 190
....*....|....*....|....*....|
gi 612672732 419 IKLF---QKRINLgqSIFMVTHDDEIIERY 445
Cdd:PRK13634 185 MEMFyklHKEKGL--TTVLVTHSMEDAARY 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-201 |
2.07e-18 |
|
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: 87.73 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmKYDELIVdpLSGVIFQDPDS 81
Cdd:TIGR02857 322 LEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-------PTEGSIA--VNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFCM---------PKVYEelAFVLENRQVPREDM-DALIINALNMVNLN----VTP---ETYIKD----LSGGMKQKLAI 140
Cdd:TIGR02857 392 DSWRdqiawvpqhPFLFA--GTIAENIRLARPDAsDAEIREALERAGLDefvaALPqglDTPIGEggagLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 141 VETILQQSKTLFLDEPTAMLDvQATEDLWTKLI-ELWEDQTVVIVEHKVKHIWNhVDRVILM 201
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLD-AETEAEVLEALrALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
272-458 |
2.36e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.79 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQL-IKYQGDVYFENQRLTK--IKHAAKHMYLVYQNPELQFITNSVYDE----- 343
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAenEKWVRSKVGLVFQDPDDQVFSSTVWDDvafgp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INIHfnhLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQ 423
Cdd:PRK13647 106 VNMG---LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILD 182
|
170 180 190
....*....|....*....|....*....|....*
gi 612672732 424 KRINLGQSIFMVTHDDEIIERYPSRRLKISDGALL 458
Cdd:PRK13647 183 RLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-214 |
3.40e-18 |
|
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: 84.75 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-----------NLIELPMKYDELIvdplsGVIFQdpdsq 82
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRptsgtarvagyDVVREPRKVRRSI-----GIVPQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 83 fcMPKVYEELAfVLENRQ-------VPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDE 155
Cdd:TIGR01188 74 --YASVDEDLT-GRENLEmmgrlygLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 156 PTAMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVDRVILMDYnGNIIADECPE 214
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALkEEGVTILLTTHYMEEADKLCDRIAIIDH-GRIIAEGTPE 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
271-438 |
3.44e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.51 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAAKHMYLVYQNPELqFITNSVYDeiNIHF- 348
Cdd:COG3839 23 DLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPtSGEILIGGRDVTDLPPKDRNIAMVFQSYAL-YPHMTVYE--NIAFp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 ---NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSH---NTFQLIKLF 422
Cdd:COG3839 100 lklRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKlrvEMRAEIKRL 179
|
170
....*....|....*.
gi 612672732 423 QKRinLGQSIFMVTHD 438
Cdd:COG3839 180 HRR--LGTTTIYVTHD 193
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
265-457 |
3.87e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.29 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 265 TLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKI------KHAAKHMYLVYQN----PEL 333
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQMdeearaKLRAKHVGFVFQSfmliPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 334 QFITNSvydEINIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSH 413
Cdd:PRK10584 104 NALENV---ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 612672732 414 NTFQLIK-LFQKRINLGQSIFMVTHDDEIIERYpSRRLKISDGAL 457
Cdd:PRK10584 181 TGDKIADlLFSLNREHGTTLILVTHDLQLAARC-DRRLRLVNGQL 224
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-195 |
4.11e-18 |
|
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: 82.83 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlieLPMKYDELIVD--PLSGVIFQDP 79
Cdd:TIGR03740 1 LETKNLSKRF--GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI------LRPTSGEIIFDghPWTRKDLHKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFCMPKVYEELAfVLENRQVpREDM----DALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDE 155
Cdd:TIGR03740 73 GSLIESPPLYENLT-ARENLKV-HTTLlglpDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 612672732 156 PTAMLDVQATEDLwTKLIELWEDQ--TVVIVEH---KVKHIWNHV 195
Cdd:TIGR03740 151 PTNGLDPIGIQEL-RELIRSFPEQgiTVILSSHilsEVQQLADHI 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-207 |
5.21e-18 |
|
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: 82.58 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIElpmkydelivDPLSGVIFQD--- 78
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-----NLLE----------EPDSGTIIIDglk 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 -PDSQFCMPKVYEELAFV------------LEN--------RQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQK 137
Cdd:cd03262 64 lTDDKKNINELRQKVGMVfqqfnlfphltvLENitlapikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 138 LAIVETILQQSKTLFLDEPTAMLD---VQATEDLWTKLIElwEDQTVVIVEHKVKHIWNHVDRVILMDyNGNI 207
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAE--EGMTMVVVTHEMGFAREVADRVIFMD-DGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-217 |
5.35e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 83.12 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIELPmkyD--ELIVDplsGVIFQD 78
Cdd:COG1126 1 MIEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-----NLLEEP---DsgTITVD---GEDLTD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 PDSQfcMPKVYEELAFV------------LEN--------RQVPREDMDALIINALNMVNL----NVTPETyikdLSGGM 134
Cdd:COG1126 68 SKKD--INKLRRKVGMVfqqfnlfphltvLENvtlapikvKKMSKAEAEERAMELLERVGLadkaDAYPAQ----LSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 135 KQKLAIVETILQQSKTLFLDEPTAMLD---VQATEDLWTKLIElwEDQTVVIVEH------KVkhiwnhVDRVILMDyNG 205
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDpelVGEVLDVMRDLAK--EGMTMVVVTHemgfarEV------ADRVVFMD-GG 212
|
250
....*....|..
gi 612672732 206 NIIADECPEIIL 217
Cdd:COG1126 213 RIVEEGPPEEFF 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-186 |
5.36e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPN---LIELPmkydelivdPLSGVIFq 77
Cdd:COG4178 362 ALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgsgRIARP---------AGARVLF- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 78 dpdsqfcMP-KVY-------EELAFVLENRQVPREDmdalIINALNMVNLnvtpeTYIKD-----------LSGGMKQKL 138
Cdd:COG4178 431 -------LPqRPYlplgtlrEALLYPATAEAFSDAE----LREALEAVGL-----GHLAErldeeadwdqvLSLGEQQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 612672732 139 AIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEH 186
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-208 |
5.54e-18 |
|
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: 83.05 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 6 DLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpnlielPMKYDelivdPLSGVIFQDPD--SQF 83
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----------PRFYD-----VDSGRILIDGHdvRDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 84 CMPKVYEELAFVLEN----------------RQVPREDmdalIINALNMVNL----NVTPETY---IKD----LSGGMKQ 136
Cdd:cd03251 70 TLASLRRQIGLVSQDvflfndtvaeniaygrPGATREE----VEEAARAANAhefiMELPEGYdtvIGErgvkLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 137 KLAIVETILQQSKTLFLDEPTAMLDVQaTEDLWTKLIE-LWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNII 208
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTE-SERLVQAALErLMKNRTTFVIAHRLSTI-ENADRIVVLE-DGKIV 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
251-463 |
5.56e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.83 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRL----TKIKHAAKHMY 325
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsGDLIVDGLKVndpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 326 LVYQN----PELQFITNSVYDEIniHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADII 401
Cdd:PRK09493 81 MVFQQfylfPHLTALENVMFGPL--RVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 402 FLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDcDGD 463
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE-DGD 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-214 |
6.03e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 6.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRK-IFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI-VPNLIELPMKYDELIVDPL------S 72
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLlEAESGQIIIDGDLLTEENVwdirhkI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLF 152
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 153 LDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIwNHVDRVILMDyNGNIIADECPE 214
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMK-NGQVESTSTPR 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-208 |
6.23e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.44 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRkIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-------NLIELpmkydelivdplsgv 74
Cdd:PRK11174 350 IEAEDLEILSPDGKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslkiNGIEL--------------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 75 ifqdpdSQFCMPKVYEELAFVLENRQVP----REDM--------DALIINALNMVNLN-VTP------ETYIKD----LS 131
Cdd:PRK11174 414 ------RELDPESWRKHLSWVGQNPQLPhgtlRDNVllgnpdasDEQLQQALENAWVSeFLPllpqglDTPIGDqaagLS 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 132 GGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNII 208
Cdd:PRK11174 488 VGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL-AQWDQIWVMQ-DGQIV 562
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
271-442 |
8.00e-18 |
|
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: 83.08 E-value: 8.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA------KHMYLVYQN----PELQFITNS 339
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSfallPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 340 VYD-EINihfnHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDShntfqL 418
Cdd:cd03294 124 AFGlEVQ----GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP-----L 194
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 419 IK------LFQKRINLGQSIFMVTHD-DEII 442
Cdd:cd03294 195 IRremqdeLLRLQAELQKTIVFITHDlDEAL 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-237 |
8.12e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 17 KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLIELPMKYDELIVDPLS------------GVIFQDPDSQFC 84
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKkikevkrlrkeiGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 85 MPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtPETYIK----DLSGGMKQKLAIVETILQQSKTLFLDEPTAML 160
Cdd:PRK13645 105 QETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL---PEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 161 DVQATEDLWTKLIELWEDQT--VVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEIILQKyVHLLSEYGVWHPRAWEF 237
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVM-HEGKVISIGSPFEIFSN-QELLTKIEIDPPKLYQL 258
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-229 |
9.07e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.86 E-value: 9.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnliELPmkydelivdPLSGVI--FQD 78
Cdd:COG4559 1 MLEAENLSVRL--GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG------ELT---------PSSGEVrlNGR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 PDSQFC----------MPKvYEELAF---VLE-------NRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQK- 137
Cdd:COG4559 64 PLAAWSpwelarrravLPQ-HSSLAFpftVEEvvalgraPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRv 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 138 -LAIV-----ETILQQSKTLFLDEPTAMLDV---QATEDLwtkLIELWEDQTVVIVehkVKHIWN----HVDRVILMDyN 204
Cdd:COG4559 143 qLARVlaqlwEPVDGGPRWLFLDEPTSALDLahqHAVLRL---ARQLARRGGGVVA---VLHDLNlaaqYADRILLLH-Q 215
|
250 260
....*....|....*....|....*.
gi 612672732 205 GNIIADECPEIILQKyvHLLSE-YGV 229
Cdd:COG4559 216 GRLVAQGTPEEVLTD--ELLERvYGA 239
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-209 |
9.68e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.04 E-value: 9.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlielpmkydelIVDPLSGVI------ 75
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG---------------LETPDSGRIvlngrd 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 ---------------FQDPDsqfCMP--KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKL 138
Cdd:COG1118 66 lftnlpprerrvgfvFQHYA---LFPhmTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 139 AIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHkvkhiwNHV------DRVILMDyNGNIIA 209
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTH------DQEealelaDRVVVMN-QGRIEQ 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-210 |
1.01e-17 |
|
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: 81.49 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIFQDPDS 81
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIK---------------PDSGEITFDGKS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFCMPKVYEELAFVLE------NRQVpREDM----------DALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETIL 145
Cdd:cd03268 64 YQKNIEALRRIGALIEapgfypNLTA-RENLrllarllgirKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 146 QQSKTLFLDEPTAMLDVQATEDLwTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIAD 210
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKEL-RELILSLRDQgiTVLISSHLLSEIQKVADRIGIIN-KGKLIEE 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
277-437 |
1.03e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLI----KYQGDVYFENQRLTKIKHAAKHMYlVYQNpELQFITNSVYDEINI--HF-- 348
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSpkgvKGSGSVLLNGMPIDAKEMRAISAY-VQQD-DLFIPTLTVREHLMFqaHLrm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 -NHLSKDQSD---DETIQLLKLLDLENVKDQHPYE---LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKL 421
Cdd:TIGR00955 129 pRRVTKKEKRervDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170
....*....|....*.
gi 612672732 422 FQKRINLGQSIFMVTH 437
Cdd:TIGR00955 209 LKGLAQKGKTIICTIH 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-210 |
1.53e-17 |
|
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: 82.01 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDP 79
Cdd:COG0411 4 LLEVRGLTKRF--GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR---------------PTSGrILFDGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 D------SQFC---------MPKVYEELAfVLEN--------------------RQVPREDMDAL--IINALNMVNLNVT 122
Cdd:COG0411 67 DitglppHRIArlgiartfqNPRLFPELT-VLENvlvaaharlgrgllaallrlPRARREEREARerAEELLERVGLADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 123 PETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVIL 200
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLADRIVV 225
|
250
....*....|
gi 612672732 201 MDYnGNIIAD 210
Cdd:COG0411 226 LDF-GRVIAE 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-209 |
1.75e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 84.83 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 6 DLRLKYPSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpmkYD----ELIVD-------PLS-- 72
Cdd:COG1132 344 NVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF----------YDptsgRILIDgvdirdlTLEsl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ----GVIFQDP----DSqfcmpkVYEELAFVLENrqVPREDmdalIINALNMVNLN--VT--PE---TYIKD----LSGG 133
Cdd:COG1132 413 rrqiGVVPQDTflfsGT------IRENIRYGRPD--ATDEE----VEEAAKAAQAHefIEalPDgydTVVGErgvnLSGG 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 134 MKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNIIA 209
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTI-RNADRILVLD-DGRIVE 554
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
271-442 |
2.46e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.96 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTK--IKHAAKHMYLVYQNPELQFITNSVYDEI--N 345
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsGEIKIDGITISKenLKEIRKKIGIIFQNPDNQFIGATVEDDIafG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SHNTFQLIKLF 422
Cdd:PRK13632 109 LENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDL 188
|
170 180
....*....|....*....|.
gi 612672732 423 QKRINlgQSIFMVTHD-DEII 442
Cdd:PRK13632 189 RKTRK--KTLISITHDmDEAI 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
14-216 |
2.54e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpmkydElivDPLSGVIFQD-------PDSQ---- 82
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF------------E---TPDSGRIMLDgqdithvPAENrhvn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 83 --------FCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLD 154
Cdd:PRK09452 90 tvfqsyalFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 155 EPTAMLDVqatedlwtKL-----IELWEDQ-----TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEII 216
Cdd:PRK09452 170 ESLSALDY--------KLrkqmqNELKALQrklgiTFVFVTHDQEEALTMSDRIVVMR-DGRIEQDGTPREI 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-184 |
3.57e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.34 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI-VPNliELPMKYDELIVDPLS------- 72
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIeKVK--SGEIFYNNQAITDDNfeklrkh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:PRK13648 85 iGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190
....*....|....*....|....*....|...
gi 612672732 152 FLDEPTAMLDVQATEDLWTKLIELWEDQTVVIV 184
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITII 197
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-207 |
4.53e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.44 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvPNLIELPMKYDELIVDPLS------GVIFQDPdSQFCMPK 87
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTDVSRLHardrkvGFVFQHY-ALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 88 VYEELAF---VLENRQVP-REDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ 163
Cdd:PRK10851 91 VFDNIAFgltVLPRRERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 612672732 164 ATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNI 207
Cdd:PRK10851 171 VRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVADRVVVMS-QGNI 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
271-443 |
4.92e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.12 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAK-HMYLVYQNPELqFITNSVYDeiNIHF 348
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETpDSGRIVLNGRDLFTNLPPRErRVGFVFQHYAL-FPHMTVAE--NIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 ----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPtFG-LDSHNTFQLiklfq 423
Cdd:COG1118 99 glrvRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP-FGaLDAKVRKEL----- 172
|
170 180
....*....|....*....|....*....
gi 612672732 424 kRINL--------GQSIFmVTHD-DEIIE 443
Cdd:COG1118 173 -RRWLrrlhdelgGTTVF-VTHDqEEALE 199
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
261-452 |
6.01e-17 |
|
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: 78.94 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIK-HAAKHM-YLVYQN---PELq 334
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRpDSGEVRWNGTPLAEQRdEPHENIlYLGHLPglkPEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 335 fitnSVYDeiNIHF-NHLSkdQSDDETI-QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:TIGR01189 89 ----SALE--NLHFwAAIH--GGAQRTIeDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 413 HNTFQLIKLFQKRINLGQSIFMVTHDDEIIEryPSRRLKI 452
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQDLGLV--EARELRL 198
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
6.25e-17 |
|
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: 77.85 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGqrKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIFqdpds 81
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK---------------PDSGEIL----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 qfcmpkvyeelafvLENRQV----PREDMDALIinalNMVnlnvtpetYikDLSGGMKQKLAIVETILQQSKTLFLDEPT 157
Cdd:cd03216 59 --------------VDGKEVsfasPRDARRAGI----AMV--------Y--QLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 158 AMLDVQATEDLWtKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIAD 210
Cdd:cd03216 111 AALTPAEVERLF-KVIRRLRAQgvAVIFISHRLDEVFEIADRVTVLR-DGRVVGT 163
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
282-463 |
8.74e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.05 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 282 ITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHA----AKHMYLVYQNPELQFITNSVYDEINIHFNHL--SKD 354
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRpQKGAVLWQGKPLDYSKRGllalRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLgvPEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 355 QSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFM 434
Cdd:PRK13638 112 EITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII 191
|
170 180
....*....|....*....|....*....
gi 612672732 435 VTHDDEIIerypsrrLKISDGALLDCDGD 463
Cdd:PRK13638 192 SSHDIDLI-------YEISDAVYVLRQGQ 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-448 |
9.63e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 9.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKI--FDHLNITIQDKEKVLLLGPSGCGKST-------LLNVLSGIVPNLIELPMKYDELIVDpL 71
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVIE-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 72 S---------------GVIFQDP-DSQFCMPKVYEELAFVLENRQ-VPREDMdalIINALNMVNLNVTPET------YIK 128
Cdd:PRK10261 91 SeqsaaqmrhvrgadmAMIFQEPmTSLNPVFTVGEQIAESIRLHQgASREEA---MVEAKRMLDQVRIPEAqtilsrYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 129 DLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDV--QATEDLWTKLIELWEDQTVVIVEHKVKHIWNHVDRVILMdYNGN 206
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM-YQGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 207 IIADECPEIILQKYVH-----LLSEY-------GVWHPRAWEF----APSRVDFPTTNSH------LLQFKN-------- 256
Cdd:PRK10261 247 AVETGSVEQIFHAPQHpytraLLAAVpqlgamkGLDYPRRFPLisleHPAKQEPPIEQDTvvdgepILQVRNlvtrfplr 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 257 -GRIIRGKSTLLSFSDLEIGL--GEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRL-----TKIKHAAKHMYLV 327
Cdd:PRK10261 327 sGLLNRVTREVHAVEKVSFDLwpGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIdtlspGKLQALRRDIQFI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 328 YQNP-----ELQFITNSVYDEINIHfNHLSKDQSDDETIQLLKLLDLenvKDQH----PYELSIGQKRRLSVATALSSKA 398
Cdd:PRK10261 407 FQDPyasldPRQTVGDSIMEPLRVH-GLLPGKAAAARVAWLLERVGL---LPEHawryPHEFSGGQRQRICIARALALNP 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 612672732 399 DIIFLDEPTFGLDSHNTFQLIKL---FQKriNLGQSIFMVTHDDEIIERYPSR 448
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQIINLlldLQR--DFGIAYLFISHDMAVVERISHR 533
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
239-437 |
1.01e-16 |
|
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: 78.36 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 239 PSRVDFpttnSHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIM-QLI--KYQGDVYFENQRLT 315
Cdd:cd03213 1 GVTLSF----RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTglGVSGEVLINGRPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 316 KIKHAaKHMYLVYQNpelqfitnsvydeiNIHFNHLSKDqsddETIQLLKLLDlenvkdqhpyELSIGQKRRLSVATALS 395
Cdd:cd03213 77 KRSFR-KIIGYVPQD--------------DILHPTLTVR----ETLMFAAKLR----------GLSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 612672732 396 SKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTH 437
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-435 |
1.09e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 17 KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNlielpMKYDELIV---DPLSGVIFQDPDsQFCMPKVYEELA 93
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH-----GTYEGEIIfegEELQASNIRDTE-RAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 94 F-----VLENRQVPRE-------DMDALIINA---LNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTA 158
Cdd:PRK13549 93 LvkelsVLENIFLGNEitpggimDYDAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 159 MLDVQATEDLWTKLIELWE-DQTVVIVEHK---VKHIWNHV-------------------DRVILMdYNGNIIADECP-- 213
Cdd:PRK13549 173 SLTESETAVLLDIIRDLKAhGIACIYISHKlneVKAISDTIcvirdgrhigtrpaagmteDDIITM-MVGRELTALYPre 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 214 -----EIILQkyvhlLSEYGVWHPrawefapsrvdfptTNSHLLQFKNgriirgkstlLSFSdleIGLGEWITITGANGS 288
Cdd:PRK13549 252 phtigEVILE-----VRNLTAWDP--------------VNPHIKRVDD----------VSFS---LRRGEILGIAGLVGA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 289 GKTTLLESIMQLI--KYQGDVYFENQRLtKIKHAA--------------KHMYLVYQNPELQFITNSVYDEINIH--FNH 350
Cdd:PRK13549 300 GRTELVQCLFGAYpgRWEGEIFIDGKPV-KIRNPQqaiaqgiamvpedrKRDGIVPVMGVGKNITLAALDRFTGGsrIDD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 351 LSKDQSDDETIQLLKlldlenVKDQHPyELSIGqkrRLS--------VATALSSKADIIFLDEPTFGLDSHNTFQLIKLF 422
Cdd:PRK13549 379 AAELKTILESIQRLK------VKTASP-ELAIA---RLSggnqqkavLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI 448
|
490
....*....|...
gi 612672732 423 QKRINLGQSIFMV 435
Cdd:PRK13549 449 NQLVQQGVAIIVI 461
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
271-455 |
1.42e-16 |
|
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: 78.76 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA-----KHMYLVYQNPELqfITN-SVYDE 343
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTDINKLKGKAlrqlrRQIGMIFQQFNL--IERlSVLEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INI-HFNHLSKDQS-----DDETIQL-LKLLDLENVKDQHpY----ELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:cd03256 99 VLSgRLGRRSTWRSlfglfPKEEKQRaLAALERVGLLDKA-YqradQLSGGQQQRVAIARALMQQPKLILADEPVASLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 612672732 413 HNTFQLIKLFqKRIN--LGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03256 178 ASSRQVMDLL-KRINreEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-208 |
1.47e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 78.74 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 5 SDLRLKYPS-GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVL-------SGIVP----NLIELPMK-YDELIvdpl 71
Cdd:cd03249 4 KNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILldgvDIRDLNLRwLRSQI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 72 sGVIFQDPDSQFCmpKVYEELAFVLENRQVPREDMDALIINALNMV-NLnvtPETYI-------KDLSGGMKQKLAIVET 143
Cdd:cd03249 80 -GLVSQEPVLFDG--TIAENIRYGKPDATDEEVEEAAKKANIHDFImSL---PDGYDtlvgergSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 144 ILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNhVDRVILMDyNGNII 208
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQ-NGQVV 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
254-411 |
1.52e-16 |
|
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: 78.74 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 254 FKNGRIIRGKStllsfsdLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKikhaaKHMY------L 326
Cdd:cd03218 10 YGKRKVVNGVS-------LSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILLDGQDITK-----LPMHkrarlgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 327 VY--QNPELqFITNSVYDEINI--HFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:cd03218 78 GYlpQEASI-FRKLTVEENILAvlEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
....*....
gi 612672732 403 LDEPTFGLD 411
Cdd:cd03218 157 LDEPFAGVD 165
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-210 |
1.58e-16 |
|
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: 78.30 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIfdHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnliELPMKYDELI--VD---------P 70
Cdd:cd03298 1 VRLDKIRFSY--GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGF-----ETPQSGRVLIngVDvtaappadrP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 LSgVIFQDpDSQFCMPKVYEELAFV----LENRQVPREDMDAliinALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQ 146
Cdd:cd03298 72 VS-MLFQE-NNLFAHLTVEQNVGLGlspgLKLTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 147 QSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIAD 210
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLD-NGRIAAQ 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-210 |
1.76e-16 |
|
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: 78.24 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDPD 80
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---------------PRSGsIRFDGRD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 ----SQFCMPKvyEELAFVLENRQV---------------------PREDMDALiinalnmvnLNVTPEtyIKD------ 129
Cdd:cd03224 64 itglPPHERAR--AGIGYVPEGRRIfpeltveenlllgayarrrakRKARLERV---------YELFPR--LKErrkqla 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 130 --LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVDRVILMDyNGN 206
Cdd:cd03224 131 gtLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEIADRAYVLE-RGR 209
|
....
gi 612672732 207 IIAD 210
Cdd:cd03224 210 VVLE 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-208 |
1.99e-16 |
|
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: 78.08 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 16 RKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNlieLPMKYDELIVD--PLSGVIFQDPDS---QFC--MP-- 86
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG---GGTTSGQILFNgqPRKPDQFQKCVAyvrQDDilLPgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 87 KVYEELAFVLENRqVPREDMDALI-----INALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLD 161
Cdd:cd03234 97 TVRETLTYTAILR-LPRKSSDAIRkkrveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 162 VQATEDLWTKLIELWEDQTVVIVE-HKVK-HIWNHVDRVILMDyNGNII 208
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTiHQPRsDLFRLFDRILLLS-SGEIV 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-207 |
2.17e-16 |
|
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: 76.87 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIfqdpds 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR---------------PTSGRV------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 qfcmpkvyeelafVLENRQVPREDMDAL--IINALnMVNLNVTPETyIKD--LSGGMKQKLAIVETILQQSKTLFLDEPT 157
Cdd:cd03246 60 -------------RLDGADISQWDPNELgdHVGYL-PQDDELFSGS-IAEniLSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 612672732 158 AMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIwNHVDRVILMDyNGNI 207
Cdd:cd03246 125 SHLDVEGERALNQAIAALkAAGATRIVIAHRPETL-ASADRILVLE-DGRV 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
245-440 |
2.35e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.38 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 245 PTTNSHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQL-IKYQGDVYFENQRLTKIKHAAKH 323
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDGQDITHVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 324 MYLVYQNPELqFITNSVYDeiNIHF----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKAD 399
Cdd:PRK09452 88 VNTVFQSYAL-FPHMTVFE--NVAFglrmQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 612672732 400 IIFLDEPTFGLDshntFQLIKLFQKRI-----NLGQSIFMVTHDDE 440
Cdd:PRK09452 165 VLLLDESLSALD----YKLRKQMQNELkalqrKLGITFVFVTHDQE 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-224 |
2.48e-16 |
|
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: 78.38 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP--------NLIELPMKYDELIVDPLS- 72
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEptsgsvliDGTDINKLKGKALRQLRRq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQDPDsqfcmpkVYEELAfVLEN----------------RQVPREDMdALIINALNMVNLNVTPETYIKDLSGGMK 135
Cdd:cd03256 80 iGMIFQQFN-------LIERLS-VLENvlsgrlgrrstwrslfGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECP 213
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLK-DGRIVFDGPP 229
|
250
....*....|.
gi 612672732 214 EIILQKYVHLL 224
Cdd:cd03256 230 AELTDEVLDEI 240
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-208 |
2.52e-16 |
|
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: 81.30 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivPNLIElPMKYDELIVD-PLSGVIFQDPD 80
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI----PRFYE-PDSGQILLDGhDLADYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 SQFCM---------PKVYEELAFVlENRQVPREDMDALIINALNMVNLNVTPE---TYIKD----LSGGMKQKLAIVETI 144
Cdd:TIGR02203 406 RQVALvsqdvvlfnDTIANNIAYG-RTEQADRAEIERALAAAYAQDFVDKLPLgldTPIGEngvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 145 LQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNII 208
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTI-EKADRIVVMD-DGRIV 546
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
271-457 |
3.33e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA-----KHMYLVYQNPELqFITNSVYDEI 344
Cdd:PRK10908 22 TFHMRPGEMAFLTGHSGAGKSTLLKLICGIERpSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHL-LMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 NIHFNhLSKDQSDDETIQLLKLLDLENVKDQ---HPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKL 421
Cdd:PRK10908 101 AIPLI-IAGASGDDIRRRVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 612672732 422 FQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGAL 457
Cdd:PRK10908 180 FEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-218 |
3.43e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.27 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnliELPmkydelivdPLSGVI--FQD 78
Cdd:PRK13548 2 MLEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG------ELS---------PDSGEVrlNGR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 PDSQF----------CMPKvYEELAF---VLE--------NRQVPREDmDALIINALNMVNLNVTPETYIKDLSGGMKQK 137
Cdd:PRK13548 65 PLADWspaelarrraVLPQ-HSSLSFpftVEEvvamgrapHGLSRAED-DALVAAALAQVDLAHLAGRDYPQLSGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 138 --LAIVETIL----QQSKTLFLDEPTAMLDVQATEDLWTKLIEL-WEDQTVVIVehkVKHIWN----HVDRVILMDyNGN 206
Cdd:PRK13548 143 vqLARVLAQLwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIV---VLHDLNlaarYADRIVLLH-QGR 218
|
250
....*....|..
gi 612672732 207 IIADECPEIILQ 218
Cdd:PRK13548 219 LVADGTPAEVLT 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-229 |
3.67e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 22 LNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-----NLIELPMkyDELIVDPLS---GVIFQDPDSQFCMPkVYEELA 93
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPL--SDWSAAELArhrAYLSQQQSPPFAMP-VFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 94 FVLenrqvPREDMDALIINALNMV--NLNVTP--ETYIKDLSGGMKQKLAIVETILQ-------QSKTLFLDEPTAMLDV 162
Cdd:COG4138 92 LHQ-----PAGASSEAVEQLLAQLaeALGLEDklSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 163 --QATEDLWtkLIELWEDQ-TVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEIILQkyVHLLSE-YGV 229
Cdd:COG4138 167 aqQAALDRL--LRELCQQGiTVVMSSHDLNHTLRHADRVWLL-KQGKLVASGETAEVMT--PENLSEvFGV 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
261-455 |
3.81e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHMY-----LVYQ----- 329
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNRAQRKAFrrdiqMVFQdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 330 -NPelQFITNSVYDEINIHFNHLSKDQSDDETIQLLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPT 407
Cdd:PRK10419 102 vNP--RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 408 FGLDSHNTFQLIKLFQK-RINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKlQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
239-446 |
4.10e-16 |
|
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: 80.41 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 239 PSRVDFPTTNSHLLQFKNGRII-RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTK 316
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 317 IKHAA--KHMYLVYQNPelQFITNSVYDEINIHfnhlSKDQSDDETIQLLKL-----------LDLENVKDQHPYELSIG 383
Cdd:TIGR02857 389 ADADSwrDQIAWVPQHP--FLFAGTIAENIRLA----RPDASDAEIREALERagldefvaalpQGLDTPIGEGGAGLSGG 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 384 QKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINlGQSIFMVTHDDEIIERYP 446
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALAD 524
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
271-444 |
4.62e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.97 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEwIT-ITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAA-----KHMYLVYQNPELQfitNS--VY 341
Cdd:COG1135 25 SLTIEKGE-IFgIIGYSGAGKSTLIRCINLLERPtSGSVLVDGVDLTALSERElraarRKIGMIFQHFNLL---SSrtVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DeiNIHF----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQ 417
Cdd:COG1135 101 E--NVALpleiAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRS 178
|
170 180
....*....|....*....|....*....
gi 612672732 418 LIKLFqKRIN--LGQSIFMVTHDDEIIER 444
Cdd:COG1135 179 ILDLL-KDINreLGLTIVLITHEMDVVRR 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-226 |
4.65e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.65 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSgivpNLIELpmkYDELIVdplSGVIFQDPDS 81
Cdd:PRK14247 4 IEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN----RLIEL---YPEARV---SGEVYLDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFCMP---------------------KVYEELAFVLE-NRQV-PREDMDALIINALNMVNLnvtpETYIKD--------L 130
Cdd:PRK14247 72 IFKMDvielrrrvqmvfqipnpipnlSIFENVALGLKlNRLVkSKKELQERVRWALEKAQL----WDEVKDrldapagkL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 131 SGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNHVDRVILMdYNGNIIAD 210
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFL-YKGQIVEW 226
|
250
....*....|....*.
gi 612672732 211 ECPEIILQKYVHLLSE 226
Cdd:PRK14247 227 GPTREVFTNPRHELTE 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-208 |
4.96e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.48 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpSGQRkIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIELP----MKYDELIVD---PLSG 73
Cdd:PRK11264 3 AIEVKNLVKKF-HGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-----NLLEQPeagtIRVGDITIDtarSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 74 vifqdpdSQFCMPKVYEELAFV------------LEN--------RQVPREDMDALIINALNMVNLNVTPETYIKDLSGG 133
Cdd:PRK11264 76 -------QKGLIRQLRQHVGFVfqnfnlfphrtvLENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 134 MKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ-TVVIVEHKVKHIWNHVDRVILMDyNGNII 208
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMD-QGRIV 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
272-437 |
4.99e-16 |
|
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: 76.86 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAA--KHMYLVYQNPELQFitNSVYDeiNIHF 348
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTsGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLFY--GTLRD--NITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 NHLSKDqsDDETIQLLKLLDLENVKDQHP-----------YELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQ 417
Cdd:cd03245 101 GAPLAD--DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180
....*....|....*....|
gi 612672732 418 LIKLFQKRINlGQSIFMVTH 437
Cdd:cd03245 179 LKERLRQLLG-DKTLIIITH 197
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
267-438 |
5.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLT--KIKHAAKHMYLVYQNPELQFITNSVYDE 343
Cdd:PRK13642 26 VSFS---ITKGEWVSIIGQNGSGKSTTARLIDGLFEeFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INIHFNHLSKDQSD-----DETIQLLKLLDLenvKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:PRK13642 103 VAFGMENQGIPREEmikrvDEALLAVNMLDF---KTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180
....*....|....*....|.
gi 612672732 419 IKLFQK-RINLGQSIFMVTHD 438
Cdd:PRK13642 180 MRVIHEiKEKYQLTVLSITHD 200
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
262-459 |
5.15e-16 |
|
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: 76.70 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIK-HAAKHMYLVY--QNPELqFIT 337
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRFDGRDITGLPpHERARAGIGYvpEGRRI-FPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 338 NSVYDEINIHFNHLSKDQSDDETIQLLKLL-DLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SH 413
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLApkiVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 612672732 414 NTFQLIklfqKRIN-LGQSIFMVthddeiiERYPSRRLKISD-GALLD 459
Cdd:cd03224 170 EIFEAI----RELRdEGVTILLV-------EQNARFALEIADrAYVLE 206
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
272-438 |
7.06e-16 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 76.43 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKikhAAKHMYLVYQNPELQF-----ITNSVYDEIN 345
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPaKGTVKVAGASPGK---GWRHIGYVPQRHEFAWdfpisVAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHFNHLSKDQSDD--ETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQ 423
Cdd:TIGR03771 78 GHIGWLRRPCVADfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFI 157
|
170
....*....|....*
gi 612672732 424 KRINLGQSIFMVTHD 438
Cdd:TIGR03771 158 ELAGAGTAILMTTHD 172
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-213 |
7.08e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKY-PSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLiELPMKYD--ELIVDPL------ 71
Cdd:PRK13642 4 ILEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-EGKVKIDgeLLTAENVwnlrrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 72 SGVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:PRK13642 83 IGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 152 FLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHvDRVILMDyNGNIIADECP 213
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASS-DRILVMK-AGEIIKEAAP 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
282-440 |
7.72e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 282 ITGANGSGKTTLLESIMQLIKYQ------GDVY----FENQRLT------KIKHAA---KHMYLVYQNPELQFITNSVyd 342
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKygtiqvGDIYigdkKNNHELItnpyskKIKNFKelrRRVSMVFQFPEYQLFKDTI-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EINIHFNHLSKDQSDDETIQLLKL------LDlENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SH 413
Cdd:PRK13631 135 EKDIMFGPVALGVKKSEAKKLAKFylnkmgLD-DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEH 213
|
170 180
....*....|....*....|....*..
gi 612672732 414 NTFQLIKLFQKRinlGQSIFMVTHDDE 440
Cdd:PRK13631 214 EMMQLILDAKAN---NKTVFVITHTME 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
271-438 |
1.02e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 78.22 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHMYLVYQN----PELqfitnSVYDeiN 345
Cdd:COG3842 25 SLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpDSGRILLDGRDVTGLPPEKRNVGMVFQDyalfPHL-----TVAE--N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHF----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSH---NTFQL 418
Cdd:COG3842 98 VAFglrmRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKlreEMREE 177
|
170 180
....*....|....*....|
gi 612672732 419 IKLFQKRinLGQSIFMVTHD 438
Cdd:COG3842 178 LRRLQRE--LGITFIYVTHD 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
272-458 |
1.34e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVY---------FENQRLTKIKHaaKHMYLVYQNPEL-QFITNSVY 341
Cdd:PRK10535 29 LDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvagqdvatLDADALAQLRR--EHFGFIFQRYHLlSHLTAAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DEINIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKL 421
Cdd:PRK10535 107 VEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAI 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 422 FQKRINLGQSIFMVTHDDEIIERyPSRRLKISDGALL 458
Cdd:PRK10535 187 LHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
14-208 |
1.68e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.45 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlielpmkydelIVDPLSGVIFQDPDS---------QFC 84
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG---------------LEKPTEGQIFIDGEDvthrsiqqrDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 85 M--------P--KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLD 154
Cdd:PRK11432 82 MvfqsyalfPhmSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 155 EPTAMLDVQATEDLWTKLIELWE--DQTVVIVEHKVKHIWNHVDRVILMDyNGNII 208
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMN-KGKIM 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-209 |
1.70e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 78.71 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNvlsgivpnlielpmkydeLIV---DPLSGVIFQD 78
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ------------------LLTrawDPQQGEILLN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 --PDSQFCMPKVYEELAFV-----------LENRQV--PREDmDALIINALNMVNLnvtpETYIKD-------------- 129
Cdd:PRK11160 401 gqPIADYSEAALRQAISVVsqrvhlfsatlRDNLLLaaPNAS-DEALIEVLQQVGL----EKLLEDdkglnawlgeggrq 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 130 LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDvQATEDLWTKLI-ELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNII 208
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLD-AETERQILELLaEHAQNKTVLMITHRLTGL-EQFDRICVMD-NGQII 552
|
.
gi 612672732 209 A 209
Cdd:PRK11160 553 E 553
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
267-437 |
1.99e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.73 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVYFENQRLTKIKHAA--KHMYLVYQNPELqfITNSVYDEI 344
Cdd:PRK11174 369 LNFT---LPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESwrKHLSWVGQNPQL--PHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 NihfnhLSKDQSDDEtiQLLKLLDLENVKD---QHP----YE-------LSIGQKRRLSVATALSSKADIIFLDEPTFGL 410
Cdd:PRK11174 444 L-----LGNPDASDE--QLQQALENAWVSEflpLLPqgldTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180
....*....|....*....|....*..
gi 612672732 411 DSHNTfQLIKLFQKRINLGQSIFMVTH 437
Cdd:PRK11174 517 DAHSE-QLVMQALNAASRRQTTLMVTH 542
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
272-440 |
2.19e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.89 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRltkIKHAAKHMYLVYQNPEL---QFITNSVydEINIH 347
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKP---VEGPGAERGVVFQNEGLlpwRNVQDNV--AFGLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 348 FNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQ----LIKLFQ 423
Cdd:PRK11248 97 LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQmqtlLLKLWQ 176
|
170
....*....|....*..
gi 612672732 424 KRinlGQSIFMVTHDDE 440
Cdd:PRK11248 177 ET---GKQVLLITHDIE 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-186 |
2.37e-15 |
|
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: 72.87 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIFQDPDS 81
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE---------------PDEGIVTWGSTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFCmpkvyeelafvlenrqvpredmdaliinalnmvnlnvtpetYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLD 161
Cdd:cd03221 64 KIG-----------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180
....*....|....*....|....*..
gi 612672732 162 VQATEdlwtKLIELWED--QTVVIVEH 186
Cdd:cd03221 103 LESIE----ALEEALKEypGTVILVSH 125
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-436 |
2.55e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 20 DHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP----NLIELPMKYDELivDP-LS-----GVIFQDPdsqfcmpKVY 89
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEptkgTITINNINYNKL--DHkLAaqlgiGIIYQEL-------SVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 90 EELAfVLEN----RQVPREDMDALIINALNM----------VNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDE 155
Cdd:PRK09700 93 DELT-VLENlyigRHLTKKVCGVNIIDWREMrvraammllrVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 156 PTAMLDVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRVILMDYNGNIIADECPEIILQKYVHLL------SEYg 228
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMvgrelqNRF- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 229 vwhprawefaPSRVDFPTTNSHLLQFKNGRIIR---GKSTLLSFSdleIGLGEWITITGANGSGKTTLLESIMQLIKYQ- 304
Cdd:PRK09700 251 ----------NAMKENVSNLAHETVFEVRNVTSrdrKKVRDISFS---VCRGEILGFAGLVGSGRTELMNCLFGVDKRAg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 305 GDVYFENQRLT---KIKHAAKHMYLVYQN-PELQFITN-SVYDEINIH--------------FNHLSKDQSDDETIQLLk 365
Cdd:PRK09700 318 GEIRLNGKDISprsPLDAVKKGMAYITESrRDNGFFPNfSIAQNMAISrslkdggykgamglFHEVDEQRTAENQRELL- 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 366 lldleNVK----DQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVT 436
Cdd:PRK09700 397 -----ALKchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-218 |
2.56e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSgivpnlielpmkydeLIVDPLSGVIFQD-- 78
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA---------------RLLTPQSGTVFLGdk 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 PDSQFCMPKVYEELAFVLENRQVP-----RE------------------DMDALIINALNMVNLNVTPETYIKDLSGGMK 135
Cdd:PRK11231 65 PISMLSSRQLARRLALLPQHHLTPegitvRElvaygrspwlslwgrlsaEDNARVNQAMEQTRINHLADRRLTDLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPE 214
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRYCDHLVVLA-NGHVMAQGTPE 223
|
....
gi 612672732 215 IILQ 218
Cdd:PRK11231 224 EVMT 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
271-458 |
2.56e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.06 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLI-------KYQGDVYFENqrltKIKHAAKHMYLVYQNPELQF---ITNSV 340
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqptsgevRVAGLVPWKR----RKKFLRRIGVVFGQKTQLWWdlpVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 341 YdeINIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHnTFQLIK 420
Cdd:cd03267 117 Y--LLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV-AQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 421 LFQKRIN--LGQSIFMVTHDDEIIERYPSRRLKISDGALL 458
Cdd:cd03267 194 NFLKEYNreRGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
277-411 |
2.56e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.82 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTK--IKHAAKHMYLVYQNPELQFITNSVYDEI--NIHFNHL 351
Cdd:PRK13635 33 GEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMVLSEetVWDVRRQVGMVFQNPDNQFVGATVQDDVafGLENIGV 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 352 SKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:PRK13635 113 PREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-219 |
2.66e-15 |
|
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: 74.95 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpmkYdelivDPLSGVIFQD--PDSQFCMPKVYEE 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF----------Y-----DPQKGQILIDgiDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 92 LAFVL-----------ENRQVPREDM-DALIINALNMVNLNV----TP---ETYI----KDLSGGMKQKLAIVETILQQS 148
Cdd:cd03254 79 IGVVLqdtflfsgtimENIRLGRPNAtDEEVIEAAKEAGAHDfimkLPngyDTVLgengGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 149 KTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNhVDRVILMDyNGNIIADECPEIILQK 219
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLD-DGKIIEEGTHDELLAK 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
271-459 |
2.85e-15 |
|
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: 74.78 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLeSIMQ--LIKYQGDVYFENQRLTKI------KHAAKHMYLVYQNpelqFitnsvyd 342
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLL-GLLAglDRPTSGTVRLAGQDLFALdedaraRLRARHVGFVFQS----F------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 einihfnhlskdqsddetiQLLKLLD-LENV---------KD------------------QH-PYELSIGQKRRLSVATA 393
Cdd:COG4181 100 -------------------QLLPTLTaLENVmlplelagrRDarararallervglghrlDHyPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 394 LSSKADIIFLDEPTFGLDSHNTFQLIKL-FQKRINLGQSIFMVTHDDEIIERYpSRRLKISDGALLD 459
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLlFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVE 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
250-421 |
2.91e-15 |
|
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: 74.61 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 250 HLLQFKNGRIIRGKStllsfsdLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ----GDVYFENQRLTKIKHAAKHMY 325
Cdd:cd03234 13 AKNWNKYARILNDVS-------LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttsGQILFNGQPRKPDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 326 LVYQNPELQFITnsVYDeiNIHF-------NHLSKDQSDDET-IQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSK 397
Cdd:cd03234 86 VRQDDILLPGLT--VRE--TLTYtailrlpRKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180
....*....|....*....|....
gi 612672732 398 ADIIFLDEPTFGLDSHNTFQLIKL 421
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVST 185
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-210 |
3.07e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.51 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSG---QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlielpmkydELIVDplSGVI-- 75
Cdd:COG1101 1 MLELKNLSKTFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG-------------SLPPD--SGSIli 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 --------------------FQDPDSQFCmpkvyEELAfVLEN--------------RQVPREDMDaLIINALNMVNLNV 121
Cdd:COG1101 66 dgkdvtklpeykrakyigrvFQDPMMGTA-----PSMT-IEENlalayrrgkrrglrRGLTKKRRE-LFRELLATLGLGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 122 tpETYIKD----LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATE---DLWTKLIElwEDQ-TVVIVEHKVKHIWN 193
Cdd:COG1101 139 --ENRLDTkvglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAAlvlELTEKIVE--ENNlTTLMVTHNMEQALD 214
|
250
....*....|....*..
gi 612672732 194 HVDRVILMDyNGNIIAD 210
Cdd:COG1101 215 YGNRLIMMH-EGRIILD 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-457 |
3.22e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 34 LLGPSGCGKSTLLNVLSGIV-PNLIELPMKYDELIvdPLSGV------IFQDPDSQFCMPK--VYEELAFVLENRQVPRE 104
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVpPDSGTLEIGGNPCA--RLTPAkahqlgIYLVPQEPLLFPNlsVKENILFGLPKRQASMQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 105 DMDALIINALNMVNLNVTPETyikdLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELwEDQTVVIV 184
Cdd:PRK15439 120 KMKQLLAALGCQLDLDSSAGS----LEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 185 --EHKVKHIWNHVDRVILM------------DYNGN-IIADECPEIILQKyvhlLSEygvwHPRAWEFAP-----SRVDF 244
Cdd:PRK15439 195 fiSHKLPEIRQLADRISVMrdgtialsgktaDLSTDdIIQAITPAAREKS----LSA----SQKLWLELPgnrrqQAAGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 245 PTTNSHLLQ---FKNgriirgkstlLSFsdlEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHA 320
Cdd:PRK15439 267 PVLTVEDLTgegFRN----------ISL---EVRAGEILGLAGVVGAGRTELAETLYGLRPARgGRIMLNGKEINALSTA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 321 AK-HMYLVYQnPE------------------------LQFITNSVYDE---------INIHFNHLskdqsddetiqllkl 366
Cdd:PRK15439 334 QRlARGLVYL-PEdrqssglyldaplawnvcalthnrRGFWIKPARENavleryrraLNIKFNHA--------------- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 367 ldlenvkDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SHNTFQLIKLFQKRinlGQSIFMVTHDDEIIE 443
Cdd:PRK15439 398 -------EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDvsaRNDIYQLIRSIAAQ---NVAVLFISSDLEEIE 467
|
490
....*....|....
gi 612672732 444 RYPSRRLKISDGAL 457
Cdd:PRK15439 468 QMADRVLVMHQGEI 481
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
251-439 |
3.26e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHA--AKHMYLV 327
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARpDAGEVLWQGEPIRRQRDEyhQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 328 YQnpelqfitNSVYDEI----NIHFNH-LSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:PRK13538 81 HQ--------PGIKTELtaleNLRFYQrLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 403 LDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDD 439
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-186 |
3.88e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSgivpNLIELPMK--------------YDElI 67
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFN----RLLELNEEarvegevrlfgrniYSP-D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 68 VDPLS-----GVIFQDPDSqFCMPKVYEELAFVLE-NRQV-PREDMDALIINALNMVNLNVTPETYIKD----LSGGMKQ 136
Cdd:PRK14267 78 VDPIEvrrevGMVFQYPNP-FPHLTIYDNVAIGVKlNGLVkSKKELDERVEWALKKAALWDEVKDRLNDypsnLSGGQRQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 612672732 137 KLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEH 186
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-208 |
4.08e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 16 RKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpNLIELPMKYDELI---------VDPLS-----GVIFQDPDS 81
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLI-EIYDSKIKVDGKVlyfgkdifqIDAIKlrkevGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 qFCMPKVYEELAFVLENRQVP-REDMDALIINALNMVNLnvTPETYIK------DLSGGMKQKLAIVETILQQSKTLFLD 154
Cdd:PRK14246 102 -FPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 612672732 155 EPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNHVDRVILMdYNGNII 208
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFL-YNGELV 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
267-466 |
4.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIKYQGDvyfENQRLT--KIKHAAKHMY-------LVYQNPELQFIT 337
Cdd:PRK13640 26 ISFS---IPRGSWTALIGHNGSGKSTISKLINGLLLPDDN---PNSKITvdGITLTAKTVWdirekvgIVFQNPDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 338 NSVYDEINIHFNHLSKDQSDDETI--QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIvrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 416 FQLIKL---FQKRINLgqSIFMVTHD-DEiiERYPSRRLKISDGALLDCDGDTNV 466
Cdd:PRK13640 180 EQILKLirkLKKKNNL--TVISITHDiDE--ANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
262-440 |
4.79e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.28 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAAKHMYLVYQNPELqFITNSV 340
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQtSGHIRFHGTDVSRLHARDRKVGFVFQHYAL-FRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 341 YDeiNIHF--------NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:PRK10851 92 FD--NIAFgltvlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190
....*....|....*....|....*....|...
gi 612672732 413 HNTFQLIKLFQKrinLGQ-----SIFmVTHDDE 440
Cdd:PRK10851 170 QVRKELRRWLRQ---LHEelkftSVF-VTHDQE 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-208 |
5.31e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.43 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLL---NVLSGIVPNL-IELPMKYDEL-IVDPLS--- 72
Cdd:PRK14239 5 ILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPEVtITGSIVYNGHnIYSPRTdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ------GVIFQDPDSqFCMpKVYEELAFVLENRQVP-REDMDALIINALnmVNLNVTPEtyIKD--------LSGGMKQK 137
Cdd:PRK14239 83 dlrkeiGMVFQQPNP-FPM-SIYENVVYGLRLKGIKdKQVLDEAVEKSL--KGASIWDE--VKDrlhdsalgLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 138 LAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNHVDRVILMdYNGNII 208
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFF-LDGDLI 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
253-411 |
5.60e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.40 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 253 QFKNGRIIRGkstllsfSDLEIGLGEWITITGANGSGKTTLLESIMQL-------IKYqGDVYFE-----NQRLTKIKHA 320
Cdd:PRK11264 12 KFHGQTVLHG-------IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeqpeagtIRV-GDITIDtarslSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 321 AKHMYLVYQNPELqFITNSVYDEInIHFNHLSKDQSDDETI----QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSS 396
Cdd:PRK11264 84 RQHVGFVFQNFNL-FPHRTVLENI-IEGPVIVKGEPKEEATararELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170
....*....|....*
gi 612672732 397 KADIIFLDEPTFGLD 411
Cdd:PRK11264 162 RPEVILFDEPTSALD 176
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-227 |
6.18e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpSGQRKIfDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlIELPMKyDELIVD--PLSGVI-FQ 77
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-----FEQPTA-GQIMLDgvDLSHVPpYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 78 DP-----DSQFCMP--KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKT 150
Cdd:PRK11607 91 RPinmmfQSYALFPhmTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 151 LFLDEPTAMLDVQATEDLWTKLIELWE--DQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIIlqkYVHLLSEY 227
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAGRIAIMN-RGKFVQIGEPEEI---YEHPTTRY 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-217 |
8.24e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.25 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSgivpnlielpmkydeLIVDPLSGVIFQDPD- 80
Cdd:PRK10253 8 LRGEQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS---------------RLMTPAHGHVWLDGEh 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 -SQFCMPKVYEELAFVLENRQVP------------------------REDMDAlIINALNMVNLNVTPETYIKDLSGGMK 135
Cdd:PRK10253 71 iQHYASKEVARRIGLLAQNATTPgditvqelvargryphqplftrwrKEDEEA-VTKAMQATGITHLADQSVDTLSGGQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECP 213
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRYASHLIALR-EGKIVAQGAP 228
|
....
gi 612672732 214 EIIL 217
Cdd:PRK10253 229 KEIV 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
252-454 |
8.33e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.18 E-value: 8.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGkstllsfSDLEIGLGEWITITGANGSGKTTLLESIMQLI------KYQGDVYFENQRLTK--IKHAAKH 323
Cdd:PRK14247 11 VSFGQVEVLDG-------VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeaRVSGEVYLDGQDIFKmdVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 324 MYLVYQNPELqfITN-SVYDEI--NIHFNHLSKDQSD-DETIQ--LLKLLDLENVKDQ--HPY-ELSIGQKRRLSVATAL 394
Cdd:PRK14247 84 VQMVFQIPNP--IPNlSIFENValGLKLNRLVKSKKElQERVRwaLEKAQLWDEVKDRldAPAgKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 395 SSKADIIFLDEPTFGLDSHNTFQLIKLFQKrINLGQSIFMVTHddeiierYPSRRLKISD 454
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLE-LKKDMTIVLVTH-------FPQQAARISD 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
280-442 |
9.65e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.45 E-value: 9.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 280 ITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTK--IKHAAKHMYLVYQNPELQFITNSVYDEINIHFNHLSKDQs 356
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKenIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 357 ddETI-----QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIkLFQKRI--NLG 429
Cdd:PRK13652 112 --ETVahrvsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLpeTYG 188
|
170
....*....|...
gi 612672732 430 QSIFMVTHDDEII 442
Cdd:PRK13652 189 MTVIFSTHQLDLV 201
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
262-440 |
9.77e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.85 E-value: 9.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLT-------KIKHAAKH--------MY 325
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNGQTINlvrdkdgQLKVADKNqlrllrtrLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 326 LVYQNPELQFITNSVYD--EINIHFNHLSKDQSDDETIQLLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENvmEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 612672732 403 LDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDE 440
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-218 |
1.31e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.87 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPsGQRKIFDhlnITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlieLPMKYDELIVD----------- 69
Cdd:COG3840 1 MLRLDDLTYRYG-DFPLRFD---LTIAAGERVAILGPSGAGKSTLLNLIAGF------LPPDSGRILWNgqdltalppae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 -PLSgVIFQDpDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtpeTYIKD-----LSGGMKQKLAIVET 143
Cdd:COG3840 71 rPVS-MLFQE-NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGL-----AGLLDrlpgqLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 144 ILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEH---KVKHIwnhVDRVILMDyNGNIIADECPEIILQ 218
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHdpeDAARI---ADRVLLVA-DGRIAADGPTAALLD 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-201 |
1.70e-14 |
|
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: 72.31 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVI-FQDPD 80
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL---------------PDSGEVlFDGKP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 SQFC-------MP---------KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETI 144
Cdd:cd03269 64 LDIAarnrigyLPeerglypkmKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 145 LQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIWNHVDRVILM 201
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLL 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-214 |
2.49e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 15 QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNlIELPMKYDELIVDPL----------------SGVIFQd 78
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITG-DKSAGSHIELLGRTVqregrlardirksranTGYIFQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 pdsQFcmpKVYEELAfVLENRQV-----------------PREDMDALiiNALNMVNLNVTPETYIKDLSGGMKQKLAIV 141
Cdd:PRK09984 94 ---QF---NLVNRLS-VLENVLIgalgstpfwrtcfswftREQKQRAL--QALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 142 ETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPE 214
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALR-QGHVFYDGSSQ 238
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-201 |
3.20e-14 |
|
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: 71.56 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 21 HLNITIQDKEKVL-LLGPSGCGKSTLLNVLSGIvpnlielpMKYDELIVDpLSGVIFQDPDSQFCMP------------- 86
Cdd:cd03297 14 TLKIDFDLNEEVTgIFGASGAGKSTLLRCIAGL--------EKPDGGTIV-LNGTVLFDSRKKINLPpqqrkiglvfqqy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 87 ------KVYEELAFVL------ENRQVPREDMDALIINALNmvnlnvtpETYIKDLSGGMKQKLAIVETILQQSKTLFLD 154
Cdd:cd03297 85 alfphlNVRENLAFGLkrkrnrEDRISVDELLDLLGLDHLL--------NRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 155 EPTAMLDVQATEDLWTKLIELWED--QTVVIVEHKVKHIWNHVDRVILM 201
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-208 |
3.33e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQrKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIELPmKYDELIVdplSGVIF---QD 78
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVL-----NLLEMP-RSGTLNI---AGNHFdfsKT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 PDsqfcmPKVYEEL------AF----------VLEN------------RQVPREDMDALiinaLNMVNLNVTPETYIKDL 130
Cdd:PRK11124 72 PS-----DKAIRELrrnvgmVFqqynlwphltVQQNlieapcrvlglsKDQALARAEKL----LERLRLKPYADRFPLHL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 131 SGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ-TVVIVEHKVKHIWNHVDRVILMDyNGNII 208
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTASRVVYME-NGHIV 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-199 |
4.55e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.28 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 7 LRLK---YPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNvlsgIVPNLIElpmkydelivdPLSG-VIFQDPDSQ 82
Cdd:PRK10247 8 LQLQnvgYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLK----IVASLIS-----------PTSGtLLFEGEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 83 FCMPK-------------------VYEELAFVLENRQVpREDMDALiINALNMVNLnvtPETY----IKDLSGGMKQKLA 139
Cdd:PRK10247 73 TLKPEiyrqqvsycaqtptlfgdtVYDNLIFPWQIRNQ-QPDPAIF-LDDLERFAL---PDTIltknIAELSGGEKQRIS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 140 IVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVI--VEHKVKHIwNHVDRVI 199
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEI-NHADKVI 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-207 |
5.15e-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: 69.88 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPN---LIELPmkydelivdPLSGVIFqd 78
Cdd:cd03223 1 IELENLSLATPDGRVLLKD-LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgsgRIGMP---------EGEDLLF-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 pdsqfcMPkvyeelafvlenrQVP-------REdmdaLIINALNMVnlnvtpetyikdLSGGMKQKLAIVETILQQSKTL 151
Cdd:cd03223 69 ------LP-------------QRPylplgtlRE----QLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 152 FLDEPTAMLDVQaTEDlwtKLIELWEDQ--TVVIVEHKvKHIWNHVDRVILMDYNGNI 207
Cdd:cd03223 114 FLDEATSALDEE-SED---RLYQLLKELgiTVISVGHR-PSLWKFHDRVLDLDGEGGW 166
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-217 |
5.22e-14 |
|
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: 71.56 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSgivpNLIElpmkydelivdPLSGVIF----- 76
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN----RLIE-----------PTSGEIFidged 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 ---QDP-----------DSQFCMP--KVYEELAFVLENRQVPREDMDALIINALNMVNLNvtPET----YIKDLSGGMKQ 136
Cdd:cd03295 65 ireQDPvelrrkigyviQQIGLFPhmTVEENIALVPKLLKWPKEKIRERADELLALVGLD--PAEfadrYPHELSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 137 KLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED--QTVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPE 214
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIM-KNGEIVQVGTPD 221
|
...
gi 612672732 215 IIL 217
Cdd:cd03295 222 EIL 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
271-457 |
5.26e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.91 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIK-----HAAKHMYLVYQnpelqfitnsvydei 344
Cdd:PRK11153 25 SLHIPAGEIFGVIGASGAGKSTLIRCINLLERpTSGRVLVDGQDLTALSekelrKARRQIGMIFQ--------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 niHFNHLS------------------KDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEP 406
Cdd:PRK11153 90 --HFNLLSsrtvfdnvalplelagtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 612672732 407 TFGLDSHNTFQLIKLFqKRIN--LGQSIFMVTHDDEIIERYPSRRLKISDGAL 457
Cdd:PRK11153 168 TSALDPATTRSILELL-KDINreLGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-208 |
6.03e-14 |
|
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: 70.27 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 13 SGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLIelpmkydelivdpLSGVIFQD--PDSQFCMPKVYe 90
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG-------------VSGEVLINgrPLDKRSFRKII- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 91 elAFvlenrqVPREDM--------DALIINALnmvnlnvtpetyIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDV 162
Cdd:cd03213 85 --GY------VPQDDIlhptltvrETLMFAAK------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 612672732 163 QATEDLWTKLIELWEDQ-TVVIVEHKVKH-IWNHVDRVILMDyNGNII 208
Cdd:cd03213 145 SSALQVMSLLRRLADTGrTIICSIHQPSSeIFELFDKLLLLS-QGRVI 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
262-437 |
6.56e-14 |
|
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: 70.32 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAAKHMYLVYQNPELqfitnsv 340
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQKNIEALRRIGALIEAPGF------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 341 YDEI----NIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTF 416
Cdd:cd03268 84 YPNLtareNLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180
....*....|....*....|.
gi 612672732 417 QLIKLFQKRINLGQSIFMVTH 437
Cdd:cd03268 164 ELRELILSLRDQGITVLISSH 184
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
252-455 |
6.89e-14 |
|
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: 70.39 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTkIKHAAKHMYL---- 326
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILpDSGEVLFDGKPLD-IAARNRIGYLpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 327 -VYQNPELQfitnsvydEINIHFNHL---SKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:cd03269 80 gLYPKMKVI--------DQLVYLAQLkglKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 612672732 403 LDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-200 |
7.16e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.96 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 11 YPSgqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIFQDPDSQfcmpkvye 90
Cdd:NF040873 2 YGG--RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR---------------PTSGTVRRAGGAR-------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 91 eLAFVLENRQVP--------------------------REDmDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETI 144
Cdd:NF040873 57 -VAYVPQRSEVPdslpltvrdlvamgrwarrglwrrltRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 145 LQQSKTLFLDEPTAMLDVQATEDLwTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVIL 200
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERI-IALLAEEHARgaTVVVVTHDLELVRRADPCVLL 191
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
271-458 |
7.24e-14 |
|
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: 72.04 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQG--------DVyfenqrltkIKHAAK---HMYLVYQNPelqfitnS 339
Cdd:TIGR01188 13 NFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSgtarvagyDV---------VREPRKvrrSIGIVPQYA-------S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 340 VYDEINIHFN--------HLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:TIGR01188 77 VDEDLTGRENlemmgrlyGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 612672732 412 SHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALL 458
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
271-438 |
7.65e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQL--IKyQGDVYFENQRLTKIKHAAKHMYLVYQN----PELqfitnSVYDei 344
Cdd:PRK11000 23 NLDIHEGEFVVFVGPSGCGKSTLLRMIAGLedIT-SGDLFIGEKRMNDVPPAERGVGMVFQSyalyPHL-----SVAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 NIHFN----HLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL-- 418
Cdd:PRK11000 95 NMSFGlklaGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMri 174
|
170 180
....*....|....*....|.
gi 612672732 419 -IKLFQKRinLGQSIFMVTHD 438
Cdd:PRK11000 175 eISRLHKR--LGRTMIYVTHD 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-161 |
8.01e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlIELPMKYDELI-------VDPLS---GVIFQdpdSQF 83
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-----LEDITSGDLFIgekrmndVPPAErgvGMVFQ---SYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 84 CMP--KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLD 161
Cdd:PRK11000 86 LYPhlSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
265-455 |
8.02e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.69 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 265 TLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY---------QGDVYFENQR----LTKIKHAakhmyLVYQNP 331
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgsgriarpaGARVLFLPQRpylpLGTLREA-----LLYPAT 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 332 ELQFitnsvydeinihfnhlskdqSDDETIQLLKLLDLENVKDQH------PYELSIGQKRRLSVATALSSKADIIFLDE 405
Cdd:COG4178 452 AEAF--------------------SDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 612672732 406 PTFGLDSHNTFQLIKLFQKRinLGQSIFM-VTHDDEiIERYPSRRLKISDG 455
Cdd:COG4178 512 ATSALDEENEAALYQLLREE--LPGTTVIsVGHRST-LAAFHDRVLELTGD 559
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-210 |
9.04e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 17 KIFDHLNITIQDKEKVLLLGPSGCGKSTL---LNVLsgIVPNLIELPMKY----------------DELIVDPLS----- 72
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNAL--LLPDTGTIEWIFkdeknkkktkekekvlEKLVIQKTRfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ---------GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtPETYIK----DLSGGMKQKLA 139
Cdd:PRK13651 99 kikeirrrvGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL---DESYLQrspfELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 140 IVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIWNHVDRVILMDyNGNIIAD 210
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFK-DGKIIKD 246
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-436 |
9.22e-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: 73.32 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNlielpMKYD-ELIVD--PLSGVIFQDPDSQfCMPKVYE 90
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH-----GTWDgEIYWSgsPLKASNIRDTERA-GIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 91 ELAF-----VLEN--------RQVPREDMDALIINALNM---VNLNVTPET-YIKDLSGGMKQKLAIVETILQQSKTLFL 153
Cdd:TIGR02633 86 ELTLvpelsVAENiflgneitLPGGRMAYNAMYLRAKNLlreLQLDADNVTrPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 154 DEPTAMLDVQATEDLWTKLIELWEDQTVVI-VEHKVKHIWNHVDRVILMDyNGNIIADE------CPEIILQK------- 219
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVyISHKLNEVKAVCDTICVIR-DGQHVATKdmstmsEDDIITMMvgreits 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 220 -YVHLLSEYG-----VWHPRAWEfapsrvdfpTTNSHLLQFKNgriirgkstlLSFSdleIGLGEWITITGANGSGKTTL 293
Cdd:TIGR02633 245 lYPHEPHEIGdvileARNLTCWD---------VINPHRKRVDD----------VSFS---LRRGEILGVAGLVGAGRTEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 294 LESIMQLI--KYQGDVYFeNQRLTKIKHAAKHM----YLVYQN-------PEL---QFITNSVYDEIN--IHFNHLSKDQ 355
Cdd:TIGR02633 303 VQALFGAYpgKFEGNVFI-NGKPVDIRNPAQAIragiAMVPEDrkrhgivPILgvgKNITLSVLKSFCfkMRIDAAAELQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 356 SDDETIQLLKlldlenVKDQHPY----ELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQS 431
Cdd:TIGR02633 382 IIGSAIQRLK------VKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVA 455
|
....*
gi 612672732 432 IFMVT 436
Cdd:TIGR02633 456 IIVVS 460
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-210 |
9.47e-14 |
|
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: 70.09 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDL--RLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlielpmkydelivDPLSGVIFQD 78
Cdd:cd03266 1 MITADALtkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL---------------EPDAGFATVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 ------------------PDSQfcmpKVYEELAfVLENRQ-------VPREDMDALIINALNMVNLNVTPETYIKDLSGG 133
Cdd:cd03266 66 gfdvvkepaearrrlgfvSDST----GLYDRLT-ARENLEyfaglygLKGDELTARLEELADRLGMEELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 134 MKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVE-HKVKHIWNHVDRVILMdYNGNIIAD 210
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERLCDRVVVL-HRGRVVYE 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-198 |
1.01e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 20 DHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielP----MKYDELIVDPLS---------GVIFQDPdsqfcM- 85
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ-----PdsgeILIDGKPVRIRSprdaialgiGMVHQHF-----Ml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 86 -PK--VYEELAFVLENRQVPREDMDALI--INAL-NMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAM 159
Cdd:COG3845 92 vPNltVAENIVLGLEPTKGGRLDRKAARarIRELsERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 160 LDVQATEDLWTKLIELWEDQ-TVVIVEHK---VKHIwnhVDRV 198
Cdd:COG3845 172 LTPQEADELFEILRRLAAEGkSIIFITHKlreVMAI---ADRV 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-186 |
1.13e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFdhlnitiqdkekvllLGPSGCGKSTLL---NVLSGIVPNL-IELPMKY-DELI----VDPLS 72
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAF---------------IGPSGCGKSTILrcfNRLNDLIPGFrVEGKVTFhGKNLyapdVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -----GVIFQDPDSqfcMPK-VYEELAFVlenrqvPR-----EDMDALIINALNMVNLNVTPETYIKD----LSGGMKQK 137
Cdd:PRK14243 89 vrrriGMVFQKPNP---FPKsIYDNIAYG------ARingykGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 138 LAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEH 186
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
252-455 |
1.26e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.17 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGkSTLLSFsDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHMYLVYQN 330
Cdd:COG3840 2 LRLDDLTYRYG-DFPLRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPpDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 331 PELqFITNSVYDEINIHFN---HLSKDQSdDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPT 407
Cdd:COG3840 80 NNL-FPHLTVAQNIGLGLRpglKLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 612672732 408 FGLD---SHNTFQLIKLFQKRINLgqSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:COG3840 158 SALDpalRQEMLDLVDELCRERGL--TVLMVTHDPEDAARIADRVLLVADG 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
246-438 |
1.60e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.67 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 246 TTNSHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHM 324
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGEDVTHRSIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 325 YLVYQNPELqFITNSVYDEI--NIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:PRK11432 81 CMVFQSYAL-FPHMSLGENVgyGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 612672732 403 LDEPTFGLDSH---NTFQLIKLFQKRINLgQSIFmVTHD 438
Cdd:PRK11432 160 FDEPLSNLDANlrrSMREKIRELQQQFNI-TSLY-VTHD 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-207 |
1.72e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnliELPmKYDELIVD--PLSGV----- 74
Cdd:PRK11247 13 LLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-----ETP-SAGELLAGtaPLAEAredtr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 75 -IFQDPDsqfCMP--KVYEELAFVLENRQVPRedmdALiiNALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:PRK11247 85 lMFQDAR---LLPwkKVIDNVGLGLKGQWRDA----AL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 152 FLDEPTAMLDVqATEDLWTKLIE-LWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNI 207
Cdd:PRK11247 156 LLDEPLGALDA-LTRIEMQDLIEsLWQQHgfTVLLVTHDVSEAVAMADRVLLIE-EGKI 212
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
270-444 |
2.10e-13 |
|
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: 68.79 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 270 SDLEIGLGEWIT-ITGANGSGKTTLLESI-------MQLIKYQG----DVYFENQRLTKIK----HAAKHMYLVYQNPEL 333
Cdd:cd03240 14 ERSEIEFFSPLTlIVGQNGAGKTTIIEALkyaltgeLPPNSKGGahdpKLIREGEVRAQVKlafeNANGKKYTITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 334 qfITNSVYdeinIHfnhlsKDQSDdetiqllKLLDLenvkdqHPYELSIGQKR------RLSVATALSSKADIIFLDEPT 407
Cdd:cd03240 94 --LENVIF----CH-----QGESN-------WPLLD------MRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 408 FGLDSHN-TFQLIKLFQKRinLGQSIF---MVTHDDEIIER 444
Cdd:cd03240 150 TNLDEENiEESLAEIIEER--KSQKNFqliVITHDEELVDA 188
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
271-437 |
2.65e-13 |
|
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: 69.18 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAA--KHMYLVYQNPELqfITNSVYDeiNIH 347
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSlrSMIGVVLQDTFL--FSGTIME--NIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 348 FNHLSKDqsDDETIQLLKLL-------DLENVKDQHPYE----LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHnTF 416
Cdd:cd03254 99 LGRPNAT--DEEVIEAAKEAgahdfimKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTE-TE 175
|
170 180
....*....|....*....|.
gi 612672732 417 QLIKLFQKRINLGQSIFMVTH 437
Cdd:cd03254 176 KLIQEALEKLMKGRTSIIIAH 196
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-208 |
3.00e-13 |
|
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: 69.18 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 5 SDLRLKYPSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLL-------NVLSGIVpnLI------ELPMKY--DELIVD 69
Cdd:cd03253 4 ENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILrllfrfyDVSSGSI--LIdgqdirEVTLDSlrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 PLSGVIFQDPdsqfcmpkvyeelafVLENRQVPREDM-DALIINA----------LNMvnlnvtPETY--------IKdL 130
Cdd:cd03253 81 PQDTVLFNDT---------------IGYNIRYGRPDAtDEEVIEAakaaqihdkiMRF------PDGYdtivgergLK-L 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 131 SGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNhVDRVILMDyNGNII 208
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLK-DGRIV 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
271-443 |
3.58e-13 |
|
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: 67.07 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTK--IKHAAKH-MYLVYQnpelqfitnsvydeini 346
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVDGKEVSFasPRDARRAgIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 347 hfnhlskdqsddetiqllklldlenvkdqhpyeLSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRI 426
Cdd:cd03216 83 ---------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLR 129
|
170
....*....|....*...
gi 612672732 427 NLGQSIFMVTHD-DEIIE 443
Cdd:cd03216 130 AQGVAVIFISHRlDEVFE 147
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-209 |
3.80e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 22 LNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP----------NLIELPMKydELIVdpLSGVIFQDPDSQFCMPkVYEE 91
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiqfagqPLEAWSAA--ELAR--HRAYLSQQQTPPFAMP-VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 92 LAFVLENRQVPREDMDAL--IINALNMVNLNVTPetyIKDLSGGMKQKLAIVETILQ-------QSKTLFLDEPTAMLDV 162
Cdd:PRK03695 90 LTLHQPDKTRTEAVASALneVAEALGLDDKLGRS---VNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 163 qATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIA 209
Cdd:PRK03695 167 -AQQAALDRLLSELCQQgiAVVMSSHDLNHTLRHADRVWLLK-QGKLLA 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
271-437 |
4.23e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.35 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQL-IKYQGDVYFEN------QRLTKIKHAAKhmyLVYQNPELQFITNSVYDE 343
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALlIPSEGKVYVDGldtsdeENLWDIRNKAG---MVFQNPDNQIVATIVEED 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INIHFNHLSKDQSD-----DETiqlLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:PRK13633 107 VAFGPENLGIPPEEirervDES---LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180
....*....|....*....|.
gi 612672732 419 IKLFqKRIN--LGQSIFMVTH 437
Cdd:PRK13633 184 VNTI-KELNkkYGITIILITH 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
271-457 |
4.34e-13 |
|
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: 68.17 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQG--------DVYFENqrlTKIKhaaKHMYLVYQNPELQFITnSVYD 342
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSgratvaghDVVREP---REVR---RRIGIVFQDLSVDDEL-TGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EINIH--FNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL-- 418
Cdd:cd03265 93 NLYIHarLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVwe 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 419 -IKLFQKRINLgqSIFMVTHDDEIIERYPSRRLKISDGAL 457
Cdd:cd03265 173 yIEKLKEEFGM--TILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
277-439 |
4.71e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHA-AKHMYLVYQ----NPELQFITNSVYDeinIHFNh 350
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQSIKKDLCTyQKQLCFVGHrsgiNPYLTLRENCLYD---IHFS- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 351 lskdQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQ 430
Cdd:PRK13540 103 ----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGG 178
|
....*....
gi 612672732 431 SIFMVTHDD 439
Cdd:PRK13540 179 AVLLTSHQD 187
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
272-444 |
7.22e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.52 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQL------IKYQGDVYFENQ----RLTKIKHAAKHMYLVYQNPELqfITNSVY 341
Cdd:PRK14258 28 MEIYQSKVTAIIGPSGCGKSTFLKCLNRMneleseVRVEGRVEFFNQniyeRRVNLNRLRRQVSMVHPKPNL--FPMSVY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DEINIHFNHLS---KDQSDDETIQLLKLLDL-ENVKDQ---HPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHN 414
Cdd:PRK14258 106 DNVAYGVKIVGwrpKLEIDDIVESALKDADLwDEIKHKihkSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIA 185
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 415 TFQLIKLFQK-RINLGQSIFMVTHDDEIIER 444
Cdd:PRK14258 186 SMKVESLIQSlRLRSELTMVIVSHNLHQVSR 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
271-443 |
7.31e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLlesimqlIK-----YQ---GDVYFENQ--RLTKIKHAAKH-MYLVYQnpELQFITN- 338
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTL-------MKilsgvYQpdsGEILLDGEpvRFRSPRDAQAAgIAIIHQ--ELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 339 SVYDeiNIHFNHLSK-----DQSD--DETIQLLKLLDLE-----NVKDqhpyeLSIGQKRRLSVATALSSKADIIFLDEP 406
Cdd:COG1129 95 SVAE--NIFLGREPRrggliDWRAmrRRARELLARLGLDidpdtPVGD-----LSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 407 TFGLDSHNT---FQLIKLFQKRinlGQSIFMVTHD-DEIIE 443
Cdd:COG1129 168 TASLTEREVerlFRIIRRLKAQ---GVAIIYISHRlDEVFE 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
242-461 |
7.60e-13 |
|
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: 67.56 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 242 VDFPTTNSHLLQFKNGRIIRGKSTLLSFS-----DLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVyfenQRLT 315
Cdd:cd03220 8 KSYPTYKGGSSSLKKLGILGRKGEVGEFWalkdvSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTV----TVRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 316 KIkhAAKHMYLVYQNPELqfitnSVYDeiNIHFNH----LSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVA 391
Cdd:cd03220 84 RV--SSLLGLGGGFNPEL-----TGRE--NIYLNGrllgLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 392 TALSSKADIIFLDEPTFGLDSHntFQL--IKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDCD 461
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAA--FQEkcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
262-438 |
7.97e-13 |
|
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: 70.47 E-value: 7.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHA--AKHMYLVYQNPELqFITn 338
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDpLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHL-FDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 339 SVYDEINIHfnhlSKDQSDDETIQLL---KLLD--------LENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPT 407
Cdd:TIGR02868 424 TVRENLRLA----RPDATDEELWAALervGLADwlralpdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|..
gi 612672732 408 FGLDSHNTFQLIK-LFQkrINLGQSIFMVTHD 438
Cdd:TIGR02868 500 EHLDAETADELLEdLLA--ALSGRTVVLITHH 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-213 |
9.51e-13 |
|
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: 67.52 E-value: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 6 DLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-----------NLIELPMKY--DELIVDPLS 72
Cdd:cd03244 7 NVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVElssgsilidgvDISKIGLHDlrSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 GVIFQ-------DPDSQFcmpkVYEELAFVLENRQvpredMDALIINALNMVNLNVTPETyiKDLSGGMKQKLAIVETIL 145
Cdd:cd03244 87 PVLFSgtirsnlDPFGEY----SDEELWQALERVG-----LKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 146 QQSKTLFLDEPTAMLDVQaTEDLWTKLIELW-EDQTVVIVEHKVKHIWnHVDRVILMDyNGNIIADECP 213
Cdd:cd03244 156 RKSKILVLDEATASVDPE-TDALIQKTIREAfKDCTVLTIAHRLDTII-DSDRILVLD-KGRVVEFDSP 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-219 |
9.89e-13 |
|
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: 68.05 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 21 HLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-------------------NLIELPMKYdelivdplSGVIFQdpdS 81
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEptsgkvlidgqdiaamsrkELRELRRKK--------ISMVFQ---S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFCMPK--VYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAM 159
Cdd:cd03294 111 FALLPHrtVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 160 LDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQK 219
Cdd:cd03294 191 LDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMK-DGRLVQVGTPEEILTN 251
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
262-438 |
1.11e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKI--KHAAKHMYLVYQN---PELQF 335
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLssRQLARRLALLPQHhltPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 336 ITNSVYDEINIHFNHLSKDQSDDETI--QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSH 413
Cdd:PRK11231 93 VRELVAYGRSPWLSLWGRLSAEDNARvnQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
|
170 180
....*....|....*....|....*
gi 612672732 414 NTFQLIKLFQKRINLGQSIFMVTHD 438
Cdd:PRK11231 173 HQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
271-440 |
1.17e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.09 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVY---FENQRLTKIKHAAKHMYLVYQNPELQFITNSVYDEINI 346
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLvsgIDTGDFSKLQGIRKLVGIVFQNPETQFVGRTVEEDLAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 347 HFNHLSKdqsddETIQLLKLLD-------LENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLI 419
Cdd:PRK13644 102 GPENLCL-----PPIEIRKRVDralaeigLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180
....*....|....*....|.
gi 612672732 420 KLFQKRINLGQSIFMVTHDDE 440
Cdd:PRK13644 177 ERIKKLHEKGKTIVYITHNLE 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-207 |
1.26e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnliELPmkydelivdPLSGVIFQ--- 77
Cdd:COG0488 315 VLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG------ELE---------PDSGTVKLget 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 78 -------------DPDSqfcmpKVYEELafvlenRQVPREDMDALIINALNmvNLNVTPE---TYIKDLSGGMKQKLAIV 141
Cdd:COG0488 378 vkigyfdqhqeelDPDK-----TVLDEL------RDGAPGGTEQEVRGYLG--RFLFSGDdafKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 142 ETILQQSKTLFLDEPTAMLDVQATEDLwTKLIELWEDqTVVIVEH------KVkhiwnhVDRVILM------DYNGNI 207
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEAL-EEALDDFPG-TVLLVSHdryfldRV------ATRILEFedggvrEYPGGY 514
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
271-411 |
1.65e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.98 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKI---KHAAKHM-YLVyQNP----ELqfitnSVY 341
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKpDSGRIFLDGEDITHLpmhKRARLGIgYLP-QEAsifrKL-----TVE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 342 DeiNI----HFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:COG1137 97 D--NIlavlELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-208 |
1.71e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 10 KYPSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIELP---------------MKYDELIVDPLS-- 72
Cdd:COG4161 10 CFYGSHQALFD-INLECPSGETLVLLGPSGAGKSSLLRVL-----NLLETPdsgqlniaghqfdfsQKPSEKAIRLLRqk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQdpdsQF-------CMPKVYEELAFVLE-NRQVPREDMDALiinaLNMVNLNVTPETYIKDLSGGMKQKLAIVET 143
Cdd:COG4161 84 vGMVFQ----QYnlwphltVMENLIEAPCKVLGlSKEQAREKAMKL----LARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 144 ILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ-TVVIVEHKVKHIWNHVDRVILMDyNGNII 208
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKVASQVVYME-KGRII 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-213 |
1.81e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PN-----LIELPMKYDELIVDPLSGVI 75
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThPDagsisLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 FQ----DPDSQfcmpkVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTL 151
Cdd:PRK13537 86 PQfdnlDPDFT-----VRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 152 FLDEPTAMLDVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECP 213
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLCDRLCVIE-EGRKIAEGAP 222
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-222 |
1.89e-12 |
|
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: 66.62 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 20 DHLNITIQDKEKVLLLGPSGCGKS-TLLNVLSGIVPNLIEL--PMKYDELIVDPLS------GVIFQDPDSQFC-MPKVY 89
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPGLTQTsgEILLDGRPLLPLSirgrhiATIMQNPRTAFNpLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 90 EELAFVLENRQVPREDMDALIINALNMVNLNVTPE---TYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATE 166
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 167 DLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQKYVH 222
Cdd:TIGR02770 163 RVLKLLRELRQLFgtGILLITHDLGVVARIADEVAVMD-DGRIVERGTVKEIFYNPKH 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
252-443 |
1.92e-12 |
|
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: 66.01 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY---QGDVYFENQRLTKIK---HAAKHMY 325
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevtEGEILFKGEDITDLPpeeRARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 326 LVYQNPelqfitnsvydeinihfnhlskdqsddETIQLLKLLD-LENVKdqhpYELSIGQKRRLSVATALSSKADIIFLD 404
Cdd:cd03217 81 LAFQYP---------------------------PEIPGVKNADfLRYVN----EGFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 612672732 405 EPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIE 443
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLD 168
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-227 |
2.24e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 16 RKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-NLIELPMKYDELIVDPLS-------GVIFQDPdSQFCMPK 87
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDEDISLLPLHararrgiGYLPQEA-SIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 88 VYEELAFVLENR----QVPREDMDALIINALNMVNLNvtpETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ 163
Cdd:PRK10895 95 VYDNLMAVLQIRddlsAEQREDRANELMEEFHIEHLR---DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 164 ATEDLwTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQ----KYVHLLSEY 227
Cdd:PRK10895 172 SVIDI-KRIIEHLRDSglGVLITDHNVRETLAVCERAYIVS-QGHLIAHGTPTEILQdehvKRVYLGEDF 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
254-411 |
2.63e-12 |
|
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: 65.68 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 254 FKNGRIIRGKStllsfsdLEIGLGEWiTITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHM--YLvyqn 330
Cdd:cd03264 10 YGKKRALDGVS-------LTLGPGMY-GLLGPNGAGKTTLMRILATLTPpSSGTIRIDGQDVLKQPQKLRRRigYL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 331 PElqfiTNSVYDEINI--HFNHL------SKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:cd03264 78 PQ----EFGVYPNFTVreFLDYIawlkgiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
....*....
gi 612672732 403 LDEPTFGLD 411
Cdd:cd03264 154 VDEPTAGLD 162
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-205 |
2.64e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.57 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHL---NITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnliELPMKYDELIVDP-------- 70
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLkdiNLEVPKGELVAIVGPVGSGKSSLLSALLG------ELEKLSGSVSVPGsiayvsqe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 ---LSG-----VIFQDP-DSQFcmpkvYEElafVLENRQVpREDMDALiinalnmvnlnvtP---ETYIKD----LSGGM 134
Cdd:cd03250 75 pwiQNGtirenILFGKPfDEER-----YEK---VIKACAL-EPDLEIL-------------PdgdLTEIGEkginLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 135 KQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLI--ELWEDQTVVIVEHKVKHIWnHVDRVILMDyNG 205
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQLQLLP-HADQIVVLD-NG 203
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-231 |
2.92e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSG---QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP--------NLIELPMKYDELIVDP 70
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpttgtvtvDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 LS---GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNL--NVTPETYIKdLSGGMKQKLAIVETIL 145
Cdd:PRK13646 83 VRkriGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsrDVMSQSPFQ-MSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 146 QQSKTLFLDEPTAMLDVQATEDLWT--KLIELWEDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQKYVHL 223
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRllKSLQTDENKTIILVSHDMNEVARYADEVIVMK-EGSIVSQTSPKELFKDKKKL 240
|
....*...
gi 612672732 224 LSeygvWH 231
Cdd:PRK13646 241 AD----WH 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
272-455 |
4.09e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.81 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQL-IKYQGDVYFENQRL--------TKIKHAAKHMYLVYQN----PELQFITN 338
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPRSGTLNIAGNHFdfsktpsdKAIRELRRNVGMVFQQynlwPHLTVQQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 339 SVydEINIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:PRK11124 103 LI--EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQI 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 419 IKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:PRK11124 181 VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
271-437 |
4.13e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.18 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIM-QLIKYQGDVYFenqrltkikhaAKHMYLVYQNPELQfiTNSVYDeiNIHFN 349
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSV-----------PGSIAYVSQEPWIQ--NGTIRE--NILFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 350 HLSKDQSDDETIQLLKLL-DLENVKDQHPYE-------LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHnTFQLI-- 419
Cdd:cd03250 90 KPFDEERYEKVIKACALEpDLEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH-VGRHIfe 168
|
170
....*....|....*...
gi 612672732 420 KLFQKRINLGQSIFMVTH 437
Cdd:cd03250 169 NCILGLLLNNKTRILVTH 186
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-161 |
4.21e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIfDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG---IVPNLIELpmkyDELIVDPLS----- 72
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVI-KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGlerITSGEIWI----GGRVVNELEpadrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVIFQD----PDsqfcMpKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtpETYIK----DLSGGMKQKLAIVET 143
Cdd:PRK11650 78 iAMVFQNyalyPH----M-SVRENMAYGLKIRGMPKAEIEERVAEAARILEL----EPLLDrkprELSGGQRQRVAMGRA 148
|
170
....*....|....*...
gi 612672732 144 ILQQSKTLFLDEPTAMLD 161
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-189 |
5.01e-12 |
|
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: 68.40 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVL------------SGIVPNLIELPMKYDELIVD 69
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstegeiqiDGVSWNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 PLSGVIFQ-------DPDSQFC---MPKVYEELAFVLENRQVPredmdaliinalNMVNLNVTPETYIkdLSGGMKQKLA 139
Cdd:TIGR01271 1298 PQKVFIFSgtfrknlDPYEQWSdeeIWKVAEEVGLKSVIEQFP------------DKLDFVLVDGGYV--LSNGHKQLMC 1363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 612672732 140 IVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVK 189
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
242-437 |
5.12e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 242 VDFPTTNSH-----LLQFKNgriirgkstlLSFS------------DLEIGLGEWITITGANGSGKTTLLesimQLIKY- 303
Cdd:PRK11160 324 VTFPTTSTAaadqvSLTLNN----------VSFTypdqpqpvlkglSLQIKAGEKVALLGRTGCGKSTLL----QLLTRa 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 304 ----QGDVYFENQRLTKIKHAA--KHMYLVYQNPELqfitnsvydeinihFNH-------LSKDQSDDET-IQLLKLLDL 369
Cdd:PRK11160 390 wdpqQGEILLNGQPIADYSEAAlrQAISVVSQRVHL--------------FSAtlrdnllLAAPNASDEAlIEVLQQVGL 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 370 EN-VKDQHPYE---------LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINlGQSIFMVTH 437
Cdd:PRK11160 456 EKlLEDDKGLNawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-210 |
5.13e-12 |
|
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: 65.43 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 20 DHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PN------LIELPMKYDELIVDPLSGVIFQDPDSQFCMPkVYEEL 92
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTsgevrvAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLP-VIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 93 AFVLENRQVP----REDMDALIinalNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDL 168
Cdd:cd03267 117 YLLAAIYDLPparfKKRLDELS----ELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 612672732 169 WTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDYnGNIIAD 210
Cdd:cd03267 193 RNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDK-GRLLYD 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
252-455 |
5.30e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.37 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQL-------IKYQGDVYFENQRltkikHAAKHM 324
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLthpdagsISLCGEPVPSRAR-----HARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 325 YLVYQ----NPELQFITNSVydeINIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADI 400
Cdd:PRK13537 83 GVVPQfdnlDPDFTVRENLL---VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 401 IFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
271-445 |
7.16e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.40 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKT-TLLeSIMQL-----IKYQGDVYFENQRLTKIKHAA------KHMYLVYQ------NPe 332
Cdd:COG4172 30 SFDIAAGETLALVGESGSGKSvTAL-SILRLlpdpaAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQepmtslNP- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 333 LQFITNSVYDEINIHFNhLSKDQSDDETIQLLKLLDLENVK---DQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFG 409
Cdd:COG4172 108 LHTIGKQIAEVLRLHRG-LSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 410 LDShnTFQ-----LIKLFQKRinLGQSIFMVTHDDEIIERY 445
Cdd:COG4172 187 LDV--TVQaqildLLKDLQRE--LGMALLLITHDLGVVRRF 223
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-219 |
7.69e-12 |
|
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: 67.46 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG--------IVPNLIELpmkyDELIVDPLSG 73
Cdd:TIGR01193 474 IVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGffqarsgeILLNGFSL----KDIDRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 74 VIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDL-------SGGMKQKLAIVETILQ 146
Cdd:TIGR01193 549 FINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELseegssiSGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 147 QSKTLFLDEPTAMLDVQATEDLWTKLIELwEDQTVVIVEHKVKhIWNHVDRVILMDYNGNIIADECPEIILQK 219
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELLDRN 699
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
246-441 |
7.86e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 246 TTNSHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAAKHM 324
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTsGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 325 YLVY--QNPELqfITNSVYDeiNIHFNHLSKDQSDDETIQLLKLLDL---ENVKDQHPYELSIGQKRRLSVATALSSKAD 399
Cdd:PRK10247 82 QVSYcaQTPTL--FGDTVYD--NLIFPWQIRNQQPDPAIFLDDLERFalpDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 612672732 400 IIFLDEPTFGLDSHN---TFQLIKLFQKRINLGqsIFMVTHD-DEI 441
Cdd:PRK10247 158 VLLLDEITSALDESNkhnVNEIIHRYVREQNIA--VLWVTHDkDEI 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
271-437 |
8.15e-12 |
|
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: 63.49 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHA-AKHMYLVYQNPELqfitnsvydeinihF 348
Cdd:cd03247 22 SLELKQGEKIALLGRSGSGKSTLLQLLTGDLKpQQGEITLDGVPVSDLEKAlSSLISVLNQRPYL--------------F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 nhlskdqsdDETIqllklldLENVKDQhpyeLSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINl 428
Cdd:cd03247 88 ---------DTTL-------RNNLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK- 146
|
....*....
gi 612672732 429 GQSIFMVTH 437
Cdd:cd03247 147 DKTLIWITH 155
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-210 |
8.57e-12 |
|
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: 64.62 E-value: 8.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQD- 78
Cdd:COG0410 3 MLEVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP---------------PRSGsIRFDGe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 ------------------PDSQFCMPK--VYEEL---AFVLENRQVPREDMDALiinalnmvnLNVTPEtyIKD------ 129
Cdd:COG0410 66 ditglpphriarlgigyvPEGRRIFPSltVEENLllgAYARRDRAEVRADLERV---------YELFPR--LKErrrqra 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 130 --LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIWNHVDRVILMDyNGN 206
Cdd:COG0410 135 gtLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADRAYVLE-RGR 213
|
....
gi 612672732 207 IIAD 210
Cdd:COG0410 214 IVLE 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
9.71e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.03 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQR---KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG-IVPNLIELPMK---------YDELI 67
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGlIKSKYGTIQVGdiyigdkknNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 68 VDPLS-------------GVIFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNvtpETYIK----DL 130
Cdd:PRK13631 101 TNPYSkkiknfkelrrrvSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD---DSYLErspfGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 131 SGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIA 209
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEVADEVIVMD-KGKILK 256
|
....
gi 612672732 210 DECP 213
Cdd:PRK13631 257 TGTP 260
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
252-454 |
1.02e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLI------KYQGDV-------YFENQRLTKIK 318
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeaRVEGEVrlfgrniYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 319 haaKHMYLVYQNPElQFITNSVYDE--INIHFNHLSKDQSD-DETIQ--LLKLLDLENVKDQ---HPYELSIGQKRRLSV 390
Cdd:PRK14267 85 ---REVGMVFQYPN-PFPHLTIYDNvaIGVKLNGLVKSKKElDERVEwaLKKAALWDEVKDRlndYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 391 ATALSSKADIIFLDEPTFGLDSHNTFQLIKL-FQKRINLgqSIFMVTHDdeiieryPSRRLKISD 454
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELlFELKKEY--TIVLVTHS-------PAQAARVSD 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
271-444 |
1.33e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.41 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDvyfenqrlTKIKHAAKHMYLVYQNPEL---------QFITNSVY 341
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG--------TVRRAGGARVAYVPQRSEVpdslpltvrDLVAMGRW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DEINIHFNHLSKDQSD-DETIQLLKLLDLENVKDQhpyELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIK 420
Cdd:NF040873 84 ARRGLWRRLTRDDRAAvDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....
gi 612672732 421 LFQKRINLGQSIFMVTHDDEIIER 444
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRR 184
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
252-459 |
1.34e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.02 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRL--TKIKHAAKHMYLVY 328
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVeaLSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 329 QNPELQFiTNSVYDEINI----HFNHLSKDQSDDETI--QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIF 402
Cdd:PRK09536 84 QDTSLSF-EFDVRQVVEMgrtpHRSRFDTWTETDRAAveRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 403 LDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLD 459
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
272-440 |
1.47e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.63 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQL-IKYQGDVYFENQRLTKIKHAAKHMYLVYQNPELqFITNSVydEINIHF-- 348
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYAL-FPHMTV--EQNIAFgl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 --NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDshntfqliKLFQKRI 426
Cdd:PRK11607 117 kqDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD--------KKLRDRM 188
|
170 180
....*....|....*....|...
gi 612672732 427 NL---------GQSIFMVTHDDE 440
Cdd:PRK11607 189 QLevvdilervGVTCVMVTHDQE 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-172 |
1.48e-11 |
|
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: 63.28 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDPDSQFCMPKVYEEL 92
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP---------------PLAGrVLLNGGPLDFQRDSIARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 93 AF------------VLENRQVPRED-MDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAM 159
Cdd:cd03231 76 LYlghapgikttlsVLENLRFWHADhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|...
gi 612672732 160 LDVQATEDLWTKL 172
Cdd:cd03231 156 LDKAGVARFAEAM 168
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
271-438 |
1.55e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 64.33 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHA--AKHMYLVYQNPELQF-ITnsVYDEINI 346
Cdd:COG4604 21 SLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDsGEVLVDGLDVATTPSRelAKRLAILRQENHINSrLT--VRELVAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 347 -HFNHlSKDQ--SDDETI--QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKL 421
Cdd:COG4604 99 gRFPY-SKGRltAEDREIidEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKL 177
|
170
....*....|....*...
gi 612672732 422 FQKRIN-LGQSIFMVTHD 438
Cdd:COG4604 178 LRRLADeLGKTVVIVLHD 195
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
247-438 |
1.68e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 247 TNSHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIM-QLIKYQGDVYFENQRL-----TKIKHA 320
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGgQIAPDHGEILFDGENIpamsrSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 321 AKHMYLVYQNPELqFITNSVYDeiNIHFNHLSKDQSDDETIQLLKLLDLENV-----KDQHPYELSIGQKRRLSVATALS 395
Cdd:PRK11831 83 RKRMSMLFQSGAL-FTDMNVFD--NVAYPLREHTQLPAPLLHSTVMMKLEAVglrgaAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 612672732 396 SKADIIFLDEPTFGLDSHNTFQLIKLFQKrIN--LGQSIFMVTHD 438
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISE-LNsaLGVTCVVVSHD 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-218 |
1.89e-11 |
|
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: 63.72 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-----------NLIELPMKYDELIvdp 70
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpdsgkilldgqDITKLPMHKRARL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 lsGVIF--QDPdSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQS 148
Cdd:cd03218 76 --GIGYlpQEA-SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 149 KTLFLDEPTAMLDVQATEDLwTKLIELWEDQT--VVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEIILQ 218
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDI-QKIIKILKDRGigVLITDHNVRETLSITDRAYII-YEGKVLAEGTPEEIAA 222
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-186 |
1.92e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 63.98 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 17 KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDPD--------------- 80
Cdd:COG4674 24 KALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTR---------------PDSGsVLFGGTDltgldeheiarlgig 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 SQFCMPKVYEELAfVLEN---------------RQVPREDMDALIINALNMVNLnvTPETYIK--DLSGGMKQKLAIVET 143
Cdd:COG4674 89 RKFQKPTVFEELT-VFENlelalkgdrgvfaslFARLTAEERDRIEEVLETIGL--TDKADRLagLLSHGQKQWLEIGML 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 144 ILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEH 186
Cdd:COG4674 166 LAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEH 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
251-438 |
1.98e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 63.98 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHA--AKHMYLV 327
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTpSSGEVRLNGRPLAAWSPWelARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 328 YQNPELQFiTNSVYDEINI-HFNHLSKDQSDDETI-QLLKLLDLENVKDQHPYELSIGQKRRLSVATAL-------SSKA 398
Cdd:COG4559 81 PQHSSLAF-PFTVEEVVALgRAPHGSSAAQDRQIVrEALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 399 DIIFLDEPTFGLD---SHNTFQLIKLFQKRinlGQSIFMVTHD 438
Cdd:COG4559 160 RWLFLDEPTSALDlahQHAVLRLARQLARR---GGGVVAVLHD 199
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-210 |
2.08e-11 |
|
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: 63.66 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 7 LRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI-VPN----LIElpmKYDELIVDPLS-----GVIF 76
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPEngrvLVD---GHDLALADPAWlrrqvGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 QDpdSQFCMPKVYEELAfvLENRQVPREDmdalIINALNMVN----LNVTPETYIK-------DLSGGMKQKLAIVETIL 145
Cdd:cd03252 83 QE--NVLFNRSIRDNIA--LADPGMSMER----VIEAAKLAGahdfISELPEGYDTivgeqgaGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 146 QQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNhVDRVILMdYNGNIIAD 210
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVM-EKGRIVEQ 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
2.19e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.93 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKypSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpMKYdelivDPLSGVIFQDPDS 81
Cdd:cd03217 1 LEIKDLHVS--VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--------PKY-----EVTEGEILFKGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFCMPkVYEE------LAFvlenrQVPREDMDALIINALNMVNLNvtpetyikdLSGGMKQKLAIVETILQQSKTLFLDE 155
Cdd:cd03217 66 ITDLP-PEERarlgifLAF-----QYPPEIPGVKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 156 PTAMLDVQATEDLwTKLIELW--EDQTVVIVEHKvKHIWNHV--DRVILMdYNGNIIADECPEIILQ 218
Cdd:cd03217 131 PDSGLDIDALRLV-AEVINKLreEGKSVLIITHY-QRLLDYIkpDRVHVL-YDGRIVKSGDKELALE 194
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-208 |
2.23e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 6 DLRLKYPSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVL-------SGIVpnlielpmKYDELIVDPLS------ 72
Cdd:PRK13657 339 DVSFSYDNSRQGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRI--------LIDGTDIRTVTraslrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 --GVIFQDPdsqfcmpkvyeeLAF---VLENRQVPRED------MDAL--------IINALNMVNLNVTPETyiKDLSGG 133
Cdd:PRK13657 410 niAVVFQDA------------GLFnrsIEDNIRVGRPDatdeemRAAAeraqahdfIERKPDGYDTVVGERG--RQLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 134 MKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNII 208
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTV-RNADRILVFD-NGRVV 548
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-186 |
2.26e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKypSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDP 79
Cdd:PRK13539 2 MLEGEDLACV--RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP---------------PAAGtIKLDGG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFcmPKVYEELAF------------VLENRQVPRE---DMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETI 144
Cdd:PRK13539 65 DIDD--PDVAEACHYlghrnamkpaltVAENLEFWAAflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 612672732 145 LQQSKTLFLDEPTAMLDVqATEDLWTKLIE--LWEDQTVVIVEH 186
Cdd:PRK13539 143 VSNRPIWILDEPTAALDA-AAVALFAELIRahLAQGGIVIAATH 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-221 |
2.28e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.85 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP------NLIELPMKYDELIVDPLSGVI--FQDPDSQFcm 85
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpdagkiTVLGVPVPARARLARARIGVVpqFDNLDLEF-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 86 pKVYEELA-----FVLENRQVpredmDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAML 160
Cdd:PRK13536 130 -TVRENLLvfgryFGMSTREI-----EAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 161 DVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIILQKYV 221
Cdd:PRK13536 204 DPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLCDRLCVLE-AGRKIAEGRPHALIDEHI 264
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-214 |
2.43e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSG--QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVL-------SGIvpnlielpmkY-------D 64
Cdd:PRK10535 4 LLELKDIRRSYPSGeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGT----------YrvagqdvA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 65 ELIVDPLS-------GVIFQDpdsqfcmpkvYEELAFV--LENRQVP-------REDMDALIINALNMVNLNVTPETYIK 128
Cdd:PRK10535 74 TLDADALAqlrrehfGFIFQR----------YHLLSHLtaAQNVEVPavyagleRKQRLLRAQELLQRLGLEDRVEYQPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 129 DLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKvKHIWNHVDRVILMdYNGNI 207
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHD-PQVAAQAERVIEI-RDGEI 221
|
....*..
gi 612672732 208 IADECPE 214
Cdd:PRK10535 222 VRNPPAQ 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-210 |
2.63e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 64.75 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYP---------SGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnLIElP----MKYDELIV 68
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLR----LEE-PtsgeILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 69 DPLSG-----------VIFQDPDSQFcMP--KVYEELAFVLE-NRQVPREDMDALIINALNMVNLNvtPET---YIKDLS 131
Cdd:COG4608 83 TGLSGrelrplrrrmqMVFQDPYASL-NPrmTVGDIIAEPLRiHGLASKAERRERVAELLELVGLR--PEHadrYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 132 GGMKQKLAIVETILQQSKTLFLDEPTAMLDV--QAT-----EDLWTKLielweDQTVVIVEHK---VKHIwnhVDRVILM 201
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVsiQAQvlnllEDLQDEL-----GLTYLFISHDlsvVRHI---SDRVAVM 231
|
250
....*....|.
gi 612672732 202 dYNGNI--IAD 210
Cdd:COG4608 232 -YLGKIveIAP 241
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
3-202 |
2.66e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.84 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 3 KVSDLRLKYPSGQRKIFDHL--NIT--IQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLIEL---------PMKYDELIVd 69
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPRKHLlkNVSgvAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsgsvllngmPIDAKEMRA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 pLSGVIFQDpDSQFCMPKVYEELAFVLE---NRQVPREDMDALIINALNMVNLNVTPETYI------KDLSGGMKQKLAI 140
Cdd:TIGR00955 100 -ISAYVQQD-DLFIPTLTVREHLMFQAHlrmPRRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 141 VETILQQSKTLFLDEPTAMLD-------VQATEDLWTKlielweDQTVVIVEHK-VKHIWNHVDRVILMD 202
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDsfmaysvVQVLKGLAQK------GKTIICTIHQpSSELFELFDKIILMA 241
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-209 |
2.71e-11 |
|
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: 64.75 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 22 LNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIELPMKyDELIVDPLSGVI-----------FQDPdSQFCMPKVY 89
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVLN-GRTLFDSRKGIFlppekrrigyvFQEA-RLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 90 EELAFVLENRQVP-REDMDALIINALNMVNLnvtPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDL 168
Cdd:TIGR02142 94 GNLRYGMKRARPSeRRISFERVIELLGIGHL---LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 169 WTKLIELWE--DQTVVIVEHKVKHIWNHVDRVILMDyNGNIIA 209
Cdd:TIGR02142 171 LPYLERLHAefGIPILYVSHSLQEVLRLADRVVVLE-DGRVAA 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
277-438 |
3.07e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.34 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA-----KHMYLVYQ------NPELQfITNSVYDEI 344
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWLGKDLLGMKDDEwravrSDIQMIFQdplaslNPRMT-IGEIIAEPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 NIHFNHLSKDQSDDET-IQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQ 423
Cdd:PRK15079 126 RTYHPKLSRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQ 205
|
170
....*....|....*.
gi 612672732 424 K-RINLGQSIFMVTHD 438
Cdd:PRK15079 206 QlQREMGLSLIFIAHD 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-166 |
3.28e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 20 DHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnLIELPMKYD-ELIVDPLSgvifQDPdsqfcmPK-----VY---- 89
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVL-LDDGRIIYEqDLIVARLQ----QDP------PRnvegtVYdfva 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 90 ---EELAFVLEN-----RQVPREDMDALI---------------------INAlNMVNLNVTPETYIKDLSGGMKQKLAI 140
Cdd:PRK11147 89 egiEEQAEYLKRyhdisHLVETDPSEKNLnelaklqeqldhhnlwqlenrINE-VLAQLGLDPDAALSSLSGGWLRKAAL 167
|
170 180
....*....|....*....|....*.
gi 612672732 141 VETILQQSKTLFLDEPTAMLDVQATE 166
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIE 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-209 |
3.55e-11 |
|
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: 64.35 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVsDLRLKYPSgqrkiFD-HLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNL---IELPmkyDELIVD------- 69
Cdd:COG4148 2 MLEV-DFRLRRGG-----FTlDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrIRLG---GEVLQDsargifl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 -----PLsGVIFQDPdSQFcmP--KVYEELAFVLEN--RQVPREDMDALI----INALnmvnLNVTPETyikdLSGGMKQ 136
Cdd:COG4148 73 pphrrRI-GYVFQEA-RLF--PhlSVRGNLLYGRKRapRAERRISFDEVVellgIGHL----LDRRPAT----LSGGERQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 137 KLAIVETILQQSKTLFLDEPTAMLDVQATEDLwTKLIELWEDQT---VVIVEHKVKHIWNHVDRVILMDyNGNIIA 209
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEI-LPYLERLRDELdipILYVSHSLDEVARLADHVVLLE-QGRVVA 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
271-459 |
3.60e-11 |
|
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: 63.08 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIK-H--AAKHMYLVYQN----PELqfitnSVYD 342
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGEDITGLPpHriARLGIGYVPEGrrifPSL-----TVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 eiNIH---FNHLSKDQSDDetiqllkllDLENV----------KDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFG 409
Cdd:COG0410 98 --NLLlgaYARRDRAEVRA---------DLERVyelfprlkerRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 410 LdS----HNTFQLIklfqKRIN-LGQSIFMVthddeiiERYPSRRLKISD-GALLD 459
Cdd:COG0410 167 L-AplivEEIFEII----RRLNrEGVTILLV-------EQNARFALEIADrAYVLE 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
271-457 |
3.73e-11 |
|
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: 61.46 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHaakhmylvyqnpelqfitnsvyDEINIHFN 349
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDP----------------------NELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 350 HLSKDqsddetIQLLKLLDLENVkdqhpyeLSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT---FQLIKLFQKRi 426
Cdd:cd03246 80 YLPQD------DELFSGSIAENI-------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGEralNQAIAALKAA- 145
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 427 nlGQSIFMVTHDDEIIERyPSRRLKISDGAL 457
Cdd:cd03246 146 --GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
252-455 |
4.01e-11 |
|
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: 60.93 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIM-QLIKYQGDVyfenQRLTKIKHAakhmylvyqn 330
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIV----TWGSTVKIG---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 331 pelqfitnsvydeiniHFNHLSKdqsddetiqllklldlenvkdqhpyelsiGQKRRLSVATALSSKADIIFLDEPTFGL 410
Cdd:cd03221 67 ----------------YFEQLSG-----------------------------GEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 612672732 411 DSHNTFQLIKLFQkriNLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03221 102 DLESIEALEEALK---EYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
277-438 |
4.09e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.99 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLIKYQGDVY-----FENQRLTKIKHAAKH------MYLVYQNPELQFitNSVY---- 341
Cdd:PRK11022 33 GEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMaekleFNGQDLQRISEKERRnlvgaeVAMIFQDPMTSL--NPCYtvgf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 ---DEINIHFNHlSKDQSDDETIQLLKLL---DLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:PRK11022 111 qimEAIKVHQGG-NKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQ 189
|
170 180
....*....|....*....|....*.
gi 612672732 416 FQLIKL---FQKRINLGqsIFMVTHD 438
Cdd:PRK11022 190 AQIIELlleLQQKENMA--LVLITHD 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
271-443 |
4.48e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.78 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ---GDVYFENQRLTKI---KHAAKHMYLVYQNPE----------LQ 334
Cdd:COG0396 20 NLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtsGSILLDGEDILELspdERARAGIFLAFQYPVeipgvsvsnfLR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 335 FITNSVYDEInihfnhLSKDQSDDETIQLLKLLDLE--------NVKdqhpyeLSIGQKRRLSVATALSSKADIIFLDEP 406
Cdd:COG0396 100 TALNARRGEE------LSAREFLKLLKEKMKELGLDedfldryvNEG------FSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 407 TFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIE 443
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILD 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-209 |
4.58e-11 |
|
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: 65.42 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 12 PSGqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP---NLIELPMKYDELIVDPLSGVIFQDPDSQ--FCMP 86
Cdd:TIGR01257 940 PSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPptsGTVLVGGKDIETNLDAVRQSLGMCPQHNilFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 87 KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATE 166
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 167 DLWTKLIELWEDQTVVIVEHkvkhiwnHVDRVILMDYNGNIIA 209
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTH-------HMDEADLLGDRIAIIS 1134
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
242-437 |
4.59e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.88 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 242 VDFPTTNSHLLQFKNGRIIRGKSTLLsfsdleiglgewitiTGANGSGKTTLLESIMQ-----LIKyqGDVYFENQRLTK 316
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTAL---------------MGESGAGKTTLLDVLAGrktagVIT--GEILINGRPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 317 ikhaakhmylvyqnpELQFITNSVyDEINIHfnhlSKDQSDDETIQLLKLLDlenvkdqhpyELSIGQKRRLSVATALSS 396
Cdd:cd03232 76 ---------------NFQRSTGYV-EQQDVH----SPNLTVREALRFSALLR----------GLSVEQRKRLTIGVELAA 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 397 KADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTH 437
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-222 |
4.88e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 16 RKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLIELPMKYDELI--------VDPLS-----GVIFQDPDSq 82
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrsifnyRDVLEfrrrvGMLFQRPNP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 83 FCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKD----LSGGMKQKLAIVETILQQSKTLFLDEPTA 158
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 159 MLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNHVDRVILMdYNGNIIADECPEIILQKYVH 222
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALF-FDGRLVEEGPTEQLFSSPKH 255
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
5.05e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlielpmkydelivDPLSGVIFQDPD 80
Cdd:PRK09536 3 MIDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTL---------------TPTAGTVLVAGD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 ----------SQFcMPKVYEE--LAFVLENRQVPR--------------EDMDALIINALNMVNLNVTPETYIKDLSGGM 134
Cdd:PRK09536 66 dvealsaraaSRR-VASVPQDtsLSFEFDVRQVVEmgrtphrsrfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 135 KQKLAIVETILQQSKTLFLDEPTAMLDVQ---ATEDLWTKLIElwEDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADE 211
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINhqvRTLELVRRLVD--DGKTAVAAIHDLDLAARYCDELVLLA-DGRVRAAG 221
|
....*.
gi 612672732 212 CPEIIL 217
Cdd:PRK09536 222 PPADVL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
267-448 |
5.33e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.70 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDV-YFENQRLTKIKHAAKHMYLVYQ--NPELQFitnSVYD 342
Cdd:PRK13536 60 LSFT---VASGECFGLLGPNGAGKSTIARMILGMTSpDAGKItVLGVPVPARARLARARIGVVPQfdNLDLEF---TVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EINIHFNHLSKDQSDDETI--QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIK 420
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
170 180
....*....|....*....|....*...
gi 612672732 421 LFQKRINLGQSIFMVTHDDEIIERYPSR 448
Cdd:PRK13536 214 RLRSLLARGKTILLTTHFMEEAERLCDR 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-217 |
5.79e-11 |
|
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: 62.41 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP----NLIEL----PMKYD--EL---- 66
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygNDVRLfgerRGGEDvwELrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 67 -IVDP----------------LSGV-----IFQDPDSqfcmpkvyeelafvlENRQVPREDMDALIINALNmvnlnvtpE 124
Cdd:COG1119 81 gLVSPalqlrfprdetvldvvLSGFfdsigLYREPTD---------------EQRERARELLELLGLAHLA--------D 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 125 TYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWtKLIELW---EDQTVVIVEHKVKHIWNHVDRVILM 201
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLL-ALLDKLaaeGAPTLVLVTHHVEEIPPGITHVLLL 216
|
250
....*....|....*.
gi 612672732 202 DyNGNIIADECPEIIL 217
Cdd:COG1119 217 K-DGRVVAAGPKEEVL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
284-444 |
6.46e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.20 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 284 GANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKiKHAAKHMYL-----VYQNpelqfitNSVYDEInIHF---NHLSKD 354
Cdd:COG4152 34 GPNGAGKTTTIRIILGILApDSGEVLWDGEPLDP-EDRRRIGYLpeergLYPK-------MKVGEQL-VYLarlKGLSKA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 355 QSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFM 434
Cdd:COG4152 105 EAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIF 184
|
170
....*....|
gi 612672732 435 VTHDDEIIER 444
Cdd:COG4152 185 SSHQMELVEE 194
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
266-438 |
7.36e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 266 LLSFSdLEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVYFENQRLTKIKHA--AKH-MYLVYQNPELQFITnsVYD 342
Cdd:COG4138 12 LGPIS-AQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAelARHrAYLSQQQSPPFAMP--VFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EINIHFNHLSKDQSDDETI-QLLKLLDLENVKDQHPYELSIGQKRR-------LSVATALSSKADIIFLDEPTFGLDSHN 414
Cdd:COG4138 89 YLALHQPAGASSEAVEQLLaQLAEALGLEDKLSRPLTQLSGGEWQRvrlaavlLQVWPTINPEGQLLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|....
gi 612672732 415 TFQLIKLFQKRINLGQSIFMVTHD 438
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHD 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-217 |
1.02e-10 |
|
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: 63.67 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQR---KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIELPMKYDELIVD------- 69
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLePTSGEVNVRVGDEWVDmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 ------PLSGVIFQDPDsQFCMPKVYEEL--AFVLEnrqVPRE--DMDALIInaLNMVNL------NVTPEtYIKDLSGG 133
Cdd:TIGR03269 359 grgrakRYIGILHQEYD-LYPHRTVLDNLteAIGLE---LPDElaRMKAVIT--LKMVGFdeekaeEILDK-YPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 134 MKQKLAIVETILQQSKTLFLDEPTAMLD----VQATEDLWTKLIELweDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIA 209
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEM--EQTFIIVSHDMDFVLDVCDRAALMR-DGKIVK 508
|
....*...
gi 612672732 210 DECPEIIL 217
Cdd:TIGR03269 509 IGDPEEIV 516
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-211 |
1.22e-10 |
|
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: 61.30 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRK--IFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlIELP------------MKYDEl 66
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-----LDRPtsgtvrlagqdlFALDE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 67 ivDPLS-------GVIFQdpdsqfcmpkvyeelAF-------VLENRQVPRE-----DMDALIINALNMVNLNVTPETYI 127
Cdd:COG4181 82 --DARArlrarhvGFVFQ---------------SFqllptltALENVMLPLElagrrDARARARALLERVGLGHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 128 KDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDvQAT----EDLwtkLIELWEDQ--TVVIVEHKVkHIWNHVDRVILM 201
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLD-AATgeqiIDL---LFELNRERgtTLVLVTHDP-ALAARCDRVLRL 219
|
250
....*....|
gi 612672732 202 DyNGNIIADE 211
Cdd:COG4181 220 R-AGRLVEDT 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
280-437 |
1.38e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.59 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 280 IT-ITGANGSGKTTLLESI--M-QLI---KYQGDVYFENQ-------RLTKIKhaaKHMYLVYQNPelqfitN----SVY 341
Cdd:COG1117 39 VTaLIGPSGCGKSTLLRCLnrMnDLIpgaRVEGEILLDGEdiydpdvDVVELR---RRVGMVFQKP------NpfpkSIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DeiNIHF-----NHLSKDQSDDETIQLLKLLDL-ENVKD---QHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:COG1117 110 D--NVAYglrlhGIKSKSELDEIVEESLRKAALwDEVKDrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 187
|
170 180
....*....|....*....|....*..
gi 612672732 413 HNTFQLIKLFQKrinLGQ--SIFMVTH 437
Cdd:COG1117 188 ISTAKIEELILE---LKKdyTIVIVTH 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-238 |
1.53e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.77 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 15 QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV--------------------PNLIELPMKYdelivdplsGV 74
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpssgtitiagyhitpetgnKNLKKLRKKV---------SL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 75 IFQDPDSQFCMPKVYEELAFVLENRQVPREDMDALIINALNMVNLnvtPETYIK----DLSGGMKQKLAIVETILQQSKT 150
Cdd:PRK13641 90 VFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL---SEDLISkspfELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 151 LFLDEPTAMLDVQATEDlwtkLIELWED-----QTVVIVEHKVKHIWNHVDRVILMDYnGNIIADECPEII------LQK 219
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKE----MMQLFKDyqkagHTVILVTHNMDDVAEYADDVLVLEH-GKLIKHASPKEIfsdkewLKK 241
|
250
....*....|....*....
gi 612672732 220 yvHLLSEygvwhPRAWEFA 238
Cdd:PRK13641 242 --HYLDE-----PATSRFA 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
262-458 |
1.56e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKI--KHAAKHMYLVYQNPEL----- 333
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYasKEVARRIGLLAQNATTpgdit 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 334 --QFITNSVYDEINIhFNHLSKdQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:PRK10253 98 vqELVARGRYPHQPL-FTRWRK-EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 612672732 412 SHNTFQLIKLFQKrINL--GQSIFMVTHDDEIIERYPSRRLKISDGALL 458
Cdd:PRK10253 176 ISHQIDLLELLSE-LNRekGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-208 |
1.62e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.13 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKI--FDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIELPMKyDELIVD-----PLS- 72
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-----NLLERPTS-GRVLVDgqdltALSe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ----------GVIFQdpdsQFCM---PKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLA 139
Cdd:PRK11153 75 kelrkarrqiGMIFQ----HFNLlssRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 140 IVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHK---VKHIwnhVDRVILMDyNGNII 208
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEmdvVKRI---CDRVAVID-AGRLV 220
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
271-464 |
1.85e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 62.89 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLikY---QGDVYFENQRLTKIKHAA--KHMYLVYQNPELqfitnsvydein 345
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGL--YrpeSGEILLDGQPVTADNREAyrQLFSAVFSDFHL------------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 ihFNHL--SKDQSDDETIQ-LLKLLDLEN---VKDQH--PYELSIGQKRRLSVATALSSKADIIFLDE------PTFgld 411
Cdd:COG4615 418 --FDRLlgLDGEADPARAReLLERLELDHkvsVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPEF--- 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 412 sHNTF--QLIKLFQKRinlGQSIFMVTHDDeiieRYPS---RRLKISDGALLDCDGDT 464
Cdd:COG4615 493 -RRVFytELLPELKAR---GKTVIAISHDD----RYFDladRVLKMDYGKLVELTGPA 542
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-442 |
1.85e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 NHLSKDQSDDETIQLLKLLDLENVKDQ---HPYE-LSIGQKRRLSVATALSSKAD-IIFLDEPTFGLDSHNTFQLIKLFQ 423
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMR 946
|
90
....*....|....*....
gi 612672732 424 KRINLGQSIFMVTHDDEII 442
Cdd:TIGR00956 947 KLADHGQAILCTIHQPSAI 965
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
265-456 |
2.12e-10 |
|
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: 59.09 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 265 TLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVyfenqrltkIKHAAKHMYLVYQNPelqfitnsvYde 343
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRI---------GMPEGEDLLFLPQRP---------Y-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 inihfnhlskdqsddetiqllklLDLENVKDQ--HPY--ELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLI 419
Cdd:cd03223 75 -----------------------LPLGTLREQliYPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 420 KLFQKRinlGQSIFMVTHdDEIIERYPSRRLKISDGA 456
Cdd:cd03223 132 QLLKEL---GITVISVGH-RPSLWKFHDRVLDLDGEG 164
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
261-462 |
2.62e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHA--AKHMYLVYQNPELQFiT 337
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSpDSGEVRLNGRPLADWSPAelARRRAVLPQHSSLSF-P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 338 NSVYD--EINIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATAL------SSKADIIFLDEPTFG 409
Cdd:PRK13548 91 FTVEEvvAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 410 LD---SHNTFQLIKLFQKRINLGqsIFMVTHDDEIIERYPSRRLKISDGALLdCDG 462
Cdd:PRK13548 171 LDlahQHHVLRLARQLAHERGLA--VIVVLHDLNLAARYADRIVLLHQGRLV-ADG 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
261-443 |
2.70e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVYFENQrltkikhaakhmylvyqnPELQFitnsv 340
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV------------------PDNQF----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 341 YDEINIhFNHLSKDQSDDETIQLLKLLDL-ENVKDQHPY-ELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:COG2401 97 GREASL-IDAIGRKGDFKDAVELLNAVGLsDAVLWLRRFkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|....*.
gi 612672732 419 IKLFQKRI-NLGQSIFMVTHDDEIIE 443
Cdd:COG2401 176 ARNLQKLArRAGITLVVATHHYDVID 201
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-213 |
3.12e-10 |
|
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: 60.59 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSG------QRK-IFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlIELPMK-------YDEL 66
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakQRApVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG-----LEKPAQgtvsfrgQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 67 IVDPLSG--------VIFQDPDSQFCMPKVYEE-LAFVLENrqvpREDMD-----ALIINALNMVNLNVT-PETYIKDLS 131
Cdd:TIGR02769 77 QLDRKQRrafrrdvqLVFQDSPSAVNPRMTVRQiIGEPLRH----LTSLDeseqkARIAELLDMVGLRSEdADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 132 GGMKQKLAIVETILQQSKTLFLDEPTAMLDVQatedLWTKLIELWED------QTVVIVEHKVKHIWNHVDRVILMDyNG 205
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMV----LQAVILELLRKlqqafgTAYLFITHDLRLVQSFCQRVAVMD-KG 227
|
....*...
gi 612672732 206 NIIaDECP 213
Cdd:TIGR02769 228 QIV-EECD 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
261-438 |
3.50e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.67 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKikhAAKHMYLVY--QNPELQFIT 337
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTRQ---ALQKNLVAYvpQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 338 NSVYDEINI-----HFNHLSKDQSDDETI--QLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGL 410
Cdd:PRK15056 94 PVLVEDVVMmgrygHMGWLRRAKKRDRQIvtAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180
....*....|....*....|....*...
gi 612672732 411 DSHNTFQLIKLFQKRINLGQSIFMVTHD 438
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-210 |
3.95e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.89 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlielpmkydelivDPLSGVIF---- 76
Cdd:COG4152 1 MLELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL---------------APDSGEVLwdge 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 ---QDPDSQFC-MP---------KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVET 143
Cdd:COG4152 64 pldPEDRRRIGyLPeerglypkmKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 144 ILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVehkVKHIWNHV----DRVILMDyNGNIIAD 210
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIF---SSHQMELVeelcDRIVIIN-KGRKVLS 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
267-455 |
4.56e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIKYQGD----------------VYFENQRLTKIKHA-AKHMYLVYQ 329
Cdd:PRK10261 35 LSFS---LQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmllrrrsrqvIELSEQSAAQMRHVrGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 330 NPELQF-----ITNSVYDEINIHFNhLSKDQSDDETIQLLKLL---DLENVKDQHPYELSIGQKRRLSVATALSSKADII 401
Cdd:PRK10261 112 EPMTSLnpvftVGEQIAESIRLHQG-ASREEAMVEAKRMLDQVripEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 402 FLDEPTFGLD---SHNTFQLIKLFQKRINLGqsIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:PRK10261 191 IADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITHDMGVVAEIADRVLVMYQG 245
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
4.58e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.00 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpmkYDelivdPLSGVIFQD-- 78
Cdd:PRK11300 5 LLSVSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF----------YK-----PTGGTILLRgq 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 -----PDSQ---------FCMPKVYEELAfVLEN------RQVP--------------REDMDALIINA--LNMVNLNVT 122
Cdd:PRK11300 68 hieglPGHQiarmgvvrtFQHVRLFREMT-VIENllvaqhQQLKtglfsgllktpafrRAESEALDRAAtwLERVGLLEH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 123 PETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLwTKLIELWEDQ---TVVIVEHKVKHIWNHVDRVI 199
Cdd:PRK11300 147 ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKEL-DELIAELRNEhnvTVLLIEHDMKLVMGISDRIY 225
|
250
....*....|....*..
gi 612672732 200 LMDYnGNIIADECPEII 216
Cdd:PRK11300 226 VVNQ-GTPLANGTPEEI 241
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
4.94e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 59.71 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlieLPMKYDELIVDPLSgvIFQDPD 80
Cdd:COG4604 1 MIEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRL------LPPDSGEVLVDGLD--VATTPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 sqfcmpkvyEELAFVL-----ENRQVPR---EDM----------------DALIIN-ALNMVNLNVTPETYIKDLSGGMK 135
Cdd:COG4604 71 ---------RELAKRLailrqENHINSRltvRELvafgrfpyskgrltaeDREIIDeAIAYLDLEDLADRYLDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLD----VQ-------ATEDLwtklielweDQTVVIVEHKVKHIWNHVDRVILMDyN 204
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQmmkllrrLADEL---------GKTVVIVLHDINFASCYADHIVAMK-D 211
|
250
....*....|....*
gi 612672732 205 GNIIADECPEIILQK 219
Cdd:COG4604 212 GRVVAQGTPEEIITP 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-186 |
5.40e-10 |
|
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: 59.69 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 34 LLGPSGCGKSTLLNVLSG-IVPNL--IELPMKYDElIVDPLSGVIFQD---------------PDSQFCMPKVYEELAFV 95
Cdd:cd03236 31 LVGPNGIGKSTALKILAGkLKPNLgkFDDPPDWDE-ILDEFRGSELQNyftkllegdvkvivkPQYVDLIPKAVKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 96 LENRQVPREDMDALIinalNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ---ATEDLWTKL 172
Cdd:cd03236 110 LLKKKDERGKLDELV----DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIREL 185
|
170
....*....|....
gi 612672732 173 IElwEDQTVVIVEH 186
Cdd:cd03236 186 AE--DDNYVLVVEH 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-163 |
5.93e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 15 QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLielpmkydelivdPLSGViFQDPDSQFcmpkvYEELAf 94
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT-------------PVAGC-VDVPDNQF-----GREAS- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 95 VLENrqVPREDMDALIINALNMVNLNvTPETYI---KDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ 163
Cdd:COG2401 102 LIDA--IGRKGDFKDAVELLNAVGLS-DAVLWLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
271-448 |
6.01e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 59.75 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIK-HAAKHM-----------YL---VYQNPELQ 334
Cdd:COG4674 30 SLYVDPGELRVIIGPNGAGKTTLMDVITGKTRpDSGSVLFGGTDLTGLDeHEIARLgigrkfqkptvFEeltVFENLELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 335 FITN-SVYDEInihFNHLSKDQSDdETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSH 413
Cdd:COG4674 110 LKGDrGVFASL---FARLTAEERD-RIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDA 185
|
170 180 190
....*....|....*....|....*....|....*
gi 612672732 414 NTFQLIKLFqKRINLGQSIFMVTHDDEIIERYPSR 448
Cdd:COG4674 186 ETERTAELL-KSLAGKHSVVVVEHDMEFVRQIARK 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
251-454 |
6.05e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.51 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHMYLVYQ 329
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRaTSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 330 NPELQFITNSVYDEINIHFNHL--SKDQSDDETIQLLKLLD-LENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEP 406
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFfaERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 612672732 407 TFGLDSHNTFQLIKLFQKRINLGQSIFMVthddeiiERYPSRRLKISD 454
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLV-------EQNANQALKLAD 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
259-442 |
6.65e-10 |
|
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: 59.17 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 259 IIRGkstlLSFsdlEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAA--KHMYLVYQNPELqF 335
Cdd:cd03253 16 VLKD----VSF---TIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSsGSILIDGQDIREVTLDSlrRAIGVVPQDTVL-F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 336 ITNSVYdeiNIHFNHLskDQSDDETIQLLKLLDLENVKDQHP--YE---------LSIGQKRRLSVATALSSKADIIFLD 404
Cdd:cd03253 88 NDTIGY---NIRYGRP--DATDEEVIEAAKAAQIHDKIMRFPdgYDtivgerglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 612672732 405 EPTFGLDSHnTFQLIklfQKRINL---GQSIFMVTHD-------DEII 442
Cdd:cd03253 163 EATSALDTH-TEREI---QAALRDvskGRTTIVIAHRlstivnaDKII 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-208 |
6.95e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.48 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKI--FDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIELPmkyDE--LIVD-----PL 71
Cdd:COG1135 1 MIELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-----NLLERP---TSgsVLVDgvdltAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 72 S-----------GVIFQDP---DSQfcmpKVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQK 137
Cdd:COG1135 73 SerelraarrkiGMIFQHFnllSSR----TVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 138 LAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHK---VKHIwnhVDRVILMDyNGNII 208
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEmdvVRRI---CDRVAVLE-NGRIV 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
34-438 |
7.21e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 34 LLGPSGCGKSTLLNVLSGIvpnlielpmkYDElivDPLSgVIFQDPDSQFCMPK---------VYEELAFV-----LENR 99
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGI----------YTR---DAGS-ILYLGKEVTFNGPKssqeagigiIHQELNLIpqltiAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 100 QVPRE---------------DMDALiinaLNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQA 164
Cdd:PRK10762 101 FLGREfvnrfgridwkkmyaEADKL----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 165 TEDLWTKLIELwEDQTVVIV--EHKVKHIWNHVDRV-ILMDynGNIIAdECPEIILQKyvHLLSEYGVwhPRAWEFAPSR 241
Cdd:PRK10762 177 TESLFRVIREL-KSQGRGIVyiSHRLKEIFEICDDVtVFRD--GQFIA-EREVADLTE--DSLIEMMV--GRKLEDQYPR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 242 VDFPTtNSHLLQFKN--GRIIRGkstlLSFSDLEiglGEWITITGANGSGKTTLLESIM-QLIKYQGDVYFENQRLTK-- 316
Cdd:PRK10762 249 LDKAP-GEVRLKVDNlsGPGVND----VSFTLRK---GEILGVSGLMGAGRTELMKVLYgALPRTSGYVTLDGHEVVTrs 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 317 -----------IKHAAKHMYLVyqnpelqfITNSVYDEINI-HFNHLSKD----QSDDETIQLLKLLDLENVK----DQH 376
Cdd:PRK10762 321 pqdglangivyISEDRKRDGLV--------LGMSVKENMSLtALRYFSRAggslKHADEQQAVSDFIRLFNIKtpsmEQA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 377 PYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SHNTFQLIKLFQKRinlGQSIFMVTHD 438
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgaKKEIYQLINQFKAE---GLSIILVSSE 454
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
71-223 |
8.28e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 LSGVIFQDPdSQFCMpKVYEELAFVLENrqVPRED---------MDALIINALNMVNLNVTPetYIKDLSGGMKQKLAIV 141
Cdd:PTZ00265 1297 LFSIVSQEP-MLFNM-SIYENIKFGKED--ATREDvkrackfaaIDEFIESLPNKYDTNVGP--YGKSLSGGQKQRIAIA 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 142 ETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWE--DQTVVIVEHKVKHIwNHVDRVILM---DYNGNIIADE----- 211
Cdd:PTZ00265 1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASI-KRSDKIVVFnnpDRTGSFVQAHgthee 1449
|
170
....*....|....*
gi 612672732 212 ---CPEIILQKYVHL 223
Cdd:PTZ00265 1450 llsVQDGVYKKYVKL 1464
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
261-420 |
8.35e-10 |
|
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: 58.43 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLI----KYQGDVYFENQRLTKIKHAAKHmylvyqnpelQFI 336
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnvSVEGDIHYNGIPYKEFAEKYPG----------EII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 337 TNSVYDeinIHFNHLSKDQsddeTIQL-LKLLDLENVKDqhpyeLSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:cd03233 87 YVSEED---VHFPTLTVRE----TLDFaLRCKGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
....*
gi 612672732 416 FQLIK 420
Cdd:cd03233 155 LEILK 159
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
271-459 |
1.00e-09 |
|
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: 58.53 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHmylvyqnpELQFITNS--VYDEI--- 344
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGFATVDGFDVVKEPAEARR--------RLGFVSDStgLYDRLtar 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 -NIHF----NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLI 419
Cdd:cd03266 97 eNLEYfaglYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 420 KLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLD 459
Cdd:cd03266 177 EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
272-438 |
1.04e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.75 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLI-KYQGDVYFENQRLTKIK-HAAKHMYLVYQNPELQ-FITNSVYDEINIHF 348
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVpRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASiFRRLSVYDNLMAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 ---NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKR 425
Cdd:PRK10895 104 qirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL 183
|
170
....*....|...
gi 612672732 426 INLGQSIFMVTHD 438
Cdd:PRK10895 184 RDSGLGVLITDHN 196
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-202 |
1.07e-09 |
|
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: 58.96 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 21 HLNI---TIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIELPMKYDELIVDPlsgvifqdpdsQFCMPK--------V 88
Cdd:cd03237 14 TLEVeggSISESEVIGILGPNGIGKTTFIKMLAGVLkPDEGDIEIELDTVSYKP-----------QYIKADyegtvrdlL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 89 YEELAFVLENRQVPREDMDALIINALNMVNLNvtpetyikDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQaTEDL 168
Cdd:cd03237 83 SSITKDFYTHPYFKTEIAKPLQIEQILDREVP--------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLM 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 169 WTKLIE---LWEDQTVVIVEHKVKHIWNHVDRVILMD 202
Cdd:cd03237 154 ASKVIRrfaENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
254-444 |
1.21e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 254 FKNGRIIRgksTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQL-----IKY-QGDVYFENQRLTkikHAAK----- 322
Cdd:PRK15134 15 FRQQQTVR---TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYpSGDIRFHGESLL---HASEqtlrg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 323 ----HMYLVYQNP-----ELQFITNSVYDEINIHfNHLSKDQSDDETIQLLKLLDLENVKDQ---HPYELSIGQKRRLSV 390
Cdd:PRK15134 89 vrgnKIAMIFQEPmvslnPLHTLEKQLYEVLSLH-RGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 391 ATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQK-RINLGQSIFMVTHDDEIIER 444
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRElQQELNMGLLFITHNLSIVRK 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-211 |
1.23e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 6 DLR-LKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP-------------------NLIELPMKYDE 65
Cdd:PRK11831 9 DMRgVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIApdhgeilfdgenipamsrsRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 66 LIvdpLSGVIFQDPDsqfcmpkVYEELAFVL-ENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETI 144
Cdd:PRK11831 89 LF---QSGALFTDMN-------VFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 145 LQQSKTLFLDEPTAMLDvQATEDLWTKLIELWEDQ---TVVIVEHKVKHIWNhvdrviLMDYnGNIIADE 211
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQD-PITMGVLVKLISELNSAlgvTCVVVSHDVPEVLS------IADH-AYIVADK 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
267-455 |
1.27e-09 |
|
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: 58.57 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFEnqrLTKIKHAAKHMYLVYQNPELQFItnsvYDEIN 345
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIEIE---LDTVSYKPQYIKADYEGTVRDLL----SSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHFNHlSKDQSDdetiqLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKR 425
Cdd:cd03237 88 DFYTH-PYFKTE-----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180 190
....*....|....*....|....*....|
gi 612672732 426 INLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
271-461 |
1.40e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLI-----KYQGDVYFENQRLTKIKHAAKHMYLVYQNPELQFitNSVYdeiN 345
Cdd:PRK10418 23 SLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAF--NPLH---T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHfNH-------LSKDQSDDETIQLLKLLDLENVK---DQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:PRK10418 98 MH-THaretclaLGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 612672732 416 FQ----LIKLFQKRinlGQSIFMVTHDDEIIERYPSRRLKISDGALLDCD 461
Cdd:PRK10418 177 ARildlLESIVQKR---ALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
233-463 |
1.47e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.99 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 233 RAWEFAPSRVDFPTTNSH----LLQFKNGRIIRGKStllSFS----DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ 304
Cdd:PRK10522 300 NKLALAPYKAEFPRPQAFpdwqTLELRNVTFAYQDN---GFSvgpiNLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 305 -GDVYFENQRLTkikhaAKHMYlvyqnpELQFITNSVYDEINIhFNHLSKDQSDD----------ETIQLLKLLDLENVK 373
Cdd:PRK10522 377 sGEILLDGKPVT-----AEQPE------DYRKLFSAVFTDFHL-FDQLLGPEGKPanpalvekwlERLKMAHKLELEDGR 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 374 DQHPyELSIGQKRRLSVATALSSKADIIFLDE------PTFgldsHNTFQLIKLFQKRInLGQSIFMVTHDDEIIERyPS 447
Cdd:PRK10522 445 ISNL-KLSKGQKKRLALLLALAEERDILLLDEwaadqdPHF----RREFYQVLLPLLQE-MGKTIFAISHDDHYFIH-AD 517
|
250
....*....|....*.
gi 612672732 448 RRLKISDGALLDCDGD 463
Cdd:PRK10522 518 RLLEMRNGQLSELTGE 533
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-208 |
1.51e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.03 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpmkYD----ELIVDplsGVIFQ 77
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF----------YDidegEILLD---GHDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 78 DpdsqFCMPKVYEELAFVLEN-----------------RQVPREDmdalIINALNMV-------NLNVTPETYIKD---- 129
Cdd:PRK11176 409 D----YTLASLRNQVALVSQNvhlfndtianniayartEQYSREQ----IEEAARMAyamdfinKMDNGLDTVIGEngvl 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 130 LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIWNhVDRVILMDyNGNII 208
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVE-DGEIV 557
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
271-455 |
1.63e-09 |
|
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: 57.50 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAAKHMYLVYQNPELqFITNSVYDEINIHFN 349
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVDVTAAPPADRPVSMLFQENNL-FAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 350 -HLSKDQSDDETIQ-LLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SHNTFQLI-KLFQ 423
Cdd:cd03298 97 pGLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEMLDLVlDLHA 176
|
170 180 190
....*....|....*....|....*....|..
gi 612672732 424 KRinlGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03298 177 ET---KMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-205 |
1.70e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKY--PSGQRKIFDHLNITIQDKEKVLLLGPSGCGKS----TLLNVLS--GIVP--------NLIELPMK-Y 63
Cdd:PRK09473 12 LLDVKDLRVTFstPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRIGgsatfngrEILNLPEKeL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 64 DELIVDPLSgVIFQDPDSQF--CMpKVYEELAFVLE-NRQVPREDMDALIINALNMVNLnvtPET------YIKDLSGGM 134
Cdd:PRK09473 92 NKLRAEQIS-MIFQDPMTSLnpYM-RVGEQLMEVLMlHKGMSKAEAFEESVRMLDAVKM---PEArkrmkmYPHEFSGGM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 135 KQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED--QTVVIVEHKVKHIWNHVDRVILMdYNG 205
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGICDKVLVM-YAG 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
128-440 |
1.77e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 128 KDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRVILMDYNGN 206
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDFVQFAGVLADCTL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 207 IIADECPEIILQKYVHLL--SE--YGVWHPRAweFAPSRVDFPTTNSHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITI 282
Cdd:PRK10938 214 AETGEREEILQQALVAQLahSEqlEGVQLPEP--DEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 283 TGANGSGKTTLLESImqlikyQGD---------VYFENQR-----LTKIKhaaKHMYLVYQNPELQF---------ITNS 339
Cdd:PRK10938 292 VGPNGAGKSTLLSLI------TGDhpqgysndlTLFGRRRgsgetIWDIK---KHIGYVSSSLHLDYrvstsvrnvILSG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 340 VYDEINIHfnHLSKDQSDDETIQLLKLLDLENVKDQHPYE-LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTfQL 418
Cdd:PRK10938 363 FFDSIGIY--QAVSDRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR-QL 439
|
330 340
....*....|....*....|....*
gi 612672732 419 IKLFQKrINLGQS---IFMVTHDDE 440
Cdd:PRK10938 440 VRRFVD-VLISEGetqLLFVSHHAE 463
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-219 |
2.03e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpMKYDELIVD----------- 69
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE------LEKGRIMIDdcdvakfgltd 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 --------PLSGVIFQ-------DPDSQFCMPKVYEELAfvlenrqvpREDMDALIINalNMVNLNVTPETYIKDLSGGM 134
Cdd:PLN03232 1308 lrrvlsiiPQSPVLFSgtvrfniDPFSEHNDADLWEALE---------RAHIKDVIDR--NPFGLDAEVSEGGENFSVGQ 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 135 KQKLAIVETILQQSKTLFLDEPTAMLDVQaTEDLWTKLI-ELWEDQTVVIVEHKVKHIWNhVDRVILMDyNGNIIADECP 213
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVR-TDSLIQRTIrEEFKSCTMLVIAHRLNTIID-CDKILVLS-SGQVLEYDSP 1453
|
....*.
gi 612672732 214 EIILQK 219
Cdd:PLN03232 1454 QELLSR 1459
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-217 |
2.85e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.89 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 23 NITIQDKEKVLLLGPSGCGKSTLLNVLSgivpNLIElPMKyDELIVDPLSGVIFQDPD--------------SQFCMP-- 86
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLN----RLIE-PTR-GQVLIDGVDIAKISDAElrevrrkkiamvfqSFALMPhm 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 87 KVYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATE 166
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 612672732 167 DLWTKLIELW--EDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADECPEIIL 217
Cdd:PRK10070 202 EMQDELVKLQakHQRTIVFISHDLDEAMRIGDRIAIMQ-NGEVVQVGTPDEIL 253
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
270-438 |
2.87e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.89 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 270 SDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA------KHMYLVYQN----PELQFITN 338
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSfalmPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 339 SVYdeiNIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD----SHN 414
Cdd:PRK10070 127 TAF---GMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEM 203
|
170 180
....*....|....*....|....
gi 612672732 415 TFQLIKLFQKRinlGQSIFMVTHD 438
Cdd:PRK10070 204 QDELVKLQAKH---QRTIVFISHD 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-168 |
3.19e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.19 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnliELP--------------MKYDEL-IVDPLSGVIFQD 78
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPsagkiwfsghditrLKNREVpFLRRQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 79 pdSQFCMPK-VYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPT 157
Cdd:PRK10908 88 --HHLLMDRtVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170
....*....|.
gi 612672732 158 AMLDVQATEDL 168
Cdd:PRK10908 166 GNLDDALSEGI 176
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-191 |
3.36e-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: 57.56 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVL------------SGIVPNLIELPMKYDELIVD 69
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntegdiqiDGVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 PLSGVIFQ-------DPDSQFC---MPKVYEELAFVLENRQVPredmdaliinalNMVNLNVTPETYIkdLSGGMKQKLA 139
Cdd:cd03289 83 PQKVFIFSgtfrknlDPYGKWSdeeIWKVAEEVGLKSVIEQFP------------GQLDFVLVDGGCV--LSHGHKQLMC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 612672732 140 IVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHI 191
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAM 200
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-208 |
3.67e-09 |
|
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: 56.50 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 7 LRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNL--IELPMKYDELIVDPlsgvifqdpdsqfc 84
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsVEGDIHYNGIPYKE-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 85 MPKVYE-ELAFVLEN-RQVP----REDMDAliinALNMVNlnvtpETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTA 158
Cdd:cd03233 77 FAEKYPgEIIYVSEEdVHFPtltvRETLDF----ALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 612672732 159 MLDVQATEDlWTKLIELWEDQ----TVVIVEHKVKHIWNHVDRVILMdYNGNII 208
Cdd:cd03233 148 GLDSSTALE-ILKCIRTMADVlkttTFVSLYQASDEIYDLFDKVLVL-YEGRQI 199
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-201 |
4.33e-09 |
|
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: 56.57 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 21 HLNITIQDKEKVLLLGPSGCGKSTLL-------NVLSGIV--PNLIELPMKYDELIVDPLSGVIFQDPDSQFCMPKVYEE 91
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLlailgemQTLEGKVhwSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 92 LAFVLE-NRQVPREDMDALIINAlnmvNLNVTP---ETYIKD----LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ 163
Cdd:cd03290 99 ITFGSPfNKQRYKAVTDACSLQP----DIDLLPfgdQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 164 ATEDLWTK-LIELWED--QTVVIVEHKVKHIwNHVDRVILM 201
Cdd:cd03290 175 LSDHLMQEgILKFLQDdkRTLVLVTHKLQYL-PHADWIIAM 214
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
267-437 |
5.57e-09 |
|
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: 56.19 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSDLEIGLGEWITITGANGSGKTTLLESIM-QLIKYQGDVYFENQRLTKIKHA---AKHMYLVYQNPELQFITNSVYD 342
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEatrSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EiNIHFNHLSKDQSDDETIQLLKL---LDLENVKDQ-----HPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHN 414
Cdd:cd03290 97 E-NITFGSPFNKQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190
....*....|....*....|....*....|
gi 612672732 415 TFQL-----IKLFQ--KRinlgqSIFMVTH 437
Cdd:cd03290 176 SDHLmqegiLKFLQddKR-----TLVLVTH 200
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-191 |
6.49e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSgqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpNLIELPMK------------YDELI-V 68
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM--NELESEVRvegrveffnqniYERRVnL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 69 DPLS---GVIFQDPDsQFCMpKVYEELAF-VLENRQVPREDMDALIINALNMVNLNVTPETYIK----DLSGGMKQKLAI 140
Cdd:PRK14258 84 NRLRrqvSMVHPKPN-LFPM-SVYDNVAYgVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 612672732 141 VETILQQSKTLFLDEPTAMLDVQAT---EDLWTKLiELWEDQTVVIVEHKVKHI 191
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSL-RLRSELTMVIVSHNLHQV 214
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-219 |
6.89e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 56.46 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTL-------LNVLSG-IVPNLIE---LPM-----KYDE 65
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGkIVIDGIDiskLPLhtlrsRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 66 LIVDPL--SGVI-FQ-DPDSQFCMPKVYEELAFV-LEN--RQVPrEDMDALIINALnmvnlnvtpetyiKDLSGGMKQKL 138
Cdd:cd03288 100 ILQDPIlfSGSIrFNlDPECKCTDDRLWEALEIAqLKNmvKSLP-GGLDAVVTEGG-------------ENFSVGQRQLF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 139 AIVETILQQSKTLFLDEPTAMLDVqATEDLWTKLI-ELWEDQTVVIVEHKVKHIWNhVDRVILMDyNGNIIADECPEIIL 217
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDM-ATENILQKVVmTAFADRTVVTIAHRVSTILD-ADLVLVLS-RGILVECDTPENLL 242
|
..
gi 612672732 218 QK 219
Cdd:cd03288 243 AQ 244
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-465 |
7.32e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 282 ITGANGSGKTTLLESIMQLI-------KYQGDVYFENQRLTKIK--HAAKHMYLVYQNPElQFITNSVYDEINIHF-NHL 351
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQIDaiKLRKEVGMVFQQPN-PFPHLSIYDNIAYPLkSHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 352 SKDQSDDETIQLLKLLDLENVKDQH------PYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKR 425
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLWKEVYdrlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 426 INlGQSIFMVTHDDEIIERYPSRRLKISDGALLDCdGDTN 465
Cdd:PRK14246 200 KN-EIAIVIVSHNPQQVARVADYVAFLYNGELVEW-GSSN 237
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
276-438 |
7.45e-09 |
|
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: 56.22 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 276 LGEWITITGANGSGKTTLL-----ESIMQLIKYQG-----DV-----------YFENQRLTKIKHAAKHMYLvyqnpelQ 334
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALkilagKLKPNLGKFDDppdwdEIldefrgselqnYFTKLLEGDVKVIVKPQYV-------D 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 335 FITNSVYDEINIHFNHLSKDQSDDEtiqLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHN 414
Cdd:cd03236 98 LIPKAVKGKVGELLKKKDERGKLDE---LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....
gi 612672732 415 TFQLIKLFQKRINLGQSIFMVTHD 438
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHD 198
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
271-414 |
7.78e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.87 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLikY---QGDVYFENQRLTKIKHAA--KHMYLVYQNPELqFiTNSVYDeiN 345
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLRF--YdptSGRILIDGVDIRDLTLESlrRQIGVVPQDTFL-F-SGTIRE--N 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 346 IHFNHlsKDQSDDETIQLLKLLDLENVKDQHP--YE---------LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHN 414
Cdd:COG1132 434 IRYGR--PDATDEEVEEAAKAAQAHEFIEALPdgYDtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-174 |
7.98e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDL---RlkypsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIF- 76
Cdd:PRK13538 1 MLEARNLaceR-----DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR---------------PDAGEVLw 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 QDPDSQFCMPKVYEELAFV------------LEN-------RQVPREDMdalIINALNMVNLNVTPETYIKDLSGGMKQK 137
Cdd:PRK13538 61 QGEPIRRQRDEYHQDLLYLghqpgikteltaLENlrfyqrlHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRR 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 612672732 138 LAIVETILQQSKTLFLDEP-TAmLDVQATEDLwTKLIE 174
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPfTA-IDKQGVARL-EALLA 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
271-438 |
8.90e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.25 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIM-QLIKYQGDVYFENQRLTKIKHA--AKHMYLVYQNPELQFITN-SVYDEINI 346
Cdd:COG1101 26 NLTIEEGDFVTVIGSNGAGKSTLLNAIAgSLPPDSGSILIDGKDVTKLPEYkrAKYIGRVFQDPMMGTAPSmTIEENLAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 347 HFNH---------LSKDQSdDETIQLLKLLD--LENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNT 415
Cdd:COG1101 106 AYRRgkrrglrrgLTKKRR-ELFRELLATLGlgLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTA 184
|
170 180
....*....|....*....|....*
gi 612672732 416 FQLIKLFQKRINlGQSI--FMVTHD 438
Cdd:COG1101 185 ALVLELTEKIVE-ENNLttLMVTHN 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
271-444 |
9.19e-09 |
|
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: 54.64 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESImqlIKYQGDvyfenQRLTKIKHAAKHMYLVYQNpELQFItnsvydeINIHFNH 350
Cdd:cd03238 15 DVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGK-----ARLISFLPKFSRNKLIFID-QLQFL-------IDVGLGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 351 LSKDQSDDEtiqllklldlenvkdqhpyeLSIGQKRRLSVATAL--SSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINL 428
Cdd:cd03238 79 LTLGQKLST--------------------LSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDL 138
|
170
....*....|....*.
gi 612672732 429 GQSIFMVTHDDEIIER 444
Cdd:cd03238 139 GNTVILIEHNLDVLSS 154
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-202 |
9.49e-09 |
|
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: 55.55 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPS-GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielPMKyDELIVD--PLS------ 72
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ-----PQG-GQVLLDgkPISqyehky 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -----GVIFQDPdsQFCMPKVYEELAFVLEnrQVPREDMDALIINALNMVNLNVTPETYIKD-------LSGGMKQKLAI 140
Cdd:cd03248 86 lhskvSLVGQEP--VLFARSLQDNIAYGLQ--SCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 141 VETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMD 202
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLD 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-211 |
9.79e-09 |
|
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: 55.62 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielP----MKYDELIVDPLSGVIFQDPDSQfcmpkVY 89
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP-----PdsgtVTVRGRVSSLLGLGGGFNPELT-----GR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 90 EELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLW 169
Cdd:cd03220 103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 170 TKLIELWEDQ-TVVIVEHKVKHIWNHVDRVILMDyNGNIIADE 211
Cdd:cd03220 183 RRLRELLKQGkTVILVSHDPSSIKRLCDRALVLE-KGKIRFDG 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
266-460 |
1.14e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 266 LLSFSdLEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVYFENQRLTKIKHA--AKH-MYLVYQN------PELQFI 336
Cdd:PRK03695 12 LGPLS-AEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAelARHrAYLSQQQtppfamPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 337 TNSVYDEinihfNHLSKDQSD-DETIQLLKLLDLENVKDQHpyeLSIGQKRR-------LSVATALSSKADIIFLDEPTF 408
Cdd:PRK03695 91 TLHQPDK-----TRTEAVASAlNEVAEALGLDDKLGRSVNQ---LSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 612672732 409 GLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDC 460
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-208 |
1.15e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 22 LNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielPMKYDELIVD-PLS-----------GVIFQDPDSQFC-MPKV 88
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-----PTSGELLIDDhPLHfgdysyrsqriRMIFQDPSTSLNpRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 89 YEELAFVLE-NRQVPREDMDALIINALNMVNLNVTPETYIKD-LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATE 166
Cdd:PRK15112 107 SQILDFPLRlNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 612672732 167 DLWTKLIELWEDQT---VVIVEH--KVKHIwnhVDRVILMDyNGNII 208
Cdd:PRK15112 187 QLINLMLELQEKQGisyIYVTQHlgMMKHI---SDQVLVMH-QGEVV 229
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-463 |
1.15e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKypSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV---------PNLIELPMKYDE---LIV 68
Cdd:PRK10636 1 MIVFSSLQIR--RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEIsadggsytfPGNWQLAWVNQEtpaLPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 69 DPLSGVIfqDPDSQFcmpkvyeelafvlenRQVPREDMDALIINALNMVNL---------------------------NV 121
Cdd:PRK10636 79 PALEYVI--DGDREY---------------RQLEAQLHDANERNDGHAIATihgkldaidawtirsraasllhglgfsNE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 122 TPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATedLWtklIELWEDQ---TVVIVEHKVKHIWNHVDRV 198
Cdd:PRK10636 142 QLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV--IW---LEKWLKSyqgTLILISHDRDFLDPIVDKI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 199 I------LMDYNGNIIADECP------------EIILQKYVHLLSEYGVWHPRAWE----------------FAPSRVDF 244
Cdd:PRK10636 217 IhieqqsLFEYTGNYSSFEVQratrlaqqqamyESQQERVAHLQSYIDRFRAKATKakqaqsrikmlermelIAPAHVDN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 245 PTTNSH---------LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIM-QLIKYQGDVYFenQRL 314
Cdd:PRK10636 297 PFHFSFrapeslpnpLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAgELAPVSGEIGL--AKG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 315 TKIKHAAKHmylvyqnpELQFITNsvyDEINI-HFNHLSKDQSDDETIQLLKLLDLENVKDQHPYE-LSIGQKRRLSVAT 392
Cdd:PRK10636 375 IKLGYFAQH--------QLEFLRA---DESPLqHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLAL 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 393 ALSSKADIIFLDEPTFGLDShNTFQliKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDCDGD 463
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDL-DMRQ--ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGD 511
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
271-465 |
1.16e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.36 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQ-LIKYQGDVYFENQRLTKIKHAAKHMYLVYQnpelqfitnsvydEINIhFN 349
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQDHTTTPPSRRPVSMLFQ-------------ENNL-FS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 350 HLSKDQ------------SDDETIQLLKLLD---LENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD--- 411
Cdd:PRK10771 85 HLTVAQniglglnpglklNAAQREKLHAIARqmgIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpal 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 412 SHNTFQLIKLF--QKRINLgqsiFMVTHDDEIIERYPSRRLKISDGAlLDCDGDTN 465
Cdd:PRK10771 165 RQEMLTLVSQVcqERQLTL----LMVSHSLEDAARIAPRSLVVADGR-IAWDGPTD 215
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-201 |
1.23e-08 |
|
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: 55.61 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVI-FQDP 79
Cdd:TIGR02323 3 LLQVSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLA---------------PDHGTAtYIMR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQ----FCMPK------VYEELAFVLEN-RQVPREDMDA--------LIINALNMVNLNVT----------PETYIKDL 130
Cdd:TIGR02323 66 SGAelelYQLSEaerrrlMRTEWGFVHQNpRDGLRMRVSAganigerlMAIGARHYGNIRATaqdwleeveiDPTRIDDL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 131 ----SGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILM 201
Cdd:TIGR02323 146 prafSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVM 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-207 |
1.80e-08 |
|
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: 53.98 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKypsgqrKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSG-VIFQDP 79
Cdd:cd03215 4 VLEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP---------------PASGeITLDGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFCMPK--VYEELAFVLENRQvpredMDALIinaLNM-VNLNVTPETYikdLSGGMKQKLAIVETILQQSKTLFLDEP 156
Cdd:cd03215 63 PVTRRSPRdaIRAGIAYVPEDRK-----REGLV---LDLsVAENIALSSL---LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 157 TAMLDVQATEDLWTKLIELWEDQTVVIV------EhkvkhIWNHVDRVILMdYNGNI 207
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLisseldE-----LLGLCDRILVM-YEGRI 182
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
271-437 |
1.86e-08 |
|
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: 54.85 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTllesIMQLIK--Y---QGDVYFENQRLTK--IKHAAKHMYLVYQNPELqfITNSVYDe 343
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKST----VVSLLErfYdptSGEILLDGVDIRDlnLRWLRSQIGLVSQEPVL--FDGTIAE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 iNIHFNhlSKDQSDDETIQLLKL-------LDLENVKD----QHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:cd03249 96 -NIRYG--KPDATDEEVEEAAKKanihdfiMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180
....*....|....*....|....*...
gi 612672732 413 HNTfqliKLFQKRIN---LGQSIFMVTH 437
Cdd:cd03249 173 ESE----KLVQEALDramKGRTTIVIAH 196
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-186 |
2.73e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.55 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP---NLIELPMKyDELIVDPLS----- 72
Cdd:PRK11701 6 LLSVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLApdaGEVHYRMR-DGQLRDLYAlseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 ---------GVIFQDPDSQFCMP-----KVYEELAFVLEN-----RQVPREDMDALIINALNMVNLnvtPETYikdlSGG 133
Cdd:PRK11701 83 rrrllrtewGFVHQHPRDGLRMQvsaggNIGERLMAVGARhygdiRATAGDWLERVEIDAARIDDL---PTTF----SGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 134 MKQKLAIVETILQQSKTLFLDEPTAMLD--VQAT-EDLWTKLI-ELweDQTVVIVEH 186
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQARlLDLLRGLVrEL--GLAVVIVTH 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
249-438 |
2.96e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 249 SHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVYFENQRLtKIKHAAKHMYLvy 328
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-RIGYVPQKLYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 329 qNPELQFITNsvydeiniHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTF 408
Cdd:PRK09544 79 -DTTLPLTVN--------RFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 409 GLDSHNTFQLIKLF-QKRINLGQSIFMVTHD 438
Cdd:PRK09544 150 GVDVNGQVALYDLIdQLRRELDCAVLMVSHD 180
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
267-444 |
3.79e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTT---LLESImqlikYQ---GDVYFENQRLTKIKHAA--KHMYLVYQNPELqfITN 338
Cdd:TIGR00958 500 LTFT---LHPGEVVALVGPSGSGKSTvaaLLQNL-----YQptgGQVLLDGVPLVQYDHHYlhRQVALVGQEPVL--FSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 339 SVYDEINIHFNHLSKDQ---------SDDETIQLLKLLDLEnvKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFG 409
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEimaaakaanAHDFIMEFPNGYDTE--VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 410 LD--SHNTFQLIKLFQKRinlgqSIFMVTHDDEIIER 444
Cdd:TIGR00958 648 LDaeCEQLLQESRSRASR-----TVLLIAHRLSTVER 679
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-208 |
4.06e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.32 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 15 QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNLIElpMKYDELIVD--PLSG---------VIFQDPDSQF 83
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVR--QTAGRVLLDgkPVAPcalrgrkiaTIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 84 cmPKVYEELAFVLEN-RQVPREDMDALIINALNMVNLNVTP---ETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAM 159
Cdd:PRK10418 93 --NPLHTMHTHARETcLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 612672732 160 LDVQATEDLWTKLIELWEDQT--VVIVEHKVKHIWNHVDRVILMDyNGNII 208
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMS-HGRIV 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-195 |
4.69e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.20 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLsgivpNLIELPMKyDELIVDPLSGVIFQDPDS 81
Cdd:PRK10619 6 LNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-----NFLEKPSE-GSIVVNGQTINLVRDKDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QFcmpKVYEE-----------LAF----------VLEN------------RQVPREDMdaliINALNMVNLNVTPE-TYI 127
Cdd:PRK10619 78 QL---KVADKnqlrllrtrltMVFqhfnlwshmtVLENvmeapiqvlglsKQEARERA----VKYLAKVGIDERAQgKYP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 128 KDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKV---KHIWNHV 195
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMgfaRHVSSHV 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-216 |
4.69e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlielpmkydelIVDPLSGVIFQDPDSQ--FCMPKVYEE 91
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG---------------LVAPDEGVIKRNGKLRigYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 92 LA-------FVLENRQVPREDmdalIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ- 163
Cdd:PRK09544 80 TTlpltvnrFLRLRPGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNg 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 164 --ATEDLWTKL-IELweDQTVVIVEHKVKHIWNHVDRVILMdyNGNIIADECPEII 216
Cdd:PRK09544 156 qvALYDLIDQLrREL--DCAVLMVSHDLHLVMAKTDEVLCL--NHHICCSGTPEVV 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-162 |
4.87e-08 |
|
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: 55.18 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 25 TIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIELPMK-------------YDELIVDPLSGVIFQDPDSQFcmpkVYE 90
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDlkisykpqyispdYDGTVEEFLRSANTDDFGSSY----YKT 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 91 ElafvlenrqvpredmdalIINALNMVNLNvtpETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDV 162
Cdd:COG1245 438 E------------------IIKPLGLEKLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
246-438 |
5.18e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 246 TTNSHLLQFKNGRIIRGKS--TLLSFSDLEIGL--GEWITITGANGSGKTTLLESIMQLI----KYQGDVYFENQ----- 312
Cdd:PRK09473 7 QQADALLDVKDLRVTFSTPdgDVTAVNDLNFSLraGETLGIVGESGSGKSQTAFALMGLLaangRIGGSATFNGReilnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 313 ---RLTKIKhaAKHMYLVYQNPELQF-----ITNSVYDEINIHfNHLSKDQSDDETIQLLKLLDLENVKDQ---HPYELS 381
Cdd:PRK09473 87 pekELNKLR--AEQISMIFQDPMTSLnpymrVGEQLMEVLMLH-KGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 382 IGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQ--KRiNLGQSIFMVTHD 438
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelKR-EFNTAIIMITHD 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-187 |
6.22e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.11 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 5 SDLRLKYPS-GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI-VPN-----LIELPM-KYDELIVDPLSGVIF 76
Cdd:TIGR00958 482 QDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQPTggqvlLDGVPLvQYDHHYLHRQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 QDPdsQFCMPKVYEELAFVLenRQVPREDM---------DALIINALNMVNLNVTPETyiKDLSGGMKQKLAIVETILQQ 147
Cdd:TIGR00958 562 QEP--VLFSGSVRENIAYGL--TDTPDEEImaaakaanaHDFIMEFPNGYDTEVGEKG--SQLSGGQKQRIAIARALVRK 635
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 612672732 148 SKTLFLDEPTAMLDVQATEDL--WTKlielWEDQTVVIVEHK 187
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLqeSRS----RASRTVLLIAHR 673
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-186 |
6.24e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSdlrlKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI----------VPNlIELPMKYDELIVDP 70
Cdd:TIGR03719 7 MNRVS----KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfngearpQPG-IKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 71 ---LSGVIFQDPDSQFCMPKVYEELAfvlENRQVPREDMDAL---------IINALNMVNLNVT------------PETY 126
Cdd:TIGR03719 82 tktVRENVEEGVAEIKDALDRFNEIS---AKYAEPDADFDKLaaeqaelqeIIDAADAWDLDSQleiamdalrcppWDAD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 127 IKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELweDQTVVIVEH 186
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTH 216
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-443 |
7.46e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 55.22 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 121 VTPETYIKDLSGGMKQKLAIVETILQQ--SKTLFLDEPTAMLDVQATEDLwTKLIELWEDQ--TVVIVEHKVKHIwNHVD 196
Cdd:PRK00635 468 LTPERALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKL-INVIKKLRDQgnTVLLVEHDEQMI-SLAD 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 197 RVILMD-----YNGNIIADECPEIILQKYVHLLSEYgVWHPRAWEFAPSRvdfPTTNshllqfknGRIIRGKSTLLSFSD 271
Cdd:PRK00635 546 RIIDIGpgagiFGGEVLFNGSPREFLAKSDSLTAKY-LRQELTIPIPEKR---TNSL--------GTLTLSKATKHNLKD 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIG--LGEWITITGANGSGKT-----TLLESIMQLIKYQGD--VYFENQRLTKIKHAAKHMYLVYQNP-ELQFItnSVY 341
Cdd:PRK00635 614 LTISlpLGRLTVVTGVSGSGKSslindTLVPAVEEFIEQGFCsnLSIQWGAISRLVHITRDLPGRSQRSiPLTYI--KAF 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DEINIHF-------------NHLSKDQS----------------DDET-------------------------------- 360
Cdd:PRK00635 692 DDLRELFaeqprskrlgltkSHFSFNTPlgacaecqglgsitttDNRTsipcpsclgkrflpqvlevrykgkniadilem 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 361 ------------------IQLLKLLDLENVKDQHP-YELSIGQKRRLSVATAL---SSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:PRK00635 772 tayeaekffldepsihekIHALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKAL 851
|
410 420
....*....|....*....|....*
gi 612672732 419 IKLFQKRINLGQSIFMVTHDDEIIE 443
Cdd:PRK00635 852 IYVLQSLTHQGHTVVIIEHNMHVVK 876
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-227 |
7.59e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.16 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRK-IFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVIfqdpd 80
Cdd:COG1134 24 LKELLLRRRRTRREEFwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE---------------PTSGRV----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 sqfcmpKVYEELAFVLE-----N-----RQ----------VPREDMDAL---II------NALNMvnlnvtPetyIKDLS 131
Cdd:COG1134 84 ------EVNGRVSALLElgagfHpeltgREniylngrllgLSRKEIDEKfdeIVefaelgDFIDQ------P---VKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 132 GGMKQKLAI-VETILqQSKTLFLDEPTAMLDVQ----ATEdlwtKLIELWED-QTVVIVEHKVKHIWNHVDRVILMDyNG 205
Cdd:COG1134 149 SGMRARLAFaVATAV-DPDILLVDEVLAVGDAAfqkkCLA----RIRELRESgRTVIFVSHSMGAVRRLCDRAIWLE-KG 222
|
250 260
....*....|....*....|..
gi 612672732 206 NIIADECPEIILQKYVHLLSEY 227
Cdd:COG1134 223 RLVMDGDPEEVIAAYEALLAGR 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
262-456 |
8.76e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTL---LESIMQLIKyqGDVYFENQRLTKIKH--AAKH-MYLVYQnpELqf 335
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLmkvLSGIHEPTK--GTITINNINYNKLDHklAAQLgIGIIYQ--EL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 336 itnSVYDEINIHFN-----HLSK----------DQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADI 400
Cdd:PRK09700 90 ---SVIDELTVLENlyigrHLTKkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 401 IFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGA 456
Cdd:PRK09700 167 IIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-219 |
8.85e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 9 LKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTL------LN-------VLSGIVPNLIELPMKYDELIVDPLSGVI 75
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtlglfrINesaegeiIIDGLNIAKIGLHDLRFKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 FQ-------DPDSQFCMpkvyEELAFVLENRQVPRedmdalIINALNmVNLNVTPETYIKDLSGGMKQKLAIVETILQQS 148
Cdd:TIGR00957 1372 FSgslrmnlDPFSQYSD----EEVWWALELAHLKT------FVSALP-DKLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 149 KTLFLDEPTAMLDVQaTEDLWTKLIEL-WEDQTVVIVEHKVKHIWNHVdRVILMDyNGNIIADECPEIILQK 219
Cdd:TIGR00957 1441 KILVLDEATAAVDLE-TDNLIQSTIRTqFEDCTVLTIAHRLNTIMDYT-RVIVLD-KGEVAEFGAPSNLLQQ 1509
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
281-459 |
1.03e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 281 TITGANGSGKTTLLESIMQL------IKYQGDVYFENQRLTKIKHA---AKHMYLVYQ--NPELQFITNSVYDEINIHFN 349
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSIFNYRDVlefRRRVGMLFQrpNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 350 HLSKDQSDDETIQLLKLLDLENVKDQ---HPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTfQLIKLFQKRI 426
Cdd:PRK14271 131 VPRKEFRGVAQARLTEVGLWDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT-EKIEEFIRSL 209
|
170 180 190
....*....|....*....|....*....|...
gi 612672732 427 NLGQSIFMVTHDDEIIERYPSRRLKISDGALLD 459
Cdd:PRK14271 210 ADRLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
271-443 |
1.09e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.65 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTL-LESImqlikyqgdvYFENQR--LTKIKHAAKHMYLVYQNPELQFITN-----SVyD 342
Cdd:cd03270 15 DVDIPRNKLVVITGVSGSGKSSLaFDTI----------YAEGQRryVESLSAYARQFLGQMDKPDVDSIEGlspaiAI-D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EINIHFNHLSKDQSDDETIQLLKLL-----------DLENVK------DQHPYELSIGQKRRLSVATALSSK-ADIIF-L 403
Cdd:cd03270 84 QKTTSRNPRSTVGTVTEIYDYLRLLfarvgirerlgFLVDVGlgyltlSRSAPTLSGGEAQRIRLATQIGSGlTGVLYvL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 404 DEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIE 443
Cdd:cd03270 164 DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-438 |
1.12e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 34 LLGPSGCGKSTLLNVLSGI-VPNLIEL-----PMKYDELIVDPLSGVIFqdpdsqfcmpkVYEELAF-----VLEN---R 99
Cdd:PRK11288 35 LMGENGAGKSTLLKILSGNyQPDAGSIlidgqEMRFASTTAALAAGVAI-----------IYQELHLvpemtVAENlylG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 100 QVP-------REDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKL 172
Cdd:PRK11288 104 QLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 173 IELWEDQTVVI-VEHKVKHIWNHVDRV-ILMDynGNIIA--DECPEI----ILQKYV--HLLSEYGvWHPRawEFAPSRv 242
Cdd:PRK11288 184 RELRAEGRVILyVSHRMEEIFALCDAItVFKD--GRYVAtfDDMAQVdrdqLVQAMVgrEIGDIYG-YRPR--PLGEVR- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 243 dfpttnshlLQFKN--GriiRGKSTLLSFSdleIGLGEWITITGANGSGKTTLlesiMQLI-----KYQGDVYFENQRLT 315
Cdd:PRK11288 258 ---------LRLDGlkG---PGLREPISFS---VRAGEIVGLFGLVGAGRSEL----MKLLygatrRTAGQVYLDGKPID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 316 --KIKHAAKH-MYLVYQNPELQFI--TNSVYDEINI----HFNHLS-------KDQSDDETIQLLklldleNVKDQHPYE 379
Cdd:PRK11288 319 irSPRDAIRAgIMLCPEDRKAEGIipVHSVADNINIsarrHHLRAGclinnrwEAENADRFIRSL------NIKTPSREQ 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 380 ----LSIGQKRRLSVATALSSKADIIFLDEPTFGLD---SHNTFQLIKLFQKRinlGQSIFMVTHD 438
Cdd:PRK11288 393 limnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgaKHEIYNVIYELAAQ---GVAVLFVSSD 455
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-168 |
1.13e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 5 SDLRLKYPSGQrKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnliELpmkydelivDPLSGVIFQDPDSQFC 84
Cdd:PLN03073 512 SDASFGYPGGP-LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG------EL---------QPSSGTVFRSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 85 M--------------PKVYEELAFVLENRQVPREDMDALIINAlnmvNLNVTPetyIKDLSGGMKQKLAIVETILQQSKT 150
Cdd:PLN03073 576 VfsqhhvdgldlssnPLLYMMRCFPGVPEQKLRAHLGSFGVTG----NLALQP---MYTLSGGQKSRVAFAKITFKKPHI 648
|
170
....*....|....*...
gi 612672732 151 LFLDEPTAMLDVQATEDL 168
Cdd:PLN03073 649 LLLDEPSNHLDLDAVEAL 666
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
130-437 |
1.14e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 130 LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTkLIELWEDQTV---VIV--------EHkvkhiwnhVDRV 198
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWE-LIDRIRAERPgmsVLVataymeeaER--------FDWL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 199 ILMDyNGNIIADECPEIILQK---------YVHLLSEYGVWHPRAWEFAPSRVDFpttnshllqfKNGRIIRGKSTLLSF 269
Cdd:NF033858 208 VAMD-AGRVLATGTPAELLARtgadtleaaFIALLPEEKRRGHQPVVIPPRPADD----------DDEPAIEARGLTMRF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 270 SD--------LEIGLGEWITITGANGSGKTT-------LLE------------------SIMQLIKY--QG-DVYFEnqr 313
Cdd:NF033858 277 GDftavdhvsFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPasegeawlfgqpvdagdiATRRRVGYmsQAfSLYGE--- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 314 LTkikhaakhmylVYQNPELqfitnsvydeiniH---FnHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSV 390
Cdd:NF033858 354 LT-----------VRQNLEL-------------HarlF-HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSL 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 612672732 391 ATALSSKADIIFLDEPTFGLD--SHNTF--QLIKLFQKRinlGQSIFMVTH 437
Cdd:NF033858 409 AVAVIHKPELLILDEPTSGVDpvARDMFwrLLIELSRED---GVTIFISTH 456
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
271-456 |
1.15e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFE---NQRLTKIKHAAKHMYLVYQNPELQFITNsvydeinI 346
Cdd:PRK13543 31 DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDgktATRGDRSRFMAYLGHLPGLKADLSTLEN-------L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 347 HF-NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKR 425
Cdd:PRK13543 104 HFlCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAH 183
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 426 INLGQSIFMVTHDDEIIERYPSRRLKISDGA 456
Cdd:PRK13543 184 LRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-186 |
1.15e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 25 TIQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlielpmkydelivDPLSGVIFQDPD----SQFCMPKVYEELAFVLenRQ 100
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVL---------------KPDEGEVDPELKisykPQYIKPDYDGTVEDLL--RS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 101 VPrEDMDA-----LIINALNMVNLNvtpETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ---ATEDLWTKL 172
Cdd:PRK13409 424 IT-DDLGSsyyksEIIKPLQLERLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRI 499
|
170
....*....|....
gi 612672732 173 IELwEDQTVVIVEH 186
Cdd:PRK13409 500 AEE-REATALVVDH 512
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-201 |
1.32e-07 |
|
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: 54.25 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG---------------IVPNLIEL--PMKY 63
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdttvtsgdatvagksILTNISDVhqNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 64 D---ELIVDPLSGvifqdpdsqfcmpkvYEELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAI 140
Cdd:TIGR01257 2017 CpqfDAIDDLLTG---------------REHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLST 2081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 141 VETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRVILM 201
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-209 |
1.32e-07 |
|
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: 53.98 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmkydelivdPLSGVI------ 75
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP---------------PTAGSVrldgad 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 ---------------------------------FQDPDSQfcmpKVYE--ELAfvlenrqvpreDMDALIinaLNMvnln 120
Cdd:COG4618 396 lsqwdreelgrhigylpqdvelfdgtiaeniarFGDADPE----KVVAaaKLA-----------GVHEMI---LRL---- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 121 vtP---ETYIKD----LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ-TVVIVEHKVkHIW 192
Cdd:COG4618 454 --PdgyDTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGaTVVVITHRP-SLL 530
|
250
....*....|....*..
gi 612672732 193 NHVDRVILMDyNGNIIA 209
Cdd:COG4618 531 AAVDKLLVLR-DGRVQA 546
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
261-413 |
1.34e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 261 RGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIM-QLIKYQGDVYfenqrltkIKHAAKHMylvyqnPELQFITNS 339
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVH--------MKGSVAYV------PQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 340 VYDEiNIHFNHLSKDQSDDETIQLLKLL-DLENVKDQHPYE-------LSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:TIGR00957 714 SLRE-NILFGKALNEKYYQQVLEACALLpDLEILPSGDRTEigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
..
gi 612672732 412 SH 413
Cdd:TIGR00957 793 AH 794
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
262-438 |
1.53e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.37 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAAKHMYlvyQNPELqFITNSV 340
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETpSAGELLAGTAPLAEAREDTRLMF---QDARL-LPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 341 YDEINIHFnhlsKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTF---Q 417
Cdd:PRK11247 99 IDNVGLGL----KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIemqD 174
|
170 180
....*....|....*....|..
gi 612672732 418 LI-KLFQKRinlGQSIFMVTHD 438
Cdd:PRK11247 175 LIeSLWQQH---GFTVLLVTHD 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
251-421 |
1.56e-07 |
|
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: 53.68 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTL---LESIMQLIKYQGDVYFENQRLtKIKH----AAKH 323
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWDGEIYWSGSPL-KASNirdtERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 324 MYLVYQnpELQFITN-SVYDEINI--HFNHLSKDQSDDETI----QLLKLLDLENVKDQHPY-ELSIGQKRRLSVATALS 395
Cdd:TIGR02633 80 IVIIHQ--ELTLVPElSVAENIFLgnEITLPGGRMAYNAMYlrakNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALN 157
|
170 180
....*....|....*....|....*.
gi 612672732 396 SKADIIFLDEPTFGLDSHNTFQLIKL 421
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDI 183
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
272-420 |
1.90e-07 |
|
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: 51.73 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAA--KHMYLVYQNPELqfITNSVYDEINIHF 348
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLALFRLVElSSGSILIDGVDISKIGLHDlrSRISIIPQDPVL--FSGTIRSNLDPFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 NHlskdqSDDETIQLLKLLDLENVKDQHPYEL-----------SIGQKRRLSVATALSSKADIIFLDEPTFGLDSHnTFQ 417
Cdd:cd03244 103 EY-----SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPE-TDA 176
|
...
gi 612672732 418 LIK 420
Cdd:cd03244 177 LIQ 179
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-161 |
2.15e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.51 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsgqrkifDHL----NITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlieLPMKYDELIVD------- 69
Cdd:PRK10771 1 MLKLTDITWLY--------HHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGF------LTPASGSLTLNgqdhttt 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 -----PLSgVIFQDpDSQFCMPKVYEELAFVLEnrqvPREDMDALIINALNMVNLNVTPETYIK----DLSGGMKQKLAI 140
Cdd:PRK10771 67 ppsrrPVS-MLFQE-NNLFSHLTVAQNIGLGLN----PGLKLNAAQREKLHAIARQMGIEDLLArlpgQLSGGQRQRVAL 140
|
170 180
....*....|....*....|.
gi 612672732 141 VETILQQSKTLFLDEPTAMLD 161
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALD 161
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
245-450 |
2.39e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 245 PTTNSHLLQFKNGRIIRGKSTLLSfsdleigLGEWITITGANGSGKTTLLESIMQLIK---YQGDVYFENQRLTKikHAA 321
Cdd:PLN03211 69 PKISDETRQIQERTILNGVTGMAS-------PGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKPTK--QIL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 322 KHMYLVYQN----PELQFITNSVYDEINIHFNHLSKDQS---DDETIQLLKLLDLEN--VKDQHPYELSIGQKRRLSVAT 392
Cdd:PLN03211 140 KRTGFVTQDdilyPHLTVRETLVFCSLLRLPKSLTKQEKilvAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAH 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 393 ALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDdeiieryPSRRL 450
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ-------PSSRV 270
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
271-438 |
2.78e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.54 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTL------LESIMqlikyQGDVYFENQRLTKIKHAAKHMYLVYQN----PELqfitnSV 340
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLlrmvagLERIT-----SGEIWIGGRVVNELEPADRDIAMVFQNyalyPHM-----SV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 341 YDeiNIHFN----HLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTF 416
Cdd:PRK11650 94 RE--NMAYGlkirGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRV 171
|
170 180
....*....|....*....|....*.
gi 612672732 417 QL---IKLFQKRinLGQ-SIFmVTHD 438
Cdd:PRK11650 172 QMrleIQRLHRR--LKTtSLY-VTHD 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-187 |
2.79e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 15 QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP--NLIELPMKYDELIVDPL---SGVIFQDpDSQFCMPKVY 89
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKQIlkrTGFVTQD-DILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 90 EELAFV----LEN---RQVPREDMDALIIN-ALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLD 161
Cdd:PLN03211 159 ETLVFCsllrLPKsltKQEKILVAESVISElGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*..
gi 612672732 162 VQATEDLWTKLIELWED-QTVVIVEHK 187
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKgKTIVTSMHQ 265
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
246-437 |
3.10e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 246 TTNSHLLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ---GDVYFENQRLTKI---KH 319
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKileGDILFKGESILDLepeER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 320 AAKHMYLVYQNP-ELQFITNSvyDEINIHFNHLSKDQSDDETIQL---------LKLLDLE------NVKDQhpyeLSIG 383
Cdd:CHL00131 82 AHLGIFLAFQYPiEIPGVSNA--DFLRLAYNSKRKFQGLPELDPLefleiinekLKLVGMDpsflsrNVNEG----FSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 384 QKRR---LSVATaLSSKADIifLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTH 437
Cdd:CHL00131 156 EKKRneiLQMAL-LDSELAI--LDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
280-412 |
3.27e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.80 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 280 ITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAA--KHMYLVYQNPELqfITNSVYDEINihfnhLSKDQS 356
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTeGEIRLDGRPLSSLSHSVlrQGVAMVQQDPVV--LADTFLANVT-----LGRDIS 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 357 DD------ETIQLLKLL-----DLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:PRK10790 443 EEqvwqalETVQLAELArslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-208 |
3.44e-07 |
|
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: 52.51 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 16 RKIFDHLNITIQDKEKVLLLGPSGCGKSTLL-------NVLSGIVpnlielpmkydeLI-------VDPLS-----GVIF 76
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfyDVTSGRI------------LIdgqdirdVTQASlraaiGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 QDP----DSqfcmpkVYEELAFvlenrqvPREDM-DALIINALNMVNL----NVTPETY--------IKdLSGGMKQKLA 139
Cdd:COG5265 439 QDTvlfnDT------IAYNIAY-------GRPDAsEEEVEAAARAAQIhdfiESLPDGYdtrvgergLK-LSGGEKQRVA 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 140 IVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHIwNHVDRVILMDyNGNII 208
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI-VDADEILVLE-AGRIV 571
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
268-450 |
3.65e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 51.93 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 268 SFSDLEIGLGEWIT-ITGANGSGKTTLLESIMQLIKYQGDVYFE---------------------NQRLTKIKHAAKH-- 323
Cdd:COG3593 13 SIKDLSIELSDDLTvLVGENNSGKSSILEALRLLLGPSSSRKFDeedfylgddpdlpeieieltfGSLLSRLLRLLLKee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 324 ------MYLVYQNPELQFITNSVYDEINIHFNHLSKDQ------SDDETIQLLKLLDLeNVKDQHPY---ELSIGQKRRL 388
Cdd:COG3593 93 dkeeleEALEELNEELKEALKALNELLSEYLKELLDGLdlelelSLDELEDLLKSLSL-RIEDGKELpldRLGSGFQRLI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 389 SVATAL-------SSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRL 450
Cdd:COG3593 172 LLALLSalaelkrAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPLENI 240
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-191 |
3.93e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.41 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 4 VSDLRLKYPSGQRkIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlieLPMKYDELIVD--PLS--------- 72
Cdd:PRK10790 343 IDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY------YPLTEGEIRLDgrPLSslshsvlrq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 GV--IFQDP----DSQFcmpkvyeelafvlENRQVPREDMDALIINALNMVNLN----VTPE---TYI----KDLSGGMK 135
Cdd:PRK10790 416 GVamVQQDPvvlaDTFL-------------ANVTLGRDISEEQVWQALETVQLAelarSLPDglyTPLgeqgNNLSVGQK 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIVEHKVKHI 191
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI 538
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
271-455 |
4.14e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKyqGDVYFENQ------------RLTK-IKHAAKHMYLVYQnpelQF-I 336
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT--GDKSAGSHiellgrtvqregRLARdIRKSRANTGYIFQ----QFnL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 337 TN--SVYDEINIH-----------FNHLSKDQSDdETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFL 403
Cdd:PRK09984 98 VNrlSVLENVLIGalgstpfwrtcFSWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 612672732 404 DEPTFGLDSHNTfQLIKLFQKRINLGQSIFMVT--HDDEIIERYPSRRLKISDG 455
Cdd:PRK09984 177 DEPIASLDPESA-RIVMDTLRDINQNDGITVVVtlHQVDYALRYCERIVALRQG 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
284-462 |
4.47e-07 |
|
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: 52.71 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 284 GANGSGKTTLLESIMQLI-KYQGDVYFENQRL-TKIKHAAKHMYLVYQNpelqfitnsvydeiNIHFNHL---------- 351
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLpPTSGTVLVGGKDIeTNLDAVRQSLGMCPQH--------------NILFHHLtvaehilfya 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 352 -----SKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRI 426
Cdd:TIGR01257 1029 qlkgrSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
|
170 180 190
....*....|....*....|....*....|....*.
gi 612672732 427 NlGQSIFMVTHDDEIIERYPSRRLKISDGALLdCDG 462
Cdd:TIGR01257 1109 S-GRTIIMSTHHMDEADLLGDRIAIISQGRLY-CSG 1142
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
251-461 |
4.55e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQL------------IKYQG-DVYFENQRLTKI 317
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpevtitgsIVYNGhNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 318 KhaaKHMYLVYQNPE---LQFITNSVYdeiNIHFNHLSKDQSDDETIQ--LLKLLDLENVKDQ---HPYELSIGQKRRLS 389
Cdd:PRK14239 85 R---KEIGMVFQQPNpfpMSIYENVVY---GLRLKGIKDKQVLDEAVEksLKGASIWDEVKDRlhdSALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 390 VATALSSKADIIFLDEPTFGLDSHNTFQ----LIKLFQKrinlgQSIFMVTHDDEIIERYPSRRLKISDGALLDCD 461
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKieetLLGLKDD-----YTMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
284-438 |
5.17e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.94 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 284 GANGSGKTTLLESIMQL------IKYQGDVYFENQRL--TKIKHAA--KHMYLVYQNPELqfITNSVYDeiNIHFN-HLS 352
Cdd:PRK14243 43 GPSGCGKSTILRCFNRLndlipgFRVEGKVTFHGKNLyaPDVDPVEvrRRIGMVFQKPNP--FPKSIYD--NIAYGaRIN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 353 KDQSD-DETIQ--LLKLLDLENVKD---QHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKri 426
Cdd:PRK14243 119 GYKGDmDELVErsLRQAALWDEVKDklkQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE-- 196
|
170
....*....|....
gi 612672732 427 nLGQ--SIFMVTHD 438
Cdd:PRK14243 197 -LKEqyTIIIVTHN 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-186 |
6.22e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.16 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 15 QRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP------NLIELPM-KYDELIVDPLS----GVIFQdpdSQF 83
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgssgevSLVGQPLhQMDEEARAKLRakhvGFVFQ---SFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 84 CMPKVYeelafVLENRQVP-----------REDMDALiinaLNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLF 152
Cdd:PRK10584 99 LIPTLN-----ALENVELPallrgessrqsRNGAKAL----LEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 612672732 153 LDEPTAMLDVQATEDLWTKLIELWEDQ--TVVIVEH 186
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
271-412 |
7.44e-07 |
|
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: 49.92 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAA--KHMYLVYQNPELqfITNSVYDeiNIH 347
Cdd:cd03251 22 SLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASlrRQIGLVSQDVFL--FNDTVAE--NIA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 348 FNhlSKDQSDDETIQLLKLLDLENVKDQHP--YE---------LSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:cd03251 98 YG--RPGATREEVEEAARAANAHEFIMELPegYDtvigergvkLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-202 |
8.33e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 17 KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPNlielpMKYDELIVdplsgviFQDPDSQFCMPK--------- 87
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH-----GSYEGEIL-------FDGEVCRFKDIRdsealgivi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 88 VYEELAFV----------LENRQVPRE--DMDALIINA---LNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLF 152
Cdd:NF040905 83 IHQELALIpylsiaenifLGNERAKRGviDWNETNRRArelLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 612672732 153 LDEPTAMLDVQATEDLWTKLIELwEDQ--TVVIVEHKVKHIWNHVDRV-ILMD 202
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLEL-KAQgiTSIIISHKLNEIRRVADSItVLRD 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
271-438 |
8.77e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.99 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLE-----------SIM-----------QLIKYQGDV-YFENQRLTKIKHAAKHMyLV 327
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNcltgfykptggTILlrgqhieglpgHQIARMGVVrTFQHVRLFREMTVIENL-LV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 328 YQNPELQfiTNSVYDEINIHFNHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPT 407
Cdd:PRK11300 104 AQHQQLK--TGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190
....*....|....*....|....*....|..
gi 612672732 408 FGLDSHNTFQLIKLF-QKRINLGQSIFMVTHD 438
Cdd:PRK11300 182 AGLNPKETKELDELIaELRNEHNVTVLLIEHD 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-209 |
8.95e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.27 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP----NLIELPMKYDELIVDPLSGVIFQ 77
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRD-ASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlasgKISILGQPTRQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 78 DPDSQFCMPKVYEELafVLENR-------QVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKT 150
Cdd:PRK15056 86 SEEVDWSFPVLVEDV--VMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 151 LFLDEPTAMLDVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRVILMdyNGNIIA 209
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMV--KGTVLA 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-208 |
9.29e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 17 KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVP---------------NLIELPMKYDELIVDPLSGVIFQDPDS 81
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmaeklefngqDLQRISEKERRNLVGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 82 QF--CMPKVYEELAFVLENRQVPREDMDALIINALNMVNLNvTPET----YIKDLSGGMKQKLAIVETILQQSKTLFLDE 155
Cdd:PRK11022 101 SLnpCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIP-DPASrldvYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 156 PTAMLDVQATEDLWTKLIELW--EDQTVVIVEHKVKHIWNHVDRVILMdYNGNII 208
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEAAHKIIVM-YAGQVV 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
116-442 |
9.95e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 116 MVNLNVTPETYIKD---LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATedLWTKLIELWEDQTVVIVEHKVKHIW 192
Cdd:PLN03073 328 LAGLSFTPEMQVKAtktFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAV--LWLETYLLKWPKTFIVVSHAREFLN 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 193 NHVDRVI------LMDYNGNIIADE---CPEIILQKYVHLLSEYGVWHPRAW-----------EFAPSRV---------- 242
Cdd:PLN03073 406 TVVTDILhlhgqkLVTYKGDYDTFErtrEEQLKNQQKAFESNERSRSHMQAFidkfrynakraSLVQSRIkaldrlghvd 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 243 ----------DFPTTNShllqfkngriiRGKSTLLSFSDLEIG----------------LGEWITITGANGSGKTTLLES 296
Cdd:PLN03073 486 avvndpdykfEFPTPDD-----------RPGPPIISFSDASFGypggpllfknlnfgidLDSRIAMVGPNGIGKSTILKL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 297 IM-QLIKYQGDVYfenqRLTKIKHAAKHMYLV-----YQNPELQFI---TNSVYDEINIHFNHLSKDQsddetiqllkll 367
Cdd:PLN03073 555 ISgELQPSSGTVF----RSAKVRMAVFSQHHVdgldlSSNPLLYMMrcfPGVPEQKLRAHLGSFGVTG------------ 618
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 368 dleNVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIK---LFQKrinlgqSIFMVTHDDEII 442
Cdd:PLN03073 619 ---NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQglvLFQG------GVLMVSHDEHLI 687
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
271-464 |
1.05e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 49.69 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVY--------------FenqrltkikhaakhmylvyqNPELqf 335
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEpTSGRVEvngrvsallelgagF--------------------HPEL-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 336 itnSVYDeiNIHFN----HLSKDQSD---DETI---QLLKLLDLEnVKDqhpYelSIGQKRRLSVATALSSKADIIFLDE 405
Cdd:COG1134 104 ---TGRE--NIYLNgrllGLSRKEIDekfDEIVefaELGDFIDQP-VKT---Y--SSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672732 406 ptfGL---DSHntFQ--LIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDGALLDcDGDT 464
Cdd:COG1134 173 ---VLavgDAA--FQkkCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM-DGDP 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
267-437 |
1.08e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSDLEIGLGEWITITGANGSGKTTLLESIMqlikyqGDVYFENQRLTKIKHAAKHMylvyqnPELQFITNSVYDEiNI 346
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAML------GELSHAETSSVVIRGSVAYV------PQVSWIFNATVRE-NI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 347 HFNhlskdqSDDETIQLLKLLDLENVkdQHPYEL----------------SIGQKRRLSVATALSSKADIIFLDEPTFGL 410
Cdd:PLN03232 700 LFG------SDFESERYWRAIDVTAL--QHDLDLlpgrdlteigergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180
....*....|....*....|....*..
gi 612672732 411 DSHNTFQLIKLFQKRINLGQSIFMVTH 437
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTN 798
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
277-437 |
1.32e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAAKH---MYLVYQNPELqFITNSVYDeiNIHFNhLS 352
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCARLTPAKAHqlgIYLVPQEPLL-FPNLSVKE--NILFG-LP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 353 KDQSDDETI-QLLKLL----DLE------NVKDQHPYELSIGQKRrlsvatalssKADIIFLDEPTFGLDSHNTFQLIKL 421
Cdd:PRK15439 113 KRQASMQKMkQLLAALgcqlDLDssagslEVADRQIVEILRGLMR----------DSRILILDEPTASLTPAETERLFSR 182
|
170
....*....|....*.
gi 612672732 422 FQKRINLGQSIFMVTH 437
Cdd:PRK15439 183 IRELLAQGVGIVFISH 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-219 |
1.44e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSgivpnlielpmkydeLIVDPLSGVIFQD--P 79
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALF---------------RIVELERGRILIDgcD 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 80 DSQFCMPKVYEELAFVlenRQVP--------------REDMDALIINAL-----------NMVNLNVTPETYIKDLSGGM 134
Cdd:PLN03130 1303 ISKFGLMDLRKVLGII---PQAPvlfsgtvrfnldpfNEHNDADLWESLerahlkdvirrNSLGLDAEVSEAGENFSVGQ 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 135 KQKLAIVETILQQSKTLFLDEPTAMLDVQaTEDLWTKLI-ELWEDQTVVIVEHKVKHIWNhVDRVILMDyNGNIIADECP 213
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIrEEFKSCTMLIIAHRLNTIID-CDRILVLD-AGRVVEFDTP 1456
|
....*.
gi 612672732 214 EIILQK 219
Cdd:PLN03130 1457 ENLLSN 1462
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
348-441 |
1.71e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 348 FNHLSKDQSDDETI----QLLKLLDLENVKDQ-----HPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQL 418
Cdd:PLN03140 979 FLRLPKEVSKEEKMmfvdEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1058
|
90 100
....*....|....*....|...
gi 612672732 419 IKLFQKRINLGQSIFMVTHDDEI 441
Cdd:PLN03140 1059 MRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
267-420 |
1.80e-06 |
|
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: 49.47 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVYFENQRLTKI--KHAAKHMYLVyqnPELQFI-TNSVYDE 343
Cdd:cd03289 23 ISFS---ISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVplQKWRKAFGVI---PQKVFIfSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INIHFNHlskdqSDDETIQLLKLLDLENVKDQHP-----------YELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:cd03289 97 LDPYGKW-----SDEEIWKVAEEVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
....*...
gi 612672732 413 hNTFQLIK 420
Cdd:cd03289 172 -ITYQVIR 178
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
251-448 |
1.86e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESI---MQL----IKYQGDVYFenQRLTK------- 316
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILngeVLLddgrIIYEQDLIV--ARLQQdpprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 317 ----------IKHAAKHMYlVYQNPELQFITNsvYDEINIhfNHLSKDQS----------DDETIQLLKLLDLEnvKDQH 376
Cdd:PRK11147 81 gtvydfvaegIEEQAEYLK-RYHDISHLVETD--PSEKNL--NELAKLQEqldhhnlwqlENRINEVLAQLGLD--PDAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 377 PYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDShNTFQLIKLFQKriNLGQSIFMVTHDDEIIERYPSR 448
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI-ETIEWLEGFLK--TFQGSIIFISHDRSFIRNMATR 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-207 |
1.96e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 9 LKYPSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVL-------SGIVPNLIELPMKY-----DELivdplsgvif 76
Cdd:PRK11147 325 VNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMlgqlqadSGRIHCGTKLEVAYfdqhrAEL---------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 77 qDPDSqfcmpKVYEELAfvlENRQ------VPREDM----DALIINALNMvnlnvTPetyIKDLSGGMKQKLAIVETILQ 146
Cdd:PRK11147 395 -DPEK-----TVMDNLA---EGKQevmvngRPRHVLgylqDFLFHPKRAM-----TP---VKALSGGERNRLLLARLFLK 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 147 QSKTLFLDEPTAMLDVQATEdLWTKLIELWEDqTVVIVEHKVKHIWNHVDRVILMDYNGNI 207
Cdd:PRK11147 458 PSNLLILDEPTNDLDVETLE-LLEELLDSYQG-TVLLVSHDRQFVDNTVTECWIFEGNGKI 516
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
113-229 |
2.24e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.02 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 113 ALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTkLIELWEDQ---TVVIVEHKVK 189
Cdd:PRK10575 131 AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA-LVHRLSQErglTVIAVLHDIN 209
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 612672732 190 HIWNHVDRVILMdYNGNIIADECPEIILQKYVhLLSEYGV 229
Cdd:PRK10575 210 MAARYCDYLVAL-RGGEMIAQGTPAELMRGET-LEQIYGI 247
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
280-442 |
2.45e-06 |
|
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: 46.98 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 280 ITITGANGSGKTTLLESIMQLIKYQGDVYFENqrltkikhaakhmylvyqnpelqfitnsvydeinihfnhlskdqSDDE 359
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------------DGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 360 TIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIK------LFQKRINLGQSIF 433
Cdd:smart00382 41 ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVI 120
|
....*....
gi 612672732 434 MVTHDDEII 442
Cdd:smart00382 121 LTTNDEKDL 129
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
260-443 |
2.76e-06 |
|
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: 47.43 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 260 IRGKSTLLSFSD--LEIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLT--KIKHAAKH-MYLVyqnPE- 332
Cdd:cd03215 7 VRGLSVKGAVRDvsFEVRAGEIVGIAGLVGNGQTELAEALFGLRPpASGEITLDGKPVTrrSPRDAIRAgIAYV---PEd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 333 -------LQFitnSVYDeiNIHFNHLskdqsddetiqllklldlenvkdqhpyeLSIGQKRRLSVATALSSKADIIFLDE 405
Cdd:cd03215 84 rkreglvLDL---SVAE--NIALSSL----------------------------LSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190
....*....|....*....|....*....|....*....
gi 612672732 406 PTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHD-DEIIE 443
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAGKAVLLISSElDELLG 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
262-420 |
2.76e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 262 GKSTL--LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIKYQGDVYFENQRLTKI--KHAAKHMYLVyqnPELQFI- 336
Cdd:TIGR01271 1231 GRAVLqdLSFS---VEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVtlQTWRKAFGVI---PQKVFIf 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 337 TNSVYDEINIHfnhlsKDQSDDETIQLLKLLDLENVKDQHP-----------YELSIGQKRRLSVATALSSKADIIFLDE 405
Cdd:TIGR01271 1305 SGTFRKNLDPY-----EQWSDEEIWKVAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170
....*....|....*
gi 612672732 406 PTFGLDShNTFQLIK 420
Cdd:TIGR01271 1380 PSAHLDP-VTLQIIR 1393
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
363-465 |
2.80e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.93 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 363 LLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDShNTFQLIKLFQKRIN--LGQSIFMVTHDDE 440
Cdd:COG4586 138 LVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV-VSKEAIREFLKEYNreRGTTILLTSHDMD 216
|
90 100
....*....|....*....|....*
gi 612672732 441 IIERYPSRRLKISDGALLdCDGDTN 465
Cdd:COG4586 217 DIEALCDRVIVIDHGRII-YDGSLE 240
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-208 |
3.94e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 47.24 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 12 PSGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlielpMKYDELIvdplSGVIF---QDPDSQFCMPKV 88
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG---------RKTAGVI----TGEILingRPLDKNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 89 YEELAFVLENRQVPREdmdALIINAlnmvnlnvtpetYIKDLSGGMKQKLAI-VETILQQSkTLFLDEPTAMLDVQATED 167
Cdd:cd03232 83 YVEQQDVHSPNLTVRE---ALRFSA------------LLRGLSVEQRKRLTIgVELAAKPS-ILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612672732 168 LWTKLIELWED-QTVVIVEHK-VKHIWNHVDRVILMDYNGNII 208
Cdd:cd03232 147 IVRFLKKLADSgQAILCTIHQpSASIFEKFDRLLLLKRGGKTV 189
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
277-438 |
4.34e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.00 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESI-MQLIKYQGDVYFENQ-----RLTKIKHAAKHMYL------VYQNPeLQFITNSVYDEI 344
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLrtewgfVHQHP-RDGLRMQVSAGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 NI----------HFNHLSKDQSDDetiqllklldLENVK------DQHPYELSIGQKRRLSVATALSSKADIIFLDEPTF 408
Cdd:PRK11701 111 NIgerlmavgarHYGDIRATAGDW----------LERVEidaariDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTG 180
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 409 GLDSHNTFQLIKLFQKRIN-LGQSIFMVTHD 438
Cdd:PRK11701 181 GLDVSVQARLLDLLRGLVReLGLAVVIVTHD 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
267-413 |
4.51e-06 |
|
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: 47.41 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIKHAA--KHMYLVYQNPELqfITNSVYDE 343
Cdd:cd03369 27 VSFK---VKAGEKIGIVGRTGAGKSTLILALFRFLEAeEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTL--FSGTIRSN 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 344 INIhFNHlskdQSDDETIQLLKLLDLENvkdqhpyELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSH 413
Cdd:cd03369 102 LDP-FDE----YSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-229 |
5.96e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSgqRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG-----IVPNLIEL---------PM-KYDE 65
Cdd:PRK13547 1 MLTADHLHVARRH--RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltggGAPRGARVtgdvtlngePLaAIDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 66 LIVDPLSGVIFQDPDSQF-----------CMPKVYEELAFVLENRQV-----PREDMDALiinalnmVNLNVTpetyikD 129
Cdd:PRK13547 79 PRLARLRAVLPQAAQPAFafsareivllgRYPHARRAGALTHRDGEIawqalALAGATAL-------VGRDVT------T 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 130 LSGGmkqKLAIVE--TILQQ----------SKTLFLDEPTAMLDVQATEDLWTKLIEL---WEDQTVVIVeHKVKHIWNH 194
Cdd:PRK13547 146 LSGG---ELARVQfaRVLAQlwpphdaaqpPRYLLLDEPTAALDLAHQHRLLDTVRRLardWNLGVLAIV-HDPNLAARH 221
|
250 260 270
....*....|....*....|....*....|....*
gi 612672732 195 VDRVILMDyNGNIIADECPEIILQKyVHLLSEYGV 229
Cdd:PRK13547 222 ADRIAMLA-DGAIVAHGAPADVLTP-AHIARCYGF 254
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-217 |
6.90e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.18 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGiVPNLIElpmkydelivdplSGVIFQDPD 80
Cdd:PRK11614 5 MLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRATS-------------GRIVFDGKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 81 -SQFCMPKVYEE-LAFVLENRQV-----------------PREDMDALIINALNMVnlnvtPETYIK------DLSGGMK 135
Cdd:PRK11614 69 iTDWQTAKIMREaVAIVPEGRRVfsrmtveenlamggffaERDQFQERIKWVYELF-----PRLHERriqragTMSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 136 QKLAIVETILQQSKTLFLDEPT---AMLDVQATEDLWTKLIElwEDQTVVIVEHKVKHIWNHVDRVILMDyNGNIIADEC 212
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDEPSlglAPIIIQQIFDTIEQLRE--QGMTIFLVEQNANQALKLADRGYVLE-NGHVVLEDT 220
|
....*
gi 612672732 213 PEIIL 217
Cdd:PRK11614 221 GDALL 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
284-443 |
7.92e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 284 GANGSGKTTLLESIMQLI-KYQGDVYFENQRL--TKIKHAAKH-MYLVYQnpEL-QFITNSVYDEI--------NIHFNH 350
Cdd:PRK10982 31 GENGAGKSTLLKCLFGIYqKDSGSILFQGKEIdfKSSKEALENgISMVHQ--ELnLVLQRSVMDNMwlgryptkGMFVDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 351 lskDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQ 430
Cdd:PRK10982 109 ---DKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGC 185
|
170
....*....|....
gi 612672732 431 SIFMVTHD-DEIIE 443
Cdd:PRK10982 186 GIVYISHKmEEIFQ 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
280-445 |
8.07e-06 |
|
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: 48.39 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 280 ITITGANGSGKTTLLEsIMQLI--KYQGDVYFenQRLTKIKHAAKHMYL-----VYQNPE--LQFITNSV--YDEINI-- 346
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLR-IMAGVdkDFNGEARP--QPGIKVGYLPQEPQLdptktVRENVEegVAEIKDALdrFNEISAky 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 347 -----HFNHLSKDQSD-DETIQLLKLLDLENV------------KDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTF 408
Cdd:TIGR03719 111 aepdaDFDKLAAEQAElQEIIDAADAWDLDSQleiamdalrcppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 612672732 409 GLDSHNTFQLIKLFQkriNLGQSIFMVTHDdeiieRY 445
Cdd:TIGR03719 191 HLDAESVAWLERHLQ---EYPGTVVAVTHD-----RY 219
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
342-456 |
8.55e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DEINIHFNHL-SKDQSDDETIQLLK-----LLDLenvkdQHPY--------ELSIGQKRRLSVATALSSKADII--FLDE 405
Cdd:PRK00635 430 QELFIFLSQLpSKSLSIEEVLQGLKsrlsiLIDL-----GLPYltperalaTLSGGEQERTALAKHLGAELIGItyILDE 504
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 612672732 406 PTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIErYPSRRLKISDGA 456
Cdd:PRK00635 505 PSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS-LADRIIDIGPGA 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
277-444 |
1.08e-05 |
|
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: 46.70 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTT---LLESIMQLikYQGDVYFENQRLTKIKHAAKH--MYLVYQNPELqfITNSVYDEINIHFNHL 351
Cdd:cd03248 40 GEVTALVGPSGSGKSTvvaLLENFYQP--QGGQVLLDGKPISQYEHKYLHskVSLVGQEPVL--FARSLQDNIAYGLQSC 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 352 SKDQ--------SDDETIQLLKLLDLENVkDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQ 423
Cdd:cd03248 116 SFECvkeaaqkaHAHSFISELASGYDTEV-GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALY 194
|
170 180
....*....|....*....|.
gi 612672732 424 KRiNLGQSIFMVTHDDEIIER 444
Cdd:cd03248 195 DW-PERRTVLVIAHRLSTVER 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
271-411 |
1.28e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.77 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIM-QLIKYQGdvyfenqrltKIKHAAKHMYlvyqNPELQFITNSVYDEiNIHFN 349
Cdd:cd03291 57 NLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEG----------KIKHSGRISF----SSQFSWIMPGTIKE-NIIFG 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 350 hLSKDQSDDETI--------QLLKLLDLEN-VKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:cd03291 122 -VSYDEYRYKSVvkacqleeDITKFPEKDNtVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
264-444 |
1.50e-05 |
|
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: 47.43 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 264 STLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTKIKHAAKHMYLVYQNPELQFITNSVYD 342
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARsGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 343 EINIHFNhlsKDQSDDETIQLLKLL----DLENVK-------DQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:TIGR01193 567 NLLLGAK---ENVSQDEIWAACEIAeikdDIENMPlgyqtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190
....*....|....*....|....*....|....
gi 612672732 412 shnTFQLIKLFQKRINLG-QSIFMVTHDDEIIER 444
Cdd:TIGR01193 644 ---TITEKKIVNNLLNLQdKTIIFVAHRLSVAKQ 674
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-436 |
1.51e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 17 KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIvpnlielpMKYDElivdplSGVIFQDPDSQFCMPK--------- 87
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--------YQKDS------GSILFQGKEIDFKSSKealengism 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 88 VYEELAFVLE-----NRQVPREDMDALIINALNMVN----------LNVTPETYIKDLSGGMKQKLAIVETILQQSKTLF 152
Cdd:PRK10982 78 VHQELNLVLQrsvmdNMWLGRYPTKGMFVDQDKMYRdtkaifdeldIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 153 LDEPTAMLDVQATEDLWtKLIELWEDQ--TVVIVEHKVKHIWNHVDRVILMDYNGNIIADECPEIILQKYVHLLseygVW 230
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLF-TIIRKLKERgcGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMM----VG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 231 HPRAWEFaPSRVDFPttNSHLLQFKNGRIIRGKSTL-LSFsdlEIGLGEWITITGANGSGKTTLLESIMQL-------IK 302
Cdd:PRK10982 233 RSLTQRF-PDKENKP--GEVILEVRNLTSLRQPSIRdVSF---DLHKGEILGIAGLVGAKRTDIVETLFGIreksagtIT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 303 YQGDVYFENQRLTKIKHAakhMYLVYQNPElqfiTNSVYDEINIHFNHL-SKDQSDDETIQLLK----------LLDLEN 371
Cdd:PRK10982 307 LHGKKINNHNANEAINHG---FALVTEERR----STGIYAYLDIGFNSLiSNIRNYKNKVGLLDnsrmksdtqwVIDSMR 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 372 VK----DQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVT 436
Cdd:PRK10982 380 VKtpghRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
282-442 |
1.56e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 282 ITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLTKIKHAakhmYLVYQNPELQF-ITNSVYDEINIHFNHLSKDQSDDE 359
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQpSSGNIYYKNCNINNIAKP----YCTYIGHNLGLkLEMTVFENLKFWSEIYNSAETLYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 360 TIQLLKLLDLenvKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDD 439
Cdd:PRK13541 107 AIHYFKLHDL---LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLE 183
|
...
gi 612672732 440 EII 442
Cdd:PRK13541 184 SSI 186
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-200 |
1.58e-05 |
|
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: 45.26 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 26 IQDKEKVLLLGPSGCGKSTLLNVLSGIVpnlielpmkydelivdplsgvifqdpdsqfcmpkvyeelafvlenrqVPRED 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQL-----------------------------------------------IPNGD 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 106 MDALiinalNMVNLNVTPEtYIkDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQ---ATEDLWTKLIELWEdQTVV 182
Cdd:cd03222 55 NDEW-----DGITPVYKPQ-YI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEEGK-KTAL 126
|
170
....*....|....*...
gi 612672732 183 IVEHKVKHIWNHVDRVIL 200
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHV 144
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-210 |
1.66e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.22 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYP-------SGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnlIELPmkyDELIV----D 69
Cdd:PRK10419 3 LLNVSGLSHHYAhgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-----LESP---SQGNVswrgE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 70 PLSG--------------VIFQDPDSQFCMPK-----VYEELAFVL----ENRQVPREDMdaliinaLNMVNLnvTPETY 126
Cdd:PRK10419 75 PLAKlnraqrkafrrdiqMVFQDSISAVNPRKtvreiIREPLRHLLsldkAERLARASEM-------LRAVDL--DDSVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 127 IK---DLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQatedLWTKLIELWED---QT---VVIVEHKVKHIWNHVDR 197
Cdd:PRK10419 146 DKrppQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV----LQAGVIRLLKKlqqQFgtaCLFITHDLRLVERFCQR 221
|
250
....*....|...
gi 612672732 198 VILMDyNGNIIAD 210
Cdd:PRK10419 222 VMVMD-NGQIVET 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
277-411 |
1.67e-05 |
|
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: 47.60 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIM-QLIKYQGdvyfenqrltKIKHAAKHMYlvyqNPELQFITNSVYDEiNIHFNhLSKDQ 355
Cdd:TIGR01271 452 GQLLAVAGSTGSGKSSLLMMIMgELEPSEG----------KIKHSGRISF----SPQTSWIMPGTIKD-NIIFG-LSYDE 515
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 356 ----SDDETIQLLKLLDLENVKDQHPY-----ELSIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:TIGR01271 516 yrytSVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
277-420 |
1.95e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.01 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIMQLIKY-QGDVYFENQRLTKIK--HAAKHMYLVYQNPELqfITNSVYDeiNIHFNHLSK 353
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDVsEGDIRFHDIPLTKLQldSWRSRLAVVSQTPFL--FSDTVAN--NIALGRPDA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 354 DQSDDETIQllkllDLENVKDQ-----HPYE---------LSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLI 419
Cdd:PRK10789 417 TQQEIEHVA-----RLASVHDDilrlpQGYDtevgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQIL 491
|
.
gi 612672732 420 K 420
Cdd:PRK10789 492 H 492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
122-207 |
2.55e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 122 TP--ETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELW-EDQTVVIVEHKVKHIWNHVDRV 198
Cdd:PRK10982 382 TPghRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGITDRI 461
|
....*....
gi 612672732 199 ILMDyNGNI 207
Cdd:PRK10982 462 LVMS-NGLV 469
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-191 |
3.50e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYPSGQR-KIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielPMKYDELIVDPLS-------- 72
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIINDSHNlkdinlkw 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -----GVIFQDP-------------------DSQFcMPKVYEELAFVLENRQVPREDMDALIINALNMVN---------- 118
Cdd:PTZ00265 458 wrskiGVVSQDPllfsnsiknnikyslyslkDLEA-LSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSnttdsnelie 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 119 -------------LNVTPETYIKD-------------------LSGGMKQKLAIVETILQQSKTLFLDEPTAMLDvQATE 166
Cdd:PTZ00265 537 mrknyqtikdsevVDVSKKVLIHDfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSE 615
|
250 260
....*....|....*....|....*...
gi 612672732 167 DLWTKLIELW---EDQTVVIVEHKVKHI 191
Cdd:PTZ00265 616 YLVQKTINNLkgnENRITIIIAHRLSTI 643
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
379-443 |
3.62e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 3.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 379 ELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHD-DEIIE 443
Cdd:PRK11288 140 YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRmEEIFA 205
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
361-442 |
4.27e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 361 IQLLKLLDLENVK-DQHPYELSIGQKRRLSVATALSSKAD---IIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVT 436
Cdd:TIGR00630 810 LQTLCDVGLGYIRlGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIE 889
|
....*.
gi 612672732 437 HDDEII 442
Cdd:TIGR00630 890 HNLDVI 895
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
260-445 |
4.27e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 260 IRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESImQLIkyqgdvyfenqrlTKIKHAAKHMYLVYQNPElqfitNS 339
Cdd:cd03227 4 LGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-GLA-------------LGGAQSATRRRSGVKAGC-----IV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 340 VYDEINIHFnhlSKDQsddetiqllklldlenvkdqhpyeLSIGQKRRLSVATALSS----KADIIFLDEPTFGLDSHNT 415
Cdd:cd03227 65 AAVSAELIF---TRLQ------------------------LSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 416 FQLIKLFqKRINLGQSIFMV-THDDEIIERY 445
Cdd:cd03227 118 QALAEAI-LEHLVKGAQVIViTHLPELAELA 147
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
277-436 |
4.60e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIM-QLIKYQGDVyfeNQRLTKIKHAAKHMylvyqnpELQFITNSVYD-EINIHFNHLSKD 354
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsNTDGFHIGV---EGVITYDGITPEEI-------KKHYRGDVVYNaETDVHFPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 355 QSDDETIQL------LKLLDLE----------------------NVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEP 406
Cdd:TIGR00956 157 ETLDFAARCktpqnrPDGVSREeyakhiadvymatyglshtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190
....*....|....*....|....*....|
gi 612672732 407 TFGLDSHNTFQLIKLFQKRINLGQSIFMVT 436
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
284-443 |
4.65e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 284 GANGSGKTTL---LESIMQL----IKYQG-DVYFENQRLTK-----IKHaaKHMYLVyqnPELQfITNSVY--DEINIHF 348
Cdd:PRK10762 37 GENGAGKSTMmkvLTGIYTRdagsILYLGkEVTFNGPKSSQeagigIIH--QELNLI---PQLT-IAENIFlgREFVNRF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 349 NHLSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINL 428
Cdd:PRK10762 111 GRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ 190
|
170
....*....|....*.
gi 612672732 429 GQSIFMVTHD-DEIIE 443
Cdd:PRK10762 191 GRGIVYISHRlKEIFE 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-186 |
5.07e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 2 LKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGivpnliELPmkydelivdPLSGVI------ 75
Cdd:PRK15064 320 LEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG------ELE---------PDSGTVkwsena 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 -----FQDPDSQFcmpkvyEELAFVLE----------NRQVPREDMDALIINAlNMVNLNVtpetyiKDLSGGMKQKLAI 140
Cdd:PRK15064 383 nigyyAQDHAYDF------ENDLTLFDwmsqwrqegdDEQAVRGTLGRLLFSQ-DDIKKSV------KVLSGGEKGRMLF 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 612672732 141 VETILQQSKTLFLDEPTAMLDVQATEDLWTKLiELWEDqTVVIVEH 186
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESLNMAL-EKYEG-TLIFVSH 493
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-206 |
5.60e-05 |
|
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: 45.51 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYPSGQrKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIVPnlielpmKYDELIVDPLSGVIF---Q 77
Cdd:TIGR00954 451 GIKFENIPLVTPNGD-VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP-------VYGGRLTKPAKGKLFyvpQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 78 DPdsQFCMPKVYEELAFVLENRQVPREDM-DALIINALNMVNLnvtpeTYI-------------KD-LSGGMKQKLAIVE 142
Cdd:TIGR00954 523 RP--YMTLGTLRDQIIYPDSSEDMKRRGLsDKDLEQILDNVQL-----THIlereggwsavqdwMDvLSGGEKQRIAMAR 595
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 143 TILQQSKTLFLDEPTAMLDVqateDLWTKLIELWEDQ--TVVIVEHKvKHIWNHVDRVILMDYNGN 206
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFgiTLFSVSHR-KSLWKYHEYLLYMDGRGG 656
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
271-443 |
6.65e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLikYQ---GDVYFENQRLTkI---KHAAKH---MylVYQNPELqFITNSVY 341
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGL--YQpdsGEILIDGKPVR-IrspRDAIALgigM--VHQHFML-VPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 342 DeiNI-------HFNHLSKDQSDDETIQLLKLLDLEnVK-DQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSH 413
Cdd:COG3845 99 E--NIvlgleptKGGRLDRKAARARIRELSERYGLD-VDpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQ 175
|
170 180 190
....*....|....*....|....*....|.
gi 612672732 414 NTFQLIKLFQKRINLGQSIFMVTHD-DEIIE 443
Cdd:COG3845 176 EADELFEILRRLAAEGKSIIFITHKlREVMA 206
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
381-443 |
7.33e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 45.47 E-value: 7.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 381 SIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIE 443
Cdd:NF041034 787 SIALALRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEELKE 849
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-209 |
7.64e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 34 LLGPSGCGKSTLLNVLSGIVpnlielpmKYDE-LIVdpLSGVIFQDPDSQFCMPKVYEELAFVL-ENRQVP--------- 102
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLT--------RPQKgRIV--LNGRVLFDAEKGICLPPEKRRIGYVFqDARLFPhykvrgnlr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 103 ---REDMDA--------LIINALnmvnLNVTPETyikdLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTK 171
Cdd:PRK11144 99 ygmAKSMVAqfdkivalLGIEPL----LDRYPGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612672732 172 LIELWEDQTVVI--VEHKVKHIWNHVDRVILMDyNGNIIA 209
Cdd:PRK11144 171 LERLAREINIPIlyVSHSLDEILRLADRVVVLE-QGKVKA 209
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
8-173 |
8.91e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 8 RLKYPSGQRKIFDhLNITIQDKEKVLLLGPSGCGKSTLLNVLSGIV-PNLIELPMKYDEL--IVDPLSGVIFQDPDSQFC 84
Cdd:PRK13541 6 QLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMqPSSGNIYYKNCNInnIAKPYCTYIGHNLGLKLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 85 MpKVYEELAFVLENRqvpreDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDvQA 164
Cdd:PRK13541 85 M-TVFENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KE 157
|
....*....
gi 612672732 165 TEDLWTKLI 173
Cdd:PRK13541 158 NRDLLNNLI 166
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
272-442 |
1.02e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 44.13 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 272 LEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDV-----YFENQRLTKI------KHAAKHMYLVYQNPE-------- 332
Cdd:COG4170 28 LTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVtadrfRWNGIDLLKLsprerrKIIGREIAMIFQEPSscldpsak 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 333 -----LQFITNSVYDEiniHFNHLSKdQSDDETIQLLK---LLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLD 404
Cdd:COG4170 108 igdqlIEAIPSWTFKG---KWWQRFK-WRKKRAIELLHrvgIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIAD 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 612672732 405 EPTFGLDSHNTFQLIKLFQK-RINLGQSIFMVTHDDEII 442
Cdd:COG4170 184 EPTNAMESTTQAQIFRLLARlNQLQGTSILLISHDLESI 222
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
320-443 |
1.03e-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: 44.30 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 320 AAKHMYLVYQNPELQFITNSvYDEINIHFNHLSKDQSDDETIQLLK------LLDLENVKDQHPYELSIGQKRRLSVATA 393
Cdd:pfam13304 172 AADLALFPDLKELLQRLVRG-LKLADLNLSDLGEGIEKSLLVDDRLrergliLLENGGGGELPAFELSDGTKRLLALLAA 250
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 612672732 394 LSS---KADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIE 443
Cdd:pfam13304 251 LLSalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
280-442 |
1.08e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 280 IT-ITGANGSGKTTLLESIMQLIKYQ-------GDVYFENQRLTKIKHAAKHMYLVYQNPELqFITNSVYDEINIHFNHL 351
Cdd:PRK11144 26 ITaIFGRSGAGKTSLINAISGLTRPQkgrivlnGRVLFDAEKGICLPPEKRRIGYVFQDARL-FPHYKVRGNLRYGMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 352 SKDQSDDetiqLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQ---KRINL 428
Cdd:PRK11144 105 MVAQFDK----IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLErlaREINI 180
|
170
....*....|....*
gi 612672732 429 gqSIFMVTHD-DEII 442
Cdd:PRK11144 181 --PILYVSHSlDEIL 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
122-201 |
1.23e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 122 TP--ETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWtKLIELW--EDQTVVIVEHKVKHIWNHVDR 197
Cdd:PRK10762 386 TPsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY-QLINQFkaEGLSIILVSSEMPEVLGMSDR 464
|
....
gi 612672732 198 VILM 201
Cdd:PRK10762 465 ILVM 468
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
267-444 |
1.23e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSdleIGLGEWITITGANGSGKTTLLESIMQLIK-YQGDVYFENQRLT--KIKHAAKHMYLVYQNPEL-----QFITN 338
Cdd:PRK15112 32 LSFT---LREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHfgDYSYRSQRIRMIFQDPSTslnprQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 339 SVydEINIHFN-HLSKDQSDDETIQLLKLLDL-ENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTF 416
Cdd:PRK15112 109 IL--DFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 612672732 417 QLIKL---FQKR-----INLGQSIFM---------VTHDDEIIER 444
Cdd:PRK15112 187 QLINLmleLQEKqgisyIYVTQHLGMmkhisdqvlVMHQGEVVER 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-179 |
1.26e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 29 KEKVLLLGPSGCGKSTLLNVLSGivpnlielpmkydeLIVDPLSGVIFQDPDSqfcmpkvyeelafvlenrqvpredmda 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAR--------------ELGPPGGGVIYIDGED--------------------------- 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672732 109 lIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQ 179
Cdd:smart00382 41 -ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-186 |
1.37e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSdlrlKYPSGQRKIFDhlNITIQ--DKEKVLLLGPSGCGKSTLLNVLSGIVPNlielpmkYD-ELIVDP-LS-GVI 75
Cdd:PRK11819 9 MNRVS----KVVPPKKQILK--DISLSffPGAKIGVLGLNGAGKSTLLRIMAGVDKE-------FEgEARPAPgIKvGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 76 FQDPD----------------SQFCMPKVYEELAfvlENRQVPREDMDAL---------IINALNMVNLNVT-------- 122
Cdd:PRK11819 76 PQEPQldpektvrenveegvaEVKAALDRFNEIY---AAYAEPDADFDALaaeqgelqeIIDAADAWDLDSQleiamdal 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672732 123 ----PETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEdlwtklielWEDQ-------TVVIVEH 186
Cdd:PRK11819 153 rcppWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA---------WLEQflhdypgTVVAVTH 218
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
251-443 |
1.41e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 251 LLQFKNGRIIRGKSTLLSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQ---GDVYFENQRLTKI---KHAAKHM 324
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKDLLELspeDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 325 YLVYQNP-EL-----QFITNSVYDEINIHFNHLSKDQSD-----DETIQLLKL-LDL----ENVKdqhpyeLSIGQKRRL 388
Cdd:PRK09580 81 FMAFQYPvEIpgvsnQFFLQTALNAVRSYRGQEPLDRFDfqdlmEEKIALLKMpEDLltrsVNVG------FSGGEKKRN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 612672732 389 SVATALSSKADIIFLDEPTFGLDshntFQLIKLFQKRINL----GQSIFMVTHDDEIIE 443
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLD----IDALKIVADGVNSlrdgKRSFIIVTHYQRILD 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-164 |
1.58e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 1 MLKVSDLRLKYpsGQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGiVP--NLIELPMKY---DELIVDPLS--- 72
Cdd:CHL00131 7 ILEIKNLHASV--NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPayKILEGDILFkgeSILDLEPEErah 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 73 -GVI--FQDPdsqFCMPKVYEE----LAFVLENRQVPREDMDAL----IINA-LNMVNLNvtpETYI-----KDLSGGMK 135
Cdd:CHL00131 84 lGIFlaFQYP---IEIPGVSNAdflrLAYNSKRKFQGLPELDPLefleIINEkLKLVGMD---PSFLsrnvnEGFSGGEK 157
|
170 180
....*....|....*....|....*....
gi 612672732 136 QKLAIVETILQQSKTLFLDEPTAMLDVQA 164
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDA 186
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
361-448 |
2.82e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 361 IQLLKLLDLENVKD---QHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQK-RINLGQSIFMVT 436
Cdd:PRK15093 137 IELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlNQNNNTTILLIS 216
|
90
....*....|..
gi 612672732 437 HDDEIIERYPSR 448
Cdd:PRK15093 217 HDLQMLSQWADK 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-457 |
3.78e-04 |
|
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: 43.08 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 277 GEWITITGANGSGKTTLLESIM-QLIKYQGDVYFENQR-LTKIKHAAKHMYLVYQNPEL-QFITNSVYDEINIHFNHLSK 353
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTgDTTVTSGDATVAGKSiLTNISDVHQNMGYCPQFDAIdDLLTGREHLYLYARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 354 DQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIF 433
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVV 2124
|
170 180
....*....|....*....|....
gi 612672732 434 MVTHDDEIIERYPSRRLKISDGAL 457
Cdd:TIGR01257 2125 LTSHSMEECEALCTRLAIMVKGAF 2148
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
278-411 |
4.43e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 278 EWITITGANGSGKTTLLESIMQLIKYQ-GDVYFENQRLTK--IKHAAKHMYLVYQNPELqfITNSVYDEINIHFNHlskd 354
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVL--FSGTVRFNIDPFSEH---- 1336
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 355 qSDDETIQLLKLLDLENVKDQHPYEL-----------SIGQKRRLSVATALSSKADIIFLDEPTFGLD 411
Cdd:PLN03232 1337 -NDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
90-210 |
4.49e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 90 EELAFVLENRQVPREDMDALIINALNMVNLNVTPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLW 169
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 612672732 170 TKLIELWED-QTVVIVEHKVKHIWNHVDRVILMDyNGNIIAD 210
Cdd:NF000106 185 DEVRSMVRDgATVLLTTQYMEEAEQLAHELTVID-RGRVIAD 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
122-210 |
5.24e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 122 TPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWtKLIELWEDQ--TVVIVEHKVKHIWNHVDRVI 199
Cdd:PRK13549 398 SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIY-KLINQLVQQgvAIIVISSELPEVLGLSDRVL 476
|
90
....*....|.
gi 612672732 200 LMdYNGNIIAD 210
Cdd:PRK13549 477 VM-HEGKLKGD 486
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
364-436 |
5.55e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 5.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672732 364 LKLLDLENVKD-----QHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVT 436
Cdd:PLN03140 316 LKILGLDICKDtivgdEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMS 393
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
252-427 |
5.90e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRI-IRGKSTLLSFSDLEIGLGEWIT--ITGANGSGKTTLLESIMQLIK-YQGDV-------------------- 307
Cdd:PTZ00265 383 IQFKNVRFhYDTRKDVEIYKDLNFTLTEGKTyaFVGESGCGKSTILKLIERLYDpTEGDIiindshnlkdinlkwwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 308 --------YFENQRLTKIKHAAKHMY-LVYQNPELQFITNSVYDEINIH----------FNHLSKDQSDDETIQLLKllD 368
Cdd:PTZ00265 463 gvvsqdplLFSNSIKNNIKYSLYSLKdLEALSNYYNEDGNDSQENKNKRnscrakcagdLNDMSNTTDSNELIEMRK--N 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 369 LENVKDQ-----------HPY-----------------ELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFqlik 420
Cdd:PTZ00265 541 YQTIKDSevvdvskkvliHDFvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY---- 616
|
....*..
gi 612672732 421 LFQKRIN 427
Cdd:PTZ00265 617 LVQKTIN 623
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
252-438 |
6.64e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.76 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLlsfsDLEIGLgewITITGANGSGKTTLLESIM---------------QLIKYQGD-----VYFEN 311
Cdd:COG0419 5 LRLENFRSYRDTETI----DFDDGL---NLIVGPNGAGKSTILEAIRyalygkarsrsklrsDLINVGSEeasveLEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 312 Q----RLTKiKHAAKHMYLVYQNPELQFITN-----SVYDEINIHFNHLsKDQSDDETIQLLKLLDLENV------KDQH 376
Cdd:COG0419 78 GgkryRIER-RQGEFAEFLEAKPSERKEALKrllglEIYEELKERLKEL-EEALESALEELAELQKLKQEilaqlsGLDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672732 377 PYELSIGQKRRLSVATALSskadiIFLDeptFG-LDSHNTFQLIKLFqkrinlgQSIFMVTHD 438
Cdd:COG0419 156 IETLSGGERLRLALADLLS-----LILD---FGsLDEERLERLLDAL-------EELAIITHV 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
351-465 |
6.85e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 351 LSKDQSDDETIQLLKLLDLENVKDQHPYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQ 430
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|....*
gi 612672732 431 SIFMVTHDDEIIERYpSRRLKISDGALLDCDGDTN 465
Cdd:NF000106 196 TVLLTTQYMEEAEQL-AHELTVIDRGRVIADGKVD 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
122-201 |
7.04e-04 |
|
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: 42.12 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 122 TPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWtKLIELWEDQ--TVVIVEHKVKHIWNHVDRVI 199
Cdd:TIGR02633 396 SPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIY-KLINQLAQEgvAIIVVSSELAEVLGLSDRVL 474
|
..
gi 612672732 200 LM 201
Cdd:TIGR02633 475 VI 476
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
326-444 |
8.24e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 326 LVYQNPELqfITNSVYDeiNIHFNHLSKDQSDDETIQLLKLLD--LENVKDQH-----PY--ELSIGQKRRLSVATALSS 396
Cdd:PTZ00265 1300 IVSQEPML--FNMSIYE--NIKFGKEDATREDVKRACKFAAIDefIESLPNKYdtnvgPYgkSLSGGQKQRIAIARALLR 1375
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 612672732 397 KADIIFLDEPTFGLDSHNTfqliKLFQKRI-----NLGQSIFMVTHDDEIIER 444
Cdd:PTZ00265 1376 EPKILLLDEATSSLDSNSE----KLIEKTIvdikdKADKTIITIAHRIASIKR 1424
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
119-209 |
9.60e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.54 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 119 LNV---TPETYIKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWEDQTVVIV------Ehkvk 189
Cdd:COG1129 381 LRIktpSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVisselpE---- 456
|
90 100
....*....|....*....|
gi 612672732 190 hIWNHVDRVILMdYNGNIIA 209
Cdd:COG1129 457 -LLGLSDRILVM-REGRIVG 474
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
267-413 |
1.10e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 267 LSFSDLEIGLGEWITITGANGSGKTTLLESIMQLIKYQGDvyfenqrlTKIKHAAKHMYLvyqnPELQFITN-SVYDEI- 344
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD--------ASVVIRGTVAYV----PQVSWIFNaTVRDNIl 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 345 ------------NIHFNHLSKDqsddetIQLLKLLDLENVKDQHpYELSIGQKRRLSVATALSSKADIIFLDEPTFGLDS 412
Cdd:PLN03130 701 fgspfdperyerAIDVTALQHD------LDLLPGGDLTEIGERG-VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
.
gi 612672732 413 H 413
Cdd:PLN03130 774 H 774
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
403-442 |
1.17e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 612672732 403 LDEPTFGLDSHNTFQLIKL--FQKRINLGQsIFMVTHDDEII 442
Cdd:PRK02224 817 LDEPTVFLDSGHVSQLVDLveSMRRLGVEQ-IVVVSHDDELV 857
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
268-297 |
1.31e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|.
gi 612672732 268 SFSDLEIGLGEWIT-ITGANGSGKTTLLESI 297
Cdd:pfam13476 8 SFRDQTIDFSKGLTlITGPNGSGKTTILDAI 38
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
252-443 |
1.76e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.41 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 252 LQFKNGRIIRGKSTLlSFSDLEIGLGEWITITGANGSGKTTLLESIMQL------------------------------- 300
Cdd:COG1106 5 FSIENFRSFKDELTL-SMVASGLRLLRVNLIYGANASGKSNLLEALYFLrnlvlnssqpgdklvepflldsesknepsef 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 301 --------IKYQGDVYFENQRLTK-----IKHAAKHMYLVYQNPELQFITNSVYDEINIHF-NHLSKDQSDDETI-QLLK 365
Cdd:COG1106 84 eilflldgVRYEYGFELDKERIISewlyfLSTAAQLNVPLLSPLYDWFDNNISLDTSSDGLtLLLKEDESLKEELlELLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 366 LLD--------------------LENVKDQHPYELSIGQ-----KRRLSVATAL---SSKADIIFLDEPTFGLDSHNTFQ 417
Cdd:COG1106 164 IADpgiedieveeeeiedlverkLIFKHKGGNVPLPLSEesdgtKRLLALAGALldaLAKGGVLLIDEIEASLHPSLLRK 243
|
250 260
....*....|....*....|....*..
gi 612672732 418 LIKLFQKRIN-LGQSIFMVTHDDEIIE 443
Cdd:COG1106 244 LLKLFLDLANkNNAQLIFTTHSTELLD 270
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
379-455 |
1.77e-03 |
|
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: 39.48 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 379 ELSIGQKRRLSVATALSSKADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIERYPSRRLKISDG 455
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
268-297 |
2.27e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 2.27e-03
10 20 30
....*....|....*....|....*....|
gi 612672732 268 SFSDLEIGLGEWITITGANGSGKTTLLESI 297
Cdd:COG4637 12 SLRDLELPLGPLTVLIGANGSGKSNLLDAL 41
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
268-332 |
2.29e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.98 E-value: 2.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672732 268 SFSDLEIGLGE---WITITGANGSGKTTLLESI----MQLIKYQGDVYFENQRLTKIKHAAKHMYLVYQNPE 332
Cdd:COG3950 13 GFEDLEIDFDNpprLTVLVGENGSGKTTLLEAIalalSGLLSRLDDVKFRKLLIRNGEFGDSAKLILYYGTS 84
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-51 |
2.47e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 2.47e-03
10 20 30
....*....|....*....|....*....|....*...
gi 612672732 14 GQRKIFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG 51
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
127-201 |
2.68e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 2.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 127 IKDLSGGMKQKLAIVETILQQSKTLFLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIWNHVDRVILM 201
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVF 482
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
119-201 |
3.13e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.89 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 119 LNV-TP--ETYIKDLSGGMKQKlAIVETILQQS-KTLFLDEPTAMLDVQATEDLWTKLIELWED-QTVVIVEHKVKHIWN 193
Cdd:PRK11288 383 LNIkTPsrEQLIMNLSGGNQQK-AILGRWLSEDmKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLG 461
|
....*...
gi 612672732 194 HVDRVILM 201
Cdd:PRK11288 462 VADRIVVM 469
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
380-443 |
4.20e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 4.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672732 380 LSIGQKRRLSVATALSSK--ADIIFLDEPTFGLDSHNTFQLIKLFQKRINLGQSIFMVTHDDEIIE 443
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR 554
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
271-301 |
4.47e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 4.47e-03
10 20 30
....*....|....*....|....*....|.
gi 612672732 271 DLEIGLGEWITITGANGSGKTTLLESIMQLI 301
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
250-297 |
4.87e-03 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 38.98 E-value: 4.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 612672732 250 HLLQFKNgriirgkstllsFSDLEIGLGEWIT-ITGANGSGKTTLLESI 297
Cdd:COG1195 6 SLTNFRN------------YESLELEFSPGINvLVGPNGQGKTNLLEAI 42
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-201 |
5.33e-03 |
|
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: 39.51 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 18 IFDHLNITIQDKEKVLLLGPSGCGKSTLLNVLSG-IVPNliELPMKYdelivdplSGVIFQDPDSQFCMP-KVYEELAFV 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPS--EGKIKH--------SGRISFSPQTSWIMPgTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672732 96 L---ENRQVPredmdalIINALNMV-NLNVTPEtyiKD----------LSGGMKQKLAIVETILQQSKTLFLDEPTAMLD 161
Cdd:TIGR01271 511 LsydEYRYTS-------VIKACQLEeDIALFPE---KDktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 612672732 162 VQATEDLWTK-LIELWEDQTVVIVEHKVKHIwNHVDRVILM 201
Cdd:TIGR01271 581 VVTEKEIFEScLCKLMSNKTRILVTSKLEHL-KKADKILLL 620
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-52 |
5.59e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 38.91 E-value: 5.59e-03
10 20 30
....*....|....*....|....*....|...
gi 612672732 20 DHLNITIQDKEKVLLLGPSGCGKSTLLNVLSGI 52
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI 71
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
27-82 |
9.12e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 37.25 E-value: 9.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 612672732 27 QDKEKVLLLGPSGCGKSTLLNVLSGI-VPNLIELpmkydelivdpLSGVIFQDPDSQ 82
Cdd:pfam03215 43 AKHRILLISGPSGCGKSTVIKELSKElGPKYREW-----------SNPTSFRSPPNQ 88
|
|
| |
