|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-499 |
3.69e-106 |
|
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: 327.25 E-value: 3.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDsdGEATGKLLIEGR----TPASA 92
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG--GRISGEVLLDGRdlleLSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGA-VGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMG 171
Cdd:COG1123 81 RGRrIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 172 ARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDYgQALtd 251
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP-QAL-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 252 agvwipGAPPALPDARSVAcdQDGHPSGDIAIETRELDIGYGAkkswfRGSETVePIARGVSVSIPSEASTCIVGHNGSG 331
Cdd:COG1123 238 ------AAVPRLGAARGRA--APAAAAAEPLLEVRNLSKRYPV-----RGKGGV-RAVDDVSLTLRRGETLGLVGESGSG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 332 KSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPS-KKLATRIGTVFQDPEHQFVTG-TVLEELQLGPKLVGV----NADKR 405
Cdd:COG1123 304 KSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlRELRRRVQMVFQDPYSSLNPRmTVGDIIAEPLRLHGLlsraERRER 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 406 IEELLERLRLTA-LTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITH 483
Cdd:COG1123 384 VAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISH 463
|
490
....*....|....*.
gi 1081004564 484 DPLVVQAMGDYVVDMD 499
Cdd:COG1123 464 DLAVVRYIADRVAVMY 479
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-245 |
1.94e-75 |
|
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: 238.00 E-value: 1.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAvLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG-----RTPASAR 93
Cdd:COG1122 1 IELENLSFSYPGGTPA-LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS-----GEVLVDGkditkKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GAVGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGAR 173
Cdd:COG1122 75 RKVGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 174 VICLDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDY 245
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLE-LLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-230 |
1.12e-73 |
|
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: 232.74 E-value: 1.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASARG 94
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS-----GEVLVDGKdltklSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 AVGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARV 174
Cdd:cd03225 76 KVGLVFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 175 ICLDEPTANIDPAGVPVLRdAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELL-ELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
298-499 |
1.12e-57 |
|
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: 191.14 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 298 WFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQD 377
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 378 PEHQFVTGTVLEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTF 454
Cdd:cd03225 84 PDDQFFGPTVEEEVAFGLENLGLPeeeIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081004564 455 GQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-257 |
1.01e-56 |
|
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: 190.72 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASA------ 92
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTS-----GKVTVDGLDTLDEenlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAVGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGA 172
Cdd:TIGR04520 76 RKKVGMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 173 RVICLDEPTANIDPAGvpvlRDAAITAAER----TGAALIVVEHRVDawvDVV--DRIIVLGRGGVIADGAPHRVLEDyG 246
Cdd:TIGR04520 156 DIIILDEATSMLDPKG----RKEVLETIRKlnkeEGITVISITHDME---EAVlaDRVIVMNKGKIVAEGTPREIFSQ-V 227
|
250
....*....|.
gi 1081004564 247 QALTDAGVWIP 257
Cdd:TIGR04520 228 ELLKEIGLDVP 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
306-499 |
3.94e-52 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 177.14 E-value: 3.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsAPWKWPSKKLATRIGTVFQDPEHQFVTG 385
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK--DITKKNLRELRRKVGLVFQNPDDQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFT 462
Cdd:COG1122 92 TVEEDVAFGPENLGLPreeIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081004564 463 ELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:COG1122 172 ELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLD 208
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
36-263 |
2.02e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 176.87 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAS--------ARGAVGLVLQDPDSQT 107
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTS-----GTVTIDGRDITAkkkkklkdLRKKVGLVFQFPEHQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLP-LDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:TIGR04521 96 FEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 187 AGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDYgQALTDAGVwipGAPPAL 263
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV-DELEKIGL---DVPEIT 248
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-238 |
2.01e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 163.75 E-value: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYRHaGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEGR-----TPASARGAVGL 98
Cdd:PRK13647 12 FRYKD-GTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI-----YLPQRGRVKVMGRevnaeNEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 VLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLD 178
Cdd:PRK13647 84 VFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 179 EPTANIDPAGVPVLRdAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAP 238
Cdd:PRK13647 164 EPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
35-244 |
2.86e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 163.33 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASA------RGAVGLVLQDPDSQTI 108
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE-----GKVYVDGLDTSDEenlwdiRNKAGMVFQNPDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAG 188
Cdd:PRK13633 100 ATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 189 VPVLRDAAITAAERTGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-257 |
8.38e-45 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 159.41 E-value: 8.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEAT--GKLLIEgRTPASARG 94
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA-GTITvgGMVLSE-ETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 AVGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARV 174
Cdd:PRK13635 82 QVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 175 ICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPHRVLEdYGQALTDAGV 254
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDE-AAQADRVIVMNKGEILEEGTPEEIFK-SGHMLQEIGL 239
|
...
gi 1081004564 255 WIP 257
Cdd:PRK13635 240 DVP 242
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
35-215 |
4.25e-44 |
|
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: 154.50 E-value: 4.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPA-------SARGAVGLVLQDPDSQT 107
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQS-----GAVLIDGEPLDysrkgllERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180 190
....*....|....*....|....*....|
gi 1081004564 188 GVPVLRDA--AITAAertGAALIVVEHRVD 215
Cdd:TIGR01166 162 GREQMLAIlrRLRAE---GMTVVISTHDVD 188
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-262 |
1.24e-42 |
|
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: 159.30 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 1 MTDEALTRGPSSSGNVPAVSARGFGYRHAGRKA---AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS--- 74
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSgsi 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 75 --DGEATGKLLieGRTPASARGAVGLVLQDPDSQtISAR--VGDDVAFGAENLGVAP-AEIGNRVRASLDLVGLDLP-LD 148
Cdd:COG1123 323 lfDGKDLTKLS--RRSLRELRRRVQMVFQDPYSS-LNPRmtVGDIIAEPLRLHGLLSrAERRERVAELLERVGLPPDlAD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 149 HPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAG----VPVLRDAAitaaERTGAALIVVEHrvDawVDVV--- 221
Cdd:COG1123 400 RYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQ----RELGLTYLFISH--D--LAVVryi 471
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1081004564 222 -DRIIVLGRGGVIADGAPHRVLEDYGQALTDAGVW-IPGAPPA 262
Cdd:COG1123 472 aDRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAaVPSLDPA 514
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-248 |
2.06e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 153.28 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 31 RKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASA-------RGAVGLVLQDP 103
Cdd:PRK13637 20 KKA--LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS-----GKIIIDGVDITDKkvklsdiRKKVGLVFQYP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLP--LDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPT 181
Cdd:PRK13637 93 EYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 182 ANIDPAGvpvlRDAAI----TAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRV------LEDYGQA 248
Cdd:PRK13637 173 AGLDPKG----RDEILnkikELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfkevetLESIGLA 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-244 |
2.46e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 152.69 E-value: 2.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAvLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-TPASARG------AVGL 98
Cdd:PRK13636 13 YNYSDGTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS-----GRILFDGKpIDYSRKGlmklreSVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 VLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLD 178
Cdd:PRK13636 87 VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 179 EPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
35-244 |
1.07e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 151.00 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPA-------SARGAVGLVLQDPDSQT 107
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS-----GEVLIKGEPIKydkksllEVRKTVGIVFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:PRK13639 92 FAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 188 GVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13639 172 GASQIMK-LLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-244 |
3.85e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 146.67 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAS----- 91
Cdd:PRK13632 6 VMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS-----GEIKIDGITISKenlke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 ARGAVGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMG 171
Cdd:PRK13632 81 IRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 172 ARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDE-AILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-257 |
4.61e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 146.48 E-value: 4.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEAtgKLLIEG-----RTPASA 92
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNS--KITVDGitltaKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAVGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGA 172
Cdd:PRK13640 83 REKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 173 RVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPHRVLEDYgQALTDA 252
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIFSKV-EMLKEI 240
|
....*
gi 1081004564 253 GVWIP 257
Cdd:PRK13640 241 GLDIP 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
31-236 |
7.10e-39 |
|
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: 141.12 E-value: 7.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 31 RKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT----PASARGaVGLVLQDP--- 103
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDS-----GEILIDGRDvtgvPPERRN-IGMVFQDYalf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DSQTisarVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTAN 183
Cdd:cd03259 85 PHLT----VAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 184 IDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
36-257 |
2.11e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 139.48 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR--TPASA---RGAVGLVLQDPDSQTISA 110
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES-----GQIIIDGDllTEENVwdiRHKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 RVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVP 190
Cdd:PRK13650 98 TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 191 VLRDAAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPhRVLEDYGQALTDAGVWIP 257
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTP-RELFSRGNDLLQLGLDIP 242
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
23-245 |
2.81e-37 |
|
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: 137.22 E-value: 2.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 23 GFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGAVGLVLQD 102
Cdd:cd03293 7 SKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS-----GEVLVDGEPVTGPGPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 PdsqtisA-----RVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICL 177
Cdd:cd03293 82 D------AllpwlTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 178 DEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGrggviadGAPHRVLEDY 245
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS-------ARPGRIVAEV 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-257 |
7.45e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 137.45 E-value: 7.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHagRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT-PASARGAVG 97
Cdd:PRK13638 2 LATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQK-----GAVLWQGKPlDYSKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 L------VLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMG 171
Cdd:PRK13638 75 LrqqvatVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 172 ARVICLDEPTANIDPAGvpvlRDAAITAAER---TGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEdYGQA 248
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAG----RTQMIAIIRRivaQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA-CTEA 229
|
....*....
gi 1081004564 249 LTDAGVWIP 257
Cdd:PRK13638 230 MEQAGLTQP 238
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-235 |
1.43e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.37 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 13 SGNVPAVSARG--FGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPA 90
Cdd:COG1116 2 SAAAPALELRGvsKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTS-----GEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 91 SARGAVGLVLQDPdsqtiS----ARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAG 166
Cdd:COG1116 77 GPGPDRGVVFQEP-----AllpwLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 167 VLAMGARVICLDEPTANIDpagvpvlrdaAITAA----------ERTGAALIVVEHRVDAWVDVVDRIIVLGR--GGVIA 234
Cdd:COG1116 152 ALANDPEVLLMDEPFGALD----------ALTRErlqdellrlwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
.
gi 1081004564 235 D 235
Cdd:COG1116 222 E 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-241 |
1.62e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 136.86 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAvLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASA-----R 93
Cdd:PRK13652 4 IETRDLCYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS-----GSVLIRGEPITKEnirevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GAVGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGAR 173
Cdd:PRK13652 78 KFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 174 VICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRV 241
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
36-257 |
4.25e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 135.92 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRTPA----SARGAVGLVLQDPDSQTISAR 111
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkPLRKKVGIVFQFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLP-LDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVP 190
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 191 VLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDyGQALTDAGVWIP 257
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD-PDELEAIGLDLP 248
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
308-499 |
4.71e-36 |
|
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: 133.15 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsapwKWPSKKLATRIGTVFQDPEHQFVTGTV 387
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-----PIKAKERRKSIGYVMQDVDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKLVGvNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTL 467
Cdd:cd03226 90 REELLLGLKELD-AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|..
gi 1081004564 468 LRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:cd03226 169 IRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-247 |
6.92e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 141.06 E-value: 6.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 9 GPSSSGNVPAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR- 87
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS-----GSITLGGVd 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 ----TPASARGAVGLVLQDPD--SQTIsarvgddvafgAENLGVAPAEIG-NRVRASLDLVGLD-----LP--LDHPTH- 152
Cdd:COG4987 399 lrdlDEDDLRRRIAVVPQRPHlfDTTL-----------RENLRLARPDATdEELWAALERVGLGdwlaaLPdgLDTWLGe 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 153 ---RLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA-GVPVLRDAAITAAERTgaaLIVVEHRvDAWVDVVDRIIVLG 228
Cdd:COG4987 468 ggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAAtEQALLADLLEALAGRT---VLLITHR-LAGLERMDRILVLE 543
|
250
....*....|....*....
gi 1081004564 229 RGGVIADGAPHRVLEDYGQ 247
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGR 562
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
311-484 |
9.89e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 134.50 E-value: 9.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG-SGSAPWKWPSKKLATRIGTVFQDPEHQFVTGTVLE 389
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrDITAKKKKKLKDLRKKVGLVFQFPEHQLFEETVYK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVN---ADKRIEELLERLRLT-ALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL 465
Cdd:TIGR04521 103 DIAFGPKNLGLSeeeAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEIL 182
|
170 180
....*....|....*....|
gi 1081004564 466 TLLRQLADD-GRTVISITHD 484
Cdd:TIGR04521 183 DLFKRLHKEkGLTVILVTHS 202
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
299-499 |
1.71e-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: 133.71 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG--SGSAPWKWPSKKlatRIGTVFQ 376
Cdd:TIGR04520 8 FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldTLDEENLWEIRK---KVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 377 DPEHQFVTGTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPT 453
Cdd:TIGR04520 85 NPDNQFVGATVEDDVAFGLENLGVPREemrKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081004564 454 FGQDRRTFTELLTLLRQLADD-GRTVISITHDP-LVVQAmgDYVVDMD 499
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEeGITVISITHDMeEAVLA--DRVIVMN 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-242 |
3.07e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.14 E-value: 3.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGAV 96
Cdd:COG1121 5 PAIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTS-----GTVRLFGKPPRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 GLVLQDPDSQ-TISARVGDDVAFGAEN----LGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMG 171
Cdd:COG1121 78 GYVPQRAEVDwDFPITVRDVVLMGRYGrrglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 172 ARVICLDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRgGVIADGAPHRVL 242
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEVL 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
23-239 |
6.80e-35 |
|
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: 131.08 E-value: 6.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 23 GFGYRHagrkaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA------- 95
Cdd:cd03261 9 SFGGRT------VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS-----GEVLIDGEDISGLSEAelyrlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 -VGLVLQDP---DSQTisarVGDDVAFG-AENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAM 170
Cdd:cd03261 78 rMGMLFQSGalfDSLT----VFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 171 GARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPH 239
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
36-263 |
8.23e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 132.03 E-value: 8.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAS------ARGAVGLVLQDPDSQTIS 109
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK-----GKVLVSGIDTGDfsklqgIRKLVGIVFQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP-AG 188
Cdd:PRK13644 93 RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPdSG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 189 VPVLRDaaITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPHRVLEDYgqALTDAGVwipgAPPAL 263
Cdd:PRK13644 173 IAVLER--IKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV--SLQTLGL----TPPSL 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-257 |
1.22e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.41 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgDDSDGEAT-GKLLIEGRTPASARGAVGLVLQDPD 104
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE-KVKSGEIFyNNQAITDDNFEKLRKHIGIVFQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 105 SQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANI 184
Cdd:PRK13648 94 NQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 185 DPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHRVLEDyGQALTDAGVWIP 257
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH-AEELTRIGLDLP 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-498 |
2.98e-34 |
|
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: 135.97 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKS-TLLaAIAGVLGdDSDGEATGKLLIEGR----TPASA----RGA- 95
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLP-DPAAHPSGSILFDGQdllgLSERElrriRGNr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 VGLVLQDPdsqtISA-----RVGDDVafgAENL----GVAPAEIGNRVRASLDLVGLDLP---LDHPTHRLSGGQKQRLA 163
Cdd:COG4172 94 IAMIFQEP----MTSlnplhTIGKQI---AEVLrlhrGLSGAAARARALELLERVGIPDPerrLDAYPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 164 LAGVLAMGARVICLDEPTANIDpagVPV-------LRDaaitAAERTGAALIVVEHrvdawvD--VV----DRIIVLGRG 230
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALD---VTVqaqildlLKD----LQRELGMALLLITH------DlgVVrrfaDRVAVMRQG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 231 GVIADGAPHRVLE----DYGQALTDAgvwIP-GAPPALPdarsvacdqdghPSGDIAIETRELDIGYGAKKSWFRGseTV 305
Cdd:COG4172 234 EIVEQGPTAELFAapqhPYTRKLLAA---EPrGDPRPVP------------PDAPPLLEARDLKVWFPIKRGLFRR--TV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPI--ARGVSVSIPSEASTCIVGHNGSGKSTLAltlggllepMA--------GTVQVAGsgsAPW-KWPSKKLAT---RI 371
Cdd:COG4172 297 GHVkaVDGVSLTLRRGETLGLVGESGSGKSTLG---------LAllrlipseGEIRFDG---QDLdGLSRRALRPlrrRM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 372 GTVFQDPehqF--------VTGTVLEELQL-GPKLVGVNADKRIEELLERLRLTALTKAN-PFSLSGGEKRRLSVATMLA 441
Cdd:COG4172 365 QVVFQDP---FgslsprmtVGQIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALI 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 442 TAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVM 499
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
17-246 |
5.48e-34 |
|
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: 136.50 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPAS 91
Cdd:COG2274 472 GDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS-----GRILIDGIdlrqiDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 ARGAVGLVLQDPD--SQTISarvgDDVAFGAENLGVApaeignRVRASLDLVGLD-----LP--LDHP----THRLSGGQ 158
Cdd:COG2274 547 LRRQIGVVLQDVFlfSGTIR----ENITLGDPDATDE------EIIEAARLAGLHdfieaLPmgYDTVvgegGSNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 159 KQRLALAGVLAMGARVICLDEPTANIDPAGvpvlrDAAITAA---ERTGAALIVVEHRvDAWVDVVDRIIVLGRGGVIAD 235
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAET-----EAIILENlrrLLKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVED 690
|
250
....*....|.
gi 1081004564 236 GAPHRVLEDYG 246
Cdd:COG2274 691 GTHEELLARKG 701
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
35-243 |
5.68e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 131.76 E-value: 5.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARGaVGLVLQDPD-----S 105
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDS-----GRILLDGRdvtgLPPEKRN-VGMVFQDYAlfphlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 qtisarVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:COG3842 94 ------VAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 186 PAgvpvLRDAaiTAAE------RTGAALIVVEH-RVDAWVdVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:COG3842 168 AK----LREE--MREElrrlqrELGITFIYVTHdQEEALA-LADRIAVMNDGRIEQVGTPEEIYE 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-246 |
7.07e-34 |
|
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: 135.27 E-value: 7.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 10 PSSSGNVPAVSARGFGYRHAGRKAAvLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-- 87
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGGRPA-LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS-----GSILINGVdl 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 ---TPASARGAVGLVLQDPdsQTISARVGDDVAFGAENlgvAPAEignRVRASLDLVGLD-----LP--LDHPT----HR 153
Cdd:COG4988 402 sdlDPASWRRQIAWVPQNP--YLFAGTIRENLRLGRPD---ASDE---ELEAALEAAGLDefvaaLPdgLDTPLgeggRG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 154 LSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAErtGAALIVVEHRvDAWVDVVDRIIVLGRGGVI 233
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIV 550
|
250
....*....|...
gi 1081004564 234 ADGAPHRVLEDYG 246
Cdd:COG4988 551 EQGTHEELLAKNG 563
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
30-245 |
1.42e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.49 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAAVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARGAVGLVLQDPDS 105
Cdd:COG1131 11 GDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS-----GEVRVLGedvaRDPAEVRRRIGYVPQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 -QTISARvgddvafgaENL-------GVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICL 177
Cdd:COG1131 85 yPDLTVR---------ENLrffarlyGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 178 DEPTANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAP----HRVLEDY 245
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPdelkARLLEDV 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
299-499 |
4.88e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.44 E-value: 4.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSG-SAPWKWPSKKlatRIGTVFQD 377
Cdd:PRK13635 13 FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlSEETVWDVRR---QVGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 378 PEHQFVTGTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTF 454
Cdd:PRK13635 90 PDNQFVGATVQDDVAFGLENIGVPREemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081004564 455 GQDRRTFTELLTLLRQLADDGR-TVISITHDpLVVQAMGDYVVDMD 499
Cdd:PRK13635 170 MLDPRGRREVLETVRQLKEQKGiTVLSITHD-LDEAAQADRVIVMN 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-232 |
5.56e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.93 E-value: 5.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEGR-----TPASARG 94
Cdd:COG4619 2 ELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-----DPPTSGEIYLDGKplsamPPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 AVGLVLQDPdsQTISARVGDDVAFGAENLGVAPAEigNRVRASLDLVGLDL-PLDHPTHRLSGGQKQRLALAGVLAMGAR 173
Cdd:COG4619 75 QVAYVPQEP--ALWGGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 174 VICLDEPTANIDPAgvpvLRDAAITA----AERTGAALIVVEHrVDAWVDVV-DRIIVLGRGGV 232
Cdd:COG4619 151 VLLLDEPTSALDPE----NTRRVEELlreyLAEEGRAVLWVSH-DPEQIERVaDRVLTLEAGRL 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
26-233 |
8.58e-33 |
|
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: 124.91 E-value: 8.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA---------V 96
Cdd:cd03255 10 YGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTS-----GEVRVDGTDISKLSEKelaafrrrhI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 GLVLQD----PDsqtISARvgDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGA 172
Cdd:cd03255 85 GFVFQSfnllPD---LTAL--ENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 173 RVICLDEPTANIDPA-GVPVLRdaAITA-AERTGAALIVVEHRVDAwVDVVDRIIVLgRGGVI 233
Cdd:cd03255 160 KIILADEPTGNLDSEtGKEVME--LLRElNKEAGTTIVVVTHDPEL-AEYADRIIEL-RDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
32-248 |
1.09e-32 |
|
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: 125.36 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 32 KAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARGAVGLVLQDPDS-Q 106
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS-----GSILIDGedvrKEPREARRQIGVLPDERGLyD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 TISARvgDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:COG4555 88 RLTVR--ENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 187 AGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDYGQA 248
Cdd:COG4555 166 MARRLLRE-ILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
36-244 |
1.18e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 126.40 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAG--------VLGDDSDGEATGKllieGRTPASARGAVGLVLQDPDSQT 107
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGlhvptqgsVRVDDTLITSTSK----NKDIKQIRKKVGLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPL-DHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:PRK13649 99 FEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 187 AGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13649 179 KGRKELMT-LFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-182 |
1.47e-32 |
|
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: 121.99 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASARGAVGLVLQDPdSQTISA 110
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE-----GTILLDGQdltddERKSLRKEIGYVFQDP-QLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 111 RVGDDVAFGAENLGVAPAEIGNRVRASLDLVGL----DLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-233 |
2.83e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.75 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYRHAGRkaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGddsdgEATGKLLIEGR-TPASAR-GAVGLVLQ 101
Cdd:cd03226 7 FSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKpIKAKERrKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 102 DPDSQTISARVGDDVAFGAENLGVAPAeignRVRASLDLVGL-DLPLDHPtHRLSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:cd03226 79 DVDYQLFTDSVREELLLGLKELDAGNE----QAETVLKDLDLyALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 181 TANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRGGVI 233
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
17-243 |
3.75e-32 |
|
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: 123.55 E-value: 3.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARG----FGYRHagrkaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLLIEGR 87
Cdd:COG1127 4 PMIEVRNltksFGDRV------VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSgeilvDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 TPASARgaVGLVLQDP---DSQTisarVGDDVAFG-AENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLA 163
Cdd:COG1127 78 YELRRR--IGMLFQGGalfDSLT----VFENVAFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 164 LAGVLAMGARVICLDEPTANIDPagvpvlrdaaITAA----------ERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVI 233
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDP----------ITSAvidelirelrDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|
gi 1081004564 234 ADGAPHRVLE 243
Cdd:COG1127 222 AEGTPEELLA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
35-244 |
9.23e-32 |
|
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: 122.55 E-value: 9.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARGAVGLV--LQDP---DS 105
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS-----GSVLFDGEditgLPPHEIARLGIGrtFQIPrlfPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 QT------ISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:cd03219 90 LTvlenvmVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 180 PTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:cd03219 170 PAAGLNPEETEELAE-LIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
26-235 |
1.41e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 121.69 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA---------V 96
Cdd:COG1136 14 YGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTS-----GEVLIDGQDISSLSERelarlrrrhI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 GLVLQD----PdsqTISARvgDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGA 172
Cdd:COG1136 89 GFVFQFfnllP---ELTAL--ENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 173 RVICLDEPTANIDPA-GVPVLrDAAITAAERTGAALIVVEH--RVDAWvdvVDRIIVLGRGGVIAD 235
Cdd:COG1136 164 KLILADEPTGNLDSKtGEEVL-ELLRELNRELGTTIVMVTHdpELAAR---ADRVIRLRDGRIVSD 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
36-244 |
4.17e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 122.15 E-value: 4.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRTPAS----ARGAVGLVLQDPDSQTISAR 111
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPL-DHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP-AGV 189
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPkARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 190 PVLRdaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13643 182 EMMQ--LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
296-498 |
7.54e-31 |
|
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: 119.52 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 296 KSWFRGSETVEpIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsAPWKWPSKKLA----TRI 371
Cdd:cd03255 8 KTYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT--DISKLSEKELAafrrRHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 372 GTVFQDpeHQFVTG-TVLEELQLGPKLVGV---NADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIV 447
Cdd:cd03255 85 GFVFQS--FNLLPDlTALENVELPLLLAGVpkkERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 448 LLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQaMGDYVVDM 498
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAE-YADRIIEL 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
34-243 |
1.18e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.18 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT-----PASARGaVGLVLQDPdsqti 108
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDS-----GRIVLNGRDlftnlPPRERR-VGFVFQHY----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 sA-----RVGDDVAFGAENLGVAPAEIGNRVRASLDLVGldlpLDHPTHR----LSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:COG1118 85 -AlfphmTVAENIAFGLRVRPPSKAEIRARVEELLELVQ----LEGLADRypsqLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 180 PTANIDpAGV-PVLRDAAITAAERTGAALIVVEH-RVDAWvDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:COG1118 160 PFGALD-AKVrKELRRWLRRLHDELGGTTVFVTHdQEEAL-ELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
35-244 |
1.20e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.35 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLL-----------AAIAGVLGDDSDGEATGKL------LIEGRTPASA----- 92
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtGTIEWIFKDEKNKKKTKEKekvlekLVIQKTRFKKikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 --RGAVGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLP-LDHPTHRLSGGQKQRLALAGVLA 169
Cdd:PRK13651 102 eiRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 170 MGARVICLDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
17-251 |
2.57e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 118.62 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAAvLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA- 95
Cdd:COG3638 1 PMLELRNLSKRYPGGTPA-LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTS-----GEILVDGQDVTALRGRa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 -------VGLVLQDP---DSQTisarVGDDVAFGAenLG-----------VAPAEIgNRVRASLDLVGLDLPLDHPTHRL 154
Cdd:COG3638 75 lrrlrrrIGMIFQQFnlvPRLS----VLTNVLAGR--LGrtstwrsllglFPPEDR-ERALEALERVGLADKAYQRADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 155 SGGQKQRLALAGVLAMGARVICLDEPTANIDPA-GVPVLRDAAiTAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVI 233
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLR-RIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
250 260
....*....|....*....|...
gi 1081004564 234 ADGAPHRVLED-----YGQALTD 251
Cdd:COG3638 227 FDGPPAELTDAvlreiYGGEAEE 249
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-230 |
2.67e-30 |
|
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: 116.33 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASAR 93
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTS-----GEILIDGVdlrdlDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GAVGLVLQDPD--SQTIsarvgddvafgAENLgvapaeignrvrasldlvgldlpldhpthrLSGGQKQRLALAGVLAMG 171
Cdd:cd03228 76 KNIAYVPQDPFlfSGTI-----------RENI------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 172 ARVICLDEPTANIDPAGvpvlrDAAITAA---ERTGAALIVVEHRVdAWVDVVDRIIVLGRG 230
Cdd:cd03228 115 PPILILDEATSALDPET-----EALILEAlraLAKGKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
26-236 |
1.02e-29 |
|
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: 116.45 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdGEATGKLLIEGR--TPASA------RGAVG 97
Cdd:cd03257 11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL-----KPTSGSIIFDGKdlLKLSRrlrkirRKEIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 LVLQDPdsqtISA-----RVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPT---HRLSGGQKQRLALAGVLA 169
Cdd:cd03257 86 MVFQDP----MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 170 MGARVICLDEPTANIDpagvPVLRDAAIT----AAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03257 162 LNPKLLIADEPTSALD----VSVQAQILDllkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
35-244 |
1.24e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 118.80 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVL--------------GDDSDGEATGKLLIEGRTP--ASARGAVGL 98
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkskygtiqvgdiyiGDKKNNHELITNPYSKKIKnfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 VLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLP-LDHPTHRLSGGQKQRLALAGVLAMGARVICL 177
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 178 DEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD 266
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
18-242 |
1.32e-29 |
|
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: 117.07 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR------TPAS 91
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSS-----GEVLLDGRdlaslsRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 ARgAVGLVLQDPDSqTISARVGDDVAFG----AENLGVAPAEIGNRVRASLDLVGL-DLpLDHPTHRLSGGQKQRLALAG 166
Cdd:COG1120 74 AR-RIAYVPQEPPA-PFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLeHL-ADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 167 VLAMGARVICLDEPTANIDPAG-VPVLRdaAITA-AERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHqLEVLE--LLRRlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-241 |
1.74e-29 |
|
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: 115.74 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGR-------TPAS 91
Cdd:cd03260 1 IELRDLNVYYGDKHA--LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKdiydldvDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 ARGAVGLVLQDPDsqTISARVGDDVAFGAENLGVAP-AEIGNRVRASLDLVGLDLPLDHPTH--RLSGGQKQRLALAGVL 168
Cdd:cd03260 79 LRRRVGMVFQKPN--PFPGSIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 169 AMGARVICLDEPTANIDPAGVPVLRDAAITAAERTgaALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRV 241
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
30-237 |
2.09e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.53 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgEAT-GKLLIEGRTPASARGA--------VGLVL 100
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE------RPTsGQVLVNGQDLSRLKRReipylrrrIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 101 QD----PDsQTisarVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVIC 176
Cdd:COG2884 86 QDfrllPD-RT----VYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 177 LDEPTANIDPAgvpvlrdaaiTAAE---------RTGAALIVVEHrvDAwvDVVD----RIIVLGRGGVIADGA 237
Cdd:COG2884 161 ADEPTGNLDPE----------TSWEimelleeinRRGTTVLIATH--DL--ELVDrmpkRVLELEDGRLVRDEA 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
283-496 |
2.47e-29 |
|
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: 115.36 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKST-----LALTLGGLLEPMAGTVQVAGSGS 357
Cdd:cd03260 1 IELRDLNVYYGDKH-----------ALKDISLDIPKGEITALIGPSGCGKSTllrllNRLNDLIPGAPDEGEVLLDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 358 APWKWPSKKLATRIGTVFQDPehQFVTGTVLEELQLGPKLVGVNADKRIEELLER-LRLTALT-----KANPFSLSGGEK 431
Cdd:cd03260 70 YDLDVDVLELRRRVGMVFQKP--NPFPGSIYDNVAYGLRLHGIKLKEELDERVEEaLRKAALWdevkdRLHALGLSGGQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 432 RRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDgRTVISITHDPLVVQAMGDYVV 496
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTA 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
311-511 |
2.57e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 116.77 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQV------AGSGSAPWKWPSKKlatrIGTVFQDPEHQFVT 384
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitSTSKNKDIKQIRKK----VGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 385 GTVLEELQLGPKLVGVNADKRIEELLERLRLTALTKA----NPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlfekNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 461 FTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMDAFHPERSGRAAP 511
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
299-508 |
3.24e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.24 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVagSGSAPWKWPSKKLATRIGTVFQDP 378
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI--DGITISKENLKEIRKKIGIIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 EHQFVTGTV-------LEELQLGPKLVgvnaDKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDE 451
Cdd:PRK13632 93 DNQFIGATVeddiafgLENKKVPPKKM----KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 452 PTFGQDRRTFTELLTLLRQLADDG-RTVISITHD-PLVVQAmgDYVVDMDAFHPERSGR 508
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRkKTLISITHDmDEAILA--DKVIVFSEGKLIAQGK 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
35-241 |
3.57e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.25 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEatgkLLIEGR----TPASARGaVGLVLQDP---DSQT 107
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPTSGE----ILIGGRdvtdLPPKDRN-IAMVFQSYalyPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 isarVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:COG3839 92 ----VYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 188 gvpvLRDAAIT--AA--ERTGAALIVVEHrvdawvDVV------DRIIVLgRGGVIAD-GAPHRV 241
Cdd:COG3839 168 ----LRVEMRAeiKRlhRRLGTTTIYVTH------DQVeamtlaDRIAVM-NDGRIQQvGTPEEL 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
36-244 |
3.70e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 116.65 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEG-----RTPASARGAVGLVLQDPDSQTISA 110
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 RVGDDVAFGAENLGVAPAEIGNRVRASLDLVglDLPLDHPTH---RLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLV--QLPEDYVKRspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 188 GVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
312-499 |
4.94e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 4.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPS--KKLATRIGTVFQDPEHQFVTGTVLE 389
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklKPLRKKVGIVFQFPEHQLFEETVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGV---NADKRIEELLERLRLTA--LTKAnPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:PRK13634 106 DICFGPMNFGVseeDAKQKAREMIELVGLPEelLARS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081004564 465 LTLLRQL-ADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:PRK13634 185 MEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMH 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
25-252 |
5.09e-29 |
|
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: 115.29 E-value: 5.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 25 GYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT-----PASARGAVGLV 99
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS-----GEVTFDGRPvtrrrRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 100 LQDPDSqtiSA----RVGDDVAFGAENLGVApaEIGNRVRASLDLVGLD------LPldhptHRLSGGQKQRLALAGVLA 169
Cdd:COG1124 85 FQDPYA---SLhprhTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpsfldrYP-----HQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 170 MGARVICLDEPTANIDpagvpvlrdaAITAAE----------RTGAALIVVEH---RVDAWvdvVDRIIVLGRGGVIADG 236
Cdd:COG1124 155 LEPELLLLDEPTSALD----------VSVQAEilnllkdlreERGLTYLFVSHdlaVVAHL---CDRVAVMQNGRIVEEL 221
|
250 260
....*....|....*....|
gi 1081004564 237 APHRVLE----DYGQALTDA 252
Cdd:COG1124 222 TVADLLAgpkhPYTRELLAA 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
36-272 |
6.92e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.58 E-value: 6.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGddsdgEATGKLLIEGRTPASA-----RGAVGLVLQDPDSQTISA 110
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAEnvwnlRRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 RVGDDVAFGAENLGVAPAEIGNRVRASLDLVG-LDLPLDHPThRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGV 189
Cdd:PRK13642 98 TVEDDVAFGMENQGIPREEMIKRVDEALLAVNmLDFKTREPA-RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 190 PVLRDAAITAAERTGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHRVLEDyGQALTDAGVWIPGAPPALPDARSV 269
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT-SEDMVEIGLDVPFSSNLMKDLRKN 254
|
...
gi 1081004564 270 ACD 272
Cdd:PRK13642 255 GFD 257
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
310-484 |
9.61e-29 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 112.52 E-value: 9.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPWKWPSKKLA---TRIGTVFQDPEHQFVTGT 386
Cdd:TIGR01166 9 KGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG---EPLDYSRKGLLerrQRVGLVFQDPDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VLEELQLGPKLVGVNADK---RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTE 463
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEverRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQ 165
|
170 180
....*....|....*....|.
gi 1081004564 464 LLTLLRQLADDGRTVISITHD 484
Cdd:TIGR01166 166 MLAILRRLRAEGMTVVISTHD 186
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
36-243 |
9.90e-29 |
|
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: 113.97 E-value: 9.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARGaVGLVLQDpdsqtiSA- 110
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDS-----GTILFGGEdatdVPVQERN-VGFVFQH------YAl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 ----RVGDDVAFGaenLGVAP-------AEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:cd03296 86 frhmTVFDNVAFG---LRVKPrserppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 180 PTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-244 |
1.58e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.93 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR--TPASA-------RGAVGLVLQDPDSQ 106
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS-----GTITIAGYhiTPETGnknlkklRKKVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 TISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPL-DHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:PRK13641 98 LFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 186 PAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13641 178 PEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
310-496 |
1.65e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.45 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS--GSAPWKWpskkLATRIGTVFQDPEHQFVTGTV 387
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevNAENEKW----VRSKVGLVFQDPDDQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDeveRRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190
....*....|....*....|....*....|..
gi 1081004564 465 LTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:PRK13647 178 MEILDRLHNQGKTVIVATHDVDLAAEWADQVI 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
312-498 |
1.80e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.54 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPS--KKLATRIGTVFQDPEHQFVTGTVLE 389
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlKKLRKKVSLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVNADKRIEELLERLRLTALTKA----NPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL 465
Cdd:PRK13641 106 DVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDliskSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 466 TLLRQLADDGRTVISITHDplvVQAMGDYVVDM 498
Cdd:PRK13641 186 QLFKDYQKAGHTVILVTHN---MDDVAEYADDV 215
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-243 |
2.79e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 119.20 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG---RT--PASA 92
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTE-----GSVLLDGvdiRQidPADL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAVGLVLQDPdsQTISARVGDDVAFGAenLGVAPAEIGNRVRAS--LDLV-----GLDLPLDHPTHRLSGGQKQRLALA 165
Cdd:TIGR03375 538 RRNIGYVPQDP--RLFYGTLRDNIALGA--PYADDEEILRAAELAgvTEFVrrhpdGLDMQIGERGRSLSGGQRQAVALA 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 166 GVLAMGARVICLDEPTANIDPAGVPVLRDA-AITAAERTgaaLIVVEHRVdAWVDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMDNRSEERFKDRlKRWLAGKT---LVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-484 |
4.05e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.86 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 21 ARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEATgklliegrTPASARgaVGLVL 100
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS-GEVS--------IPKGLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 101 QDP---DSQT---------------------ISARVGDDVAFGAE--NLGVAPAEIG-----NRVRASLDLVGL-DLPLD 148
Cdd:COG0488 68 QEPpldDDLTvldtvldgdaelraleaeleeLEAKLAEPDEDLERlaELQEEFEALGgweaeARAEEILSGLGFpEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 149 HPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDaaiTAAERTGAaLIVVEH-R--VDAwvdVVDRII 225
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEE---FLKNYPGT-VLVVSHdRyfLDR---VATRIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 226 VLGRGGVI------ADGAPHRVLEDYGQALTDAG---------VWI------------------------PGAPPalPDA 266
Cdd:COG0488 221 ELDRGKLTlypgnySAYLEQRAERLEQEAAAYAKqqkkiakeeEFIrrfrakarkakqaqsrikalekleREEPP--RRD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 267 RSVACD-QDGHPSGDIAIETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEP 345
Cdd:COG0488 299 KTVEIRfPPPERLGKKVLELEGLSKSYGDK-----------TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 346 MAGTVQVaGSGsapwkwpskklaTRIGTVFQDPEHQFVTGTVLEEL-QLGPKLvgvnADKRIEELLERLRLT---ALTKA 421
Cdd:COG0488 368 DSGTVKL-GET------------VKIGYFDQHQEELDPDKTVLDELrDGAPGG----TEQEVRGYLGRFLFSgddAFKPV 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 422 NpfSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLadDGrTVISITHD 484
Cdd:COG0488 431 G--VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHD 488
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
312-499 |
4.36e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWpsKKLATRIGTVFQDPEHQFVTGTVLEEL 391
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF--EKLRKHIGIVFQNPDNQFVGSIVKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 392 QLGPKLVGVNADK---RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLL 468
Cdd:PRK13648 106 AFGLENHAVPYDEmhrRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLV 185
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 469 RQL-ADDGRTVISITHDplVVQAM-GDYVVDMD 499
Cdd:PRK13648 186 RKVkSEHNITIISITHD--LSEAMeADHVIVMN 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
312-502 |
4.37e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 113.68 E-value: 4.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG--SGSAPWKWPSKKLATRIGTVFQDPEHQFVTGTVLE 389
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVNADKRIEELLERLRLTALTK----ANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL 465
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAEKIAAEKLEMVGLADefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081004564 466 TLLRQLADDGRTVISITHDPLVVQAMGDYVVDMDAFH 502
Cdd:PRK13643 185 QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGH 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
35-243 |
5.74e-28 |
|
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: 111.56 E-value: 5.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARGaVGLVLQD----Pdsq 106
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS-----GEILLDGKditnLPPHKRP-VNTVFQNyalfP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 tiSARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:cd03300 86 --HLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 187 AGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:cd03300 164 KLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
282-485 |
8.30e-28 |
|
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: 112.06 E-value: 8.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 282 AIETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAgsGSAPWK 361
Cdd:COG1120 1 MLEAENLSVGYGGR-----------PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD--GRDLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 362 WPSKKLATRIGTVFQDPEHQFvTGTVLEELQLG-----PKLVGVNAD--KRIEELLERLRLTALtKANPF-SLSGGEKRR 433
Cdd:COG1120 68 LSRRELARRIAYVPQEPPAPF-GLTVRELVALGryphlGLFGRPSAEdrEAVEEALERTGLEHL-ADRPVdELSGGERQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 434 LSVATMLATAPDIVLLDEPTfgqdrrTF------TELLTLLRQLADD-GRTVISITHDP 485
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPT------SHldlahqLEVLELLRRLARErGRTVVMVLHDL 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
34-244 |
1.03e-27 |
|
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: 111.12 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLliEGRTPASARGAVGLVLQD---PDS 105
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSgsvliDGTDINKL--KGKALRQLRRQIGMIFQQfnlIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 QTisarVGDDVAFGAenLG-----------VAPAEIgNRVRASLDLVGLdlpLDHPTHR---LSGGQKQRLALAGVLAMG 171
Cdd:cd03256 93 LS----VLENVLSGR--LGrrstwrslfglFPKEEK-QRALAALERVGL---LDKAYQRadqLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 172 ARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
293-498 |
1.34e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.52 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 293 GAKKSWFRGSETVePIARGVSVSIPSEASTCIVGHNGSGKS----------TlaltlggllePMAGTVQVAGSgsAPWKW 362
Cdd:COG1136 9 NLTKSYGTGEGEV-TALRGVSLSIEAGEFVAIVGPSGSGKStllnilggldR----------PTSGEVLIDGQ--DISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLA----TRIGTVFQD----PEHqfvtgTVLEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEK 431
Cdd:COG1136 76 SERELArlrrRHIGFVFQFfnllPEL-----TALENVALPLLLAGVSrkeRRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 432 RRLSVATMLATAPDIVLLDEPTfGQ-DRRTFTELLTLLRQLADD-GRTVISITHDPLVVqAMGDYVVDM 498
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPT-GNlDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRL 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
310-499 |
1.72e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.54 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsAPWKWPsKKLATRIGTVFQDPE-HQFVTgtVL 388
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE--DVARDP-AEVRRRIGYVPQEPAlYPDLT--VR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 389 EELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRtft 462
Cdd:COG1131 92 ENLRFFARLYGLPrkeARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDpeaRR--- 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081004564 463 ELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:COG1131 169 ELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIID 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
35-230 |
2.06e-27 |
|
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: 109.65 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARGaVGLVLQD----PDsq 106
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS-----GRIYIGGRdvtdLPPKDRD-IAMVFQNyalyPH-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 tisARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDp 186
Cdd:cd03301 87 ---MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081004564 187 AGVPV-LRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:cd03301 163 AKLRVqMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
24-244 |
2.86e-27 |
|
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: 110.51 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGyrhaGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARGAVGLV 99
Cdd:COG0411 14 FG----GLVA--VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTS-----GRILFDGRditgLPPHRIARLGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 100 -----LQDPDSQT------ISARVGDDVAFGAENLGVAP-----AEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLA 163
Cdd:COG0411 83 rtfqnPRLFPELTvlenvlVAAHARLGRGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 164 LAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
.
gi 1081004564 244 D 244
Cdd:COG0411 243 D 243
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-244 |
3.19e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.25 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASA 92
Cdd:PRK13548 1 AMLEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDS-----GEVRLNGRpladWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAVGLVLqdPDSQTISA--RVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLA- 169
Cdd:PRK13548 74 LARRRAVL--PQHSSLSFpfTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 170 -----MGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHrvdawvDV------VDRIIVLGRGGVIADGAP 238
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLH------DLnlaaryADRIVLLHQGRLVADGTP 225
|
....*.
gi 1081004564 239 HRVLED 244
Cdd:PRK13548 226 AEVLTP 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
323-499 |
3.35e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.87 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 323 CIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPS--------------KKLATRIGTVFQDPEHQFVTGTVL 388
Cdd:PRK13631 56 FIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfKELRRRVSMVFQFPEYQLFKDTIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 389 EELQLGPKLVGVN---ADKRIEELLERLRL-TALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:PRK13631 136 KDIMFGPVALGVKkseAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM 215
|
170 180 190
....*....|....*....|....*....|....*
gi 1081004564 465 LTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:PRK13631 216 MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
17-208 |
4.65e-27 |
|
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: 108.34 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASA 92
Cdd:COG4133 1 MMLEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSA-----GEVLWNGEpirdAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAVGLVLQDP---DSQTisarVGDDVAFGAENLGVAPAEIgnRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLA 169
Cdd:COG4133 74 RRRLAYLGHADglkPELT----VRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 170 MGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALI 208
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
35-244 |
5.71e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 108.93 E-value: 5.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT-------PASARGAVGLVLQD----P 103
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDS-----GTITVDGEDltdskkdINKLRRKVGMVFQQfnlfP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DsqtisARVGDDVAFGAEN-LGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:COG1126 91 H-----LTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 183 NIDP---AGV-PVLRDAAitaaeRTGAALIVVEH-----RvdawvDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:COG1126 166 ALDPelvGEVlDVMRDLA-----KEGMTMVVVTHemgfaR-----EVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
307-499 |
6.36e-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: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVagSGSAPWKWPSKKLATRIGTVFQdpehqfvtgt 386
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI--DGKDIAKLPLEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 vleelqlgpklvgvnadkrieellerlrltaltkanpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLT 466
Cdd:cd00267 81 ---------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 467 LLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:cd00267 122 LLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
306-496 |
8.63e-27 |
|
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: 108.00 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsapwkwPSKKLATRIGTVFQ--DPEHQFv 383
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-------PLEKERKRIGYVPQrrSIDRDF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 TGTVLEELQLG--PKLVGV----NADK-RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQ 456
Cdd:cd03235 84 PISVRDVVLMGlyGHKGLFrrlsKADKaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081004564 457 DRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:cd03235 164 DPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
284-496 |
8.80e-27 |
|
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: 106.75 E-value: 8.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 284 ETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAgsGSAPWKWP 363
Cdd:cd03214 1 EVENLSVGYGGR-----------TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD--GKDLASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 364 SKKLATRIGTVFQdpehqfvtgtVLEELQLGPKlvgvnADKRIEEllerlrltaltkanpfsLSGGEKRRLSVATMLATA 443
Cdd:cd03214 68 PKELARKIAYVPQ----------ALELLGLAHL-----ADRPFNE-----------------LSGGERQRVLLARALAQE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 444 PDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVV 496
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVI 169
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-242 |
1.49e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.72 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYrhaGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgdDSDGeatGKLLIEGR-----TPASARGAVGL 98
Cdd:COG1132 347 FSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY--DPTS---GRILIDGVdirdlTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 VLQDP----DSqtisarVGDDVAFGAENlgvAPAEignRVRASLDLVGLD-----LP--LDHPT----HRLSGGQKQRLA 163
Cdd:COG1132 419 VPQDTflfsGT------IRENIRYGRPD---ATDE---EVEEAAKAAQAHefieaLPdgYDTVVgergVNLSGGQRQRIA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 164 LAGVLAMGARVICLDEPTANIDPAGvpvlrDAAITAA---ERTGAALIVVEHRVDAwVDVVDRIIVLGRGGVIADGaPHR 240
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTET-----EALIQEAlerLMKGRTTIVIAHRLST-IRNADRILVLDDGRIVEQG-THE 559
|
..
gi 1081004564 241 VL 242
Cdd:COG1132 560 EL 561
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
283-484 |
2.67e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.24 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRelDIGYgakkSWFRGSETVepiaRGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPWKW 362
Cdd:PRK13639 2 LETR--DLKY----SYPDGTEAL----KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG---EPIKY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLAT---RIGTVFQDPEHQFVTGTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSV 436
Cdd:PRK13639 69 DKKSLLEvrkTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEeveKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081004564 437 ATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHD 484
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
35-233 |
4.17e-26 |
|
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: 106.07 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTpasargavgLVLQDPDSQTISARVG- 113
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS-----GTIIIDGLK---------LTDDKKNINELRQKVGm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 114 --------------DDVAFGAEN-LGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLD 178
Cdd:cd03262 81 vfqqfnlfphltvlENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 179 EPTANIDPAGV----PVLRDAAitaaeRTGAALIVVEHRVDAWVDVVDRIIVLgRGGVI 233
Cdd:cd03262 161 EPTSALDPELVgevlDVMKDLA-----EEGMTMVVVTHEMGFAREVADRVIFM-DDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
282-500 |
8.11e-26 |
|
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: 106.04 E-value: 8.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 282 AIETRELDIGYGAKKSWFrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgSAPWK 361
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRV-------PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR-PVTRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 362 WPsKKLATRIGTVFQDPE-----HQFVTGTVLEELQLgpkLVGVNADKRIEELLERLRLTA--LTKaNPFSLSGGEKRRL 434
Cdd:COG1124 73 RR-KAFRRRVQMVFQDPYaslhpRHTVDRILAEPLRI---HGLPDREERIAELLEQVGLPPsfLDR-YPHQLSGGQRQRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 435 SVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQL-ADDGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-230 |
8.95e-26 |
|
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: 105.18 E-value: 8.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLliEGRTPASARGAVGLVLQdpDSQTI 108
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSgtirvNGQDVSDL--RGRAIPYLRRKIGVVFQ--DFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SAR-VGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:cd03292 91 PDRnVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 188 G----VPVLRDaaITAAertGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:cd03292 171 TtweiMNLLKK--INKA---GTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
298-500 |
9.08e-26 |
|
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: 105.28 E-value: 9.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 298 WFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKL-ATRIGTVFQ 376
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 377 DP-------------------EHQFVTGTVLEELQLGPKLVGVNADkriEELLERLrltaltkanPFSLSGGEKRRLSVA 437
Cdd:cd03257 90 DPmsslnprmtigeqiaeplrIHGKLSKKEARKEAVLLLLVGVGLP---EEVLNRY---------PHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 438 TMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYA 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
35-236 |
9.96e-26 |
|
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: 104.92 E-value: 9.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGAVGLVLQDPD-SQTISARVG 113
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTS-----GSIRVFGKPLEKERKRIGYVPQRRSiDRDFPISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 114 DDVAFGAEN----LGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGV 189
Cdd:cd03235 89 DVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 190 PVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRgGVIADG 236
Cdd:cd03235 169 EDIYE-LLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
32-244 |
1.14e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.56 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 32 KAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIaGVLGDDSDGEatgkLLIEG---RTPASA----RGAVGLVLQD-- 102
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGD----LIVDGlkvNDPKVDerliRQEAGMVFQQfy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 --PDSQTIsarvgDDVAFGAENL-GVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:PRK09493 88 lfPHLTAL-----ENVMFGPLRVrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 180 PTANIDP----AGVPVLRDAAitaaeRTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK09493 163 PTSALDPelrhEVLKVMQDLA-----EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
35-243 |
1.37e-25 |
|
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: 105.11 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARGaVGLVLQD----PDSQ 106
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS-----GKILLNGKditnLPPEKRD-ISYVPQNyalfPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 tisarVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:cd03299 88 -----VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 187 AGVPVLRDAAITAAERTGAALIVVEHR-VDAWVdVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDfEEAWA-LADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-236 |
1.52e-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: 103.28 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAS------AR 93
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS-----GEILLDGKDLASlspkelAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 gAVGLVLQdpdsqtisarvgddvafgaenlgvapaeignrvraSLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGAR 173
Cdd:cd03214 74 -KIAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 174 VICLDEPTANIDPAG-VPVLrDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03214 118 ILLLDEPTSHLDIAHqIELL-ELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-236 |
1.60e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 104.59 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT-----PASARGAV 96
Cdd:cd03245 6 RNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTS-----GSVLLDGTDirqldPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 GLVLQDPdsQTISARVGDDVAFGaenlgvAPAEIGNRVRASLDLVGL-DLPLDHPT----------HRLSGGQKQRLALA 165
Cdd:cd03245 81 GYVPQDV--TLFYGTLRDNITLG------APLADDERILRAAELAGVtDFVNKHPNgldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 166 GVLAMGARVICLDEPTANIDPAGVPVLRDA-AITAAERTgaaLIVVEHRVdAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERlRQLLGDKT---LIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-230 |
1.72e-25 |
|
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: 102.32 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASARG 94
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS-----GEILIDGKdiaklPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 AVGLVLQdpdsqtisarvgddvafgaenlgvapaeignrvrasldlvgldlpldhpthrLSGGQKQRLALAGVLAMGARV 174
Cdd:cd00267 74 RIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 175 ICLDEPTANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-479 |
2.49e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARG----FGyrhaGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG-----R 87
Cdd:COG1129 3 PLLEMRGisksFG----GVKA--LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS-----GEILLDGepvrfR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 TPASARGA-VGLVLQDP---DSQTIsarvgddvafgAEN--LGVAPAEIG--------NRVRASLDLVGLDLPLDHPTHR 153
Cdd:COG1129 72 SPRDAQAAgIAIIHQELnlvPNLSV-----------AENifLGREPRRGGlidwramrRRARELLARLGLDIDPDTPVGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 154 LSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRGGVI 233
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 234 ADGAPHRVLEDY------GQALTDagvwipgappALPDARsvacdqdgHPSGDIAIETRELdigygakkswfrgseTVEP 307
Cdd:COG1129 220 GTGPVAELTEDElvrlmvGRELED----------LFPKRA--------AAPGEVVLEVEGL---------------SVGG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSI-PSEastcIV---GHNGSGKSTLALTLGGLLEPMAGTVQVAGSgSAPWKWPSKKLATRIGTVfqdPEHQFV 383
Cdd:COG1129 267 VVRDVSFSVrAGE----ILgiaGLVGAGRTELARALFGADPADSGEIRLDGK-PVRIRSPRDAIRAGIAYV---PEDRKG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 TG-------------TVLEELQLGPKLVGVNADKRIEELLERLRL-TALTKANPFSLSGGEKRRLSVATMLATAPDIVLL 449
Cdd:COG1129 339 EGlvldlsirenitlASLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
490 500 510
....*....|....*....|....*....|
gi 1081004564 450 DEPTFGQDRRTFTELLTLLRQLADDGRTVI 479
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVI 448
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
299-499 |
3.81e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMA---GTVQVAGSG-SAPWKWPSKKlatRIGTV 374
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITlTAKTVWDIRE---KVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 375 FQDPEHQFVTGTVLEELQLGPKLVGVNADKRIE---ELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDE 451
Cdd:PRK13640 90 FQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081004564 452 PTFGQDRRTFTELLTLLRQLA-DDGRTVISITHDpLVVQAMGDYVVDMD 499
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKkKNNLTVISITHD-IDEANMADQVLVLD 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
28-244 |
3.85e-25 |
|
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: 103.28 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 28 HAG-RKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdGEATGKLLIEGR----TPASARGAVGLVLQd 102
Cdd:cd03224 7 NAGyGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL-----PPRSGSIRFDGRditgLPPHERARAGIGYV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 PDSQTISAR--VGDDVAFGAENLGvapaeiGNRVRASLDLVgLDL-P-----LDHPTHRLSGGQKQRLALAGVLAMGARV 174
Cdd:cd03224 81 PEGRRIFPEltVEENLLLGAYARR------RAKRKARLERV-YELfPrlkerRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 175 ICLDEPTANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-227 |
4.17e-25 |
|
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: 108.91 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 8 RGPSSSGNVPAVSARGFGYRHAGRKAAvLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGR 87
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAYPGRRPA-LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 TPASARGAVGLVLQDPdsQTISARVGDDVAFGAenLGVAPAEIGNRVRAS--LDLV-----GLDLPLDHPTHRLSGGQKQ 160
Cdd:TIGR02857 390 DADSWRDQIAWVPQHP--FLFAGTIAENIRLAR--PDASDAEIREALERAglDEFVaalpqGLDTPIGEGGAGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 161 RLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAErtGAALIVVEHRvDAWVDVVDRIIVL 227
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
307-500 |
6.77e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 102.20 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGSAPWKWPSkklatRIGTVFQDPehQFV 383
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplSAMPPPEWRR-----QVAYVPQEP--ALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 TGTVLEELQLGPKLVGVNAD-KRIEELLERLRLTALTKANPFS-LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTF 461
Cdd:COG4619 87 GGTVRDNLPFPFQLRERKFDrERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081004564 462 TELLTLLRQL-ADDGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:COG4619 167 RRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
32-230 |
8.23e-25 |
|
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: 101.11 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 32 KAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAS-------ARGAVGLVLQDPd 104
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDS-----GSILIDGEDLTDledelppLRRRIGMVFQDF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 105 sQTISAR-VGDDVAFGaenlgvapaeignrvrasldlvgldlpldhpthrLSGGQKQRLALAGVLAMGARVICLDEPTAN 183
Cdd:cd03229 86 -ALFPHLtVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 184 IDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:cd03229 131 LDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
37-245 |
1.65e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 105.11 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 37 NDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEatgkLLIEGR----TPASARGaVGLVLQD----Pdsqti 108
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-LEDITSGD----LFIGEKrmndVPPAERG-VGMVFQSyalyP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDpAG 188
Cdd:PRK11000 89 HLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD-AA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 189 VPVLRDAAITAA-ERTGAALIVVEH-RVDAwVDVVDRIIVLGRGGVIADGAPhrvLEDY 245
Cdd:PRK11000 168 LRVQMRIEISRLhKRLGRTMIYVTHdQVEA-MTLADKIVVLDAGRVAQVGKP---LELY 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
26-236 |
1.70e-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: 101.89 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA--------VG 97
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTS-----GSVLVDGTDLTLLSGKelrkarrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 LVLQdpDSQTISAR-VGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVIC 176
Cdd:cd03258 86 MIFQ--HFNLLSSRtVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 177 LDEPTANIDPAG----VPVLRDaaitAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03258 164 CDEATSALDPETtqsiLALLRD----INRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
35-241 |
2.01e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.40 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEG----RTPASARgAVGLVLQDpdsqtiSA 110
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQTSGHIRFHGtdvsRLHARDR-KVGFVFQH------YA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 -----RVGDDVAFGaenLGVAP-------AEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLD 178
Cdd:PRK10851 85 lfrhmTVFDNIAFG---LTVLPrrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 179 EPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRV 241
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-185 |
2.02e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.63 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARgfgYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR---TPASARGa 95
Cdd:COG4525 9 VSVR---YPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS-----GEITLDGVpvtGPGADRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 vgLVLQDpDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVI 175
Cdd:COG4525 80 --VVFQK-DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170
....*....|
gi 1081004564 176 CLDEPTANID 185
Cdd:COG4525 157 LMDEPFGALD 166
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
35-484 |
2.06e-24 |
|
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: 106.81 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDG----------EATGKLLIEGR--TPASARGAVgLVLQD 102
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSgriiyhvalcEKCGYVERPSKvgEPCPVCGGT-LEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 PD----SQTISARV---------------GDDVAFgaENLGVAPAEIG-------NRVRASLDLVGLDLPLDHPTHRLSG 156
Cdd:TIGR03269 94 VDfwnlSDKLRRRIrkriaimlqrtfalyGDDTVL--DNVLEALEEIGyegkeavGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 157 GQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 237 APHRVLEDYGQALtdagvwipgapPALPDARSVACdqdghpsGDIAIETRELdigygaKKSWFRGSETVEPIARGVSVSI 316
Cdd:TIGR03269 252 TPDEVVAVFMEGV-----------SEVEKECEVEV-------GEPIIKVRNV------SKRYISVDRGVVKAVDNVSLEV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 317 PSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQV-AGSgsaPWKWPSKK------LATR-IGTVFQDPE---HQFVTG 385
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGD---EWVDMTKPgpdgrgRAKRyIGILHQEYDlypHRTVLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLG-P------------KLVGVNaDKRIEELLERLrltaltkanPFSLSGGEKRRLSVATMLATAPDIVLLDEP 452
Cdd:TIGR03269 385 NLTEAIGLElPdelarmkavitlKMVGFD-EEKAEEILDKY---------PDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
490 500 510
....*....|....*....|....*....|....*
gi 1081004564 453 TFGQD---RRTFTEllTLLRQLADDGRTVISITHD 484
Cdd:TIGR03269 455 TGTMDpitKVDVTH--SILKAREEMEQTFIIVSHD 487
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
35-230 |
2.11e-24 |
|
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: 99.78 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARGAVGLVLQDPD-SQTIS 109
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS-----GEIKVLGkdikKEPEEVKRRIGYLPEEPSlYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARvgddvafgaENLgvapaeignrvrasldlvgldlpldhpthRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGV 189
Cdd:cd03230 90 VR---------ENL-----------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081004564 190 PVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:cd03230 132 REFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-232 |
2.82e-24 |
|
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: 99.60 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDdsdgeATGKLLIEGRT-----PASARG 94
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP-----TSGRVRLDGADisqwdPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 AVGLVLQDPD--SQTIsarvgddvafgAENLgvapaeignrvrasldlvgldlpldhpthrLSGGQKQRLALAGVLAMGA 172
Cdd:cd03246 77 HVGYLPQDDElfSGSI-----------AENI------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 173 RVICLDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRGGV 232
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQ-AIAALKAAGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
280-499 |
3.56e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 280 DIAIETRELDIGYGakkswfRGSETVepiaRGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsaP 359
Cdd:PRK13636 3 DYILKVEELNYNYS------DGTHAL----KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK---P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 360 WKWPSK---KLATRIGTVFQDPEHQFVTGTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRR 433
Cdd:PRK13636 70 IDYSRKglmKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDevrKRVDNALKRTGIEHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 434 LSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
308-498 |
4.01e-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: 100.00 E-value: 4.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPW--KWPSKKLATRIGTVFQD---PEHQf 382
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnsKKASKFRREKLGYLFQNfalIENE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 vtgTVLEELQLGPKLVGVNA---DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:TIGR03608 92 ---TVEENLDLGLKYKKLSKkekREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPK 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 460 TFTELLTLLRQLADDGRTVISITHDPLVVQaMGDYVVDM 498
Cdd:TIGR03608 169 NRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
312-483 |
4.58e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATRIGTVFQDPEHQFVTGTVLEEL 391
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPEYQLFEETIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 392 QLGPKLVGVNAD---KRIEELLERLRLT--ALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLT 466
Cdd:PRK13637 106 AFGPINLGLSEEeieNRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170
....*....|....*...
gi 1081004564 467 LLRQLADD-GRTVISITH 483
Cdd:PRK13637 186 KIKELHKEyNMTIILVSH 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
324-498 |
6.42e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.35 E-value: 6.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAP---WKwpskkLATRIGTVFQDPEHQFVTGTVLEELQLGPKLVGV 400
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvWD-----IRHKIGMVFQNPDNQFVGATVEDDVAFGLENKGI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 401 NAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GR 476
Cdd:PRK13650 113 PHEemkERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQM 192
|
170 180
....*....|....*....|..
gi 1081004564 477 TVISITHDpLVVQAMGDYVVDM 498
Cdd:PRK13650 193 TVISITHD-LDEVALSDRVLVM 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
282-496 |
8.16e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 100.16 E-value: 8.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 282 AIETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKStlaltlggllEPMAGTVQVAGSgsapwk 361
Cdd:COG1121 6 AIELENLTVSYGGR-----------PVLEDVSLTIPPGEFVAIVGPNGAGKStllkailgllPPTSGTVRLFGK------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 362 wPSKKLATRIGTVFQDPE--HQFVTgTVLEELQLG-------PKLVGVNADKRIEELLERLRLTALtkAN-PFS-LSGGE 430
Cdd:COG1121 69 -PPRRARRRIGYVPQRAEvdWDFPI-TVRDVVLMGrygrrglFRRPSRADREAVDEALERVGLEDL--ADrPIGeLSGGQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 431 KRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVL 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
365-484 |
1.18e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.32 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 365 KKLATRIGTVFQDPEHQFVTGTVLEELQLGPKLVGVN---ADKRIEELLERLRL-TALTKANPFSLSGGEKRRLSVATML 440
Cdd:PRK13651 101 KEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSkeeAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1081004564 441 ATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHD 484
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-246 |
1.73e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.84 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYRHagrKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASARGAVGL 98
Cdd:cd03254 10 FSYDE---KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK-----GQILIDGIdirdiSRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 VLQDPD--SQTISarvgDDVAFGAENLGVAPAEIGNRVRASLDLV-----GLDLPLDHPTHRLSGGQKQRLALAGVLAMG 171
Cdd:cd03254 82 VLQDTFlfSGTIM----ENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 172 ARVICLDEPTANIDPAgvpvlRDAAITAAERT---GAALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHRVLEDYG 246
Cdd:cd03254 158 PKILILDEATSNIDTE-----TEKLIQEALEKlmkGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
310-453 |
1.99e-23 |
|
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: 96.18 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVagSGSAPWKWPSKKLATRIGTVFQDPeHQFVTGTVLE 389
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL--DGQDLTDDERKSLRKEIGYVFQDP-QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 390 ELQLGPKLVGV---NADKRIEELLERLRLTALTK----ANPFSLSGGEKRRLSVATMLATAPDIVLLDEPT 453
Cdd:pfam00005 79 NLRLGLLLKGLskrEKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
35-244 |
2.08e-23 |
|
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: 98.90 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLliegRTPASARGAVGLVLQdpdsqtis 109
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSgsirfDGEDITGL----PPHRIARLGIGYVPE-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 arvGDDVaFG----AENL--GVAPAEIGNRVRASLDLVgLDL-P-----LDHPTHRLSGGQKQRLALAGVLAMGARVICL 177
Cdd:COG0410 86 ---GRRI-FPsltvEENLllGAYARRDRAEVRADLERV-YELfPrlkerRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 178 DEPTanidpAGV-PVLRD---AAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:COG0410 161 DEPS-----LGLaPLIVEeifEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
324-498 |
2.12e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.24 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgSAPWKWPSKKLAT---RIGTVFQDPEHQFVTGTVLEELQLGPKLVGV 400
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDI-TITHKTKDKYIRPvrkRIGMVFQFPESQLFEDTVEREIIFGPKNFKM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 401 NADK---RIEELLERLRLTA-LTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLA-DDG 475
Cdd:PRK13646 117 NLDEvknYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDEN 196
|
170 180
....*....|....*....|...
gi 1081004564 476 RTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK13646 197 KTIILVSHDMNEVARYADEVIVM 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
283-496 |
3.24e-23 |
|
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: 98.39 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKW 362
Cdd:COG4555 2 IEVENLSKKYGKV-----------PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--KE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLAtRIGTVFQDPEhqFVTG-TVLEELQ-LGP--KLVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVAT 438
Cdd:COG4555 69 PREARR-QIGVLPDERG--LYDRlTVRENIRyFAElyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 439 MLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVV 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
300-499 |
3.39e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.39 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 300 RGSETVEPIA-RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWK--WpskKLATRIGTVFQ 376
Cdd:PRK13633 16 SNEESTEKLAlDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlW---DIRNKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 377 DPEHQFVTGTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPT 453
Cdd:PRK13633 93 NPDNQIVATIVEEDVAFGPENLGIPPEeirERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081004564 454 FGQDRRTFTELLTLLRQLAD-DGRTVISITH-DPLVVQAmgDYVVDMD 499
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKkYGITIILITHyMEEAVEA--DRIIVMD 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
27-242 |
3.86e-23 |
|
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: 98.14 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 27 RHAGRKAAVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT-----PASARGAVGLVLQ 101
Cdd:cd03295 9 RYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTS-----GEIFIDGEDireqdPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 102 D----PdsqtiSARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLP--LDHPTHRLSGGQKQRLALAGVLAMGARVI 175
Cdd:cd03295 83 QiglfP-----HMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 176 CLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
307-499 |
5.87e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.05 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGSAPWKWPskKLATRIGTVFQDpeHQFV 383
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIP--YLRRRIGVVFQD--FRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 TG-TVLEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:COG2884 92 PDrTVYENVALPLRVTGKSrkeIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081004564 460 TFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:COG2884 172 TSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELE 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
310-499 |
7.08e-23 |
|
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: 96.83 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATRIGTVFQDpEHQFVTGTVLE 389
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGMVFQQ-FNLFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLV-GVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL 465
Cdd:cd03262 96 NITLAPIKVkGMSkaeAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170 180 190
....*....|....*....|....*....|....
gi 1081004564 466 TLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:cd03262 176 DVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
256-500 |
8.78e-23 |
|
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: 102.15 E-value: 8.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 256 IPGAPPALPDArsvacDQDGHPSGDIAIETRELDIGYgakkswfrgSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTL 335
Cdd:COG4987 312 LLDAPPAVTEP-----AEPAPAPGGPSLELEDVSFRY---------PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 336 ALTLGGLLEPMAGTVQVAGSgsAPWKWPSKKLATRIGTVFQDPeHQFvTGTVLEELQLG-PKLvgvnADKRIEELLERLR 414
Cdd:COG4987 378 LALLLRFLDPQSGSITLGGV--DLRDLDEDDLRRRIAVVPQRP-HLF-DTTLRENLRLArPDA----TDEELWAALERVG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 415 LTALTKANP-----------FSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITH 483
Cdd:COG4987 450 LGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITH 528
|
250
....*....|....*..
gi 1081004564 484 DPLVVQAMgDYVVDMDA 500
Cdd:COG4987 529 RLAGLERM-DRILVLED 544
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-496 |
1.11e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.32 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 25 GYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRTpasargavglvLQDPD 104
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGES-----------LLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 105 SQTISARVGDDVA--FGAENLGVAP--------AEI-----GNRVRAS-------LDLVGLDLPL----DHPtHRLSGGQ 158
Cdd:PRK15134 83 EQTLRGVRGNKIAmiFQEPMVSLNPlhtlekqlYEVlslhrGMRREAArgeilncLDRVGIRQAAkrltDYP-HQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 159 KQRLALAGVLAMGARVICLDEPTANIDpagvpVLRDAAITAAERT-----GAALIVVEHRVDAWVDVVDRIIVLGRGGVI 233
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALD-----VSVQAQILQLLRElqqelNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 234 ADGAPHRVL----EDYGQALTDAGvwipgappalPDARSVACDQDGHPsgdiAIETRELDIGYGAKKSWFRGSETVEPIA 309
Cdd:PRK15134 237 EQNRAATLFsaptHPYTQKLLNSE----------PSGDPVPLPEPASP----LLDVEQLQVAFPIRKGILKRTVDHNVVV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLlepMAGTVQVAGSGSAPWKWPSKKL---ATRIGTVFQDPEHQF---- 382
Cdd:PRK15134 303 KNISFTLRPGETLGLVGESGSGKSTTGLALLRL---INSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNSSLnprl 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 -VTGTVLEELQL-GPKLVGVNADKRIEELLERLRLTALTKAN-PFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:PRK15134 380 nVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
|
490 500 510
....*....|....*....|....*....|....*...
gi 1081004564 460 TFTELLTLLRQLADDGR-TVISITHDPLVVQAMGDYVV 496
Cdd:PRK15134 460 VQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVI 497
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-246 |
1.22e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 96.53 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASAR 93
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDS-----GRILIDGHdvrdyTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GAVGLVLQDPdsQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLV-----GLDLPLDHPTHRLSGGQKQRLALAGVL 168
Cdd:cd03251 76 RQIGLVSQDV--FLFNDTVAENIAYGRPGATREEVEEAARAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 169 AMGARVICLDEPTANIDPAGVPVLRDA-AITAAERTGaalIVVEHRVDAwVDVVDRIIVLGRGGVIADGApHRVLEDYG 246
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAAlERLMKNRTT---FVIAHRLST-IENADRIVVLEDGKIVERGT-HEELLAQG 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
283-499 |
1.25e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYgakkswfRGSETVepiARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKW 362
Cdd:PRK13652 4 IETRDLCYSY-------SGSKEA---LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLATRIGTVFQDPEHQFVTGTVLEELQLGPKLVGVNADK---RIEELLERLRLTALTKANPFSLSGGEKRRLSVATM 439
Cdd:PRK13652 72 NIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETvahRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 440 LATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
311-491 |
1.62e-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: 95.94 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLA---TRIGTVFQDpEHQFVTGTV 387
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGRAIPylrRKIGVVFQD-FRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKLVGV---NADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:cd03292 96 YENVAFALEVTGVpprEIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180
....*....|....*....|....*..
gi 1081004564 465 LTLLRQLADDGRTVISITHDPLVVQAM 491
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHAKELVDTT 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
299-500 |
2.01e-22 |
|
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: 96.11 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG------SGSApwkwpSKKLATRIG 372
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllSGKE-----LRKARRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 373 TVFQDpEHQFVTGTVLEELQLGPKLVGV---NADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLL 449
Cdd:cd03258 86 MIFQH-FNLLSSRTVFENVALPLEIAGVpkaEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 450 DEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
26-225 |
2.11e-22 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 95.47 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAG----------VLGDDSDGeATGKLLIEgrtpasARGA 95
Cdd:TIGR02982 11 YGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGlrsvqegslkVLGQELHG-ASKKQLVQ------LRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 VGLVLQDPD-SQTISARvgDDVAFGAE-NLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGAR 173
Cdd:TIGR02982 84 IGYIFQAHNlLGFLTAR--QNVQMALElQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 174 VICLDEPTANIDPA-GVPVLRDAAITAAERTGAALIVV-EHRVdawVDVVDRII 225
Cdd:TIGR02982 162 LVLADEPTAALDSKsGRDVVELMQKLAKEQGCTILMVThDNRI---LDVADRIL 212
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
311-513 |
2.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.70 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSG-SAPWKWpskKLATRIGTVFQDPEHQFVTGTVLE 389
Cdd:PRK13642 25 GVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELlTAENVW---NLRRKIGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLT 466
Cdd:PRK13642 102 DVAFGMENQGIPREemiKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081004564 467 LLRQLADDGR-TVISITHDpLVVQAMGDYVVDMDAfhPERSGRAAPGQ 513
Cdd:PRK13642 182 VIHEIKEKYQlTVLSITHD-LDEAASSDRILVMKA--GEIIKEAAPSE 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
262-500 |
2.94e-22 |
|
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: 100.22 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 262 ALPDARSVACDQDGHPSGDIAIETRELDIGYGAKKswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGG 341
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR----------PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 342 LLEPMAGTVQVAgsGSAPWKWPSKKLATRIGTVFQDPehQFVTGTVLEELQLGpklvGVNA-DKRIEELLERLRLTALTK 420
Cdd:COG4988 386 FLPPYSGSILIN--GVDLSDLDPASWRRQIAWVPQNP--YLFAGTIRENLRLG----RPDAsDEELEAALEAAGLDEFVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 421 ANP-----------FSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITHDPLVVQ 489
Cdd:COG4988 458 ALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLA 536
|
250
....*....|.
gi 1081004564 490 AMgDYVVDMDA 500
Cdd:COG4988 537 QA-DRILVLDD 546
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-186 |
3.12e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 96.26 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDG-EATGKLLIEGR-------T 88
Cdd:COG1117 10 PKIEVRNLNVYYGDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNR-MNDLIPGaRVEGEILLDGEdiydpdvD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 89 PASARGAVGLVLQDPD----SqtisarVGDDVAFGAENLGVAP-AEIGNRVRASLDLVGL-----DlPLDHPTHRLSGGQ 158
Cdd:COG1117 87 VVELRRRVGMVFQKPNpfpkS------IYDNVAYGLRLHGIKSkSELDEIVEESLRKAALwdevkD-RLKKSALGLSGGQ 159
|
170 180
....*....|....*....|....*...
gi 1081004564 159 KQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
34-244 |
3.33e-22 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 95.83 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA--------VGLVLQD--- 102
Cdd:TIGR02315 16 QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSS-----GSILLEGTDITKLRGKklrklrrrIGMIFQHynl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 PDSQTI-----SARVGDDvAFGAENLGVAPAEIGNRVRASLDLVGLdlpLDHPTHR---LSGGQKQRLALAGVLAMGARV 174
Cdd:TIGR02315 91 IERLTVlenvlHGRLGYK-PTWRSLLGRFSEEDKERALSALERVGL---ADKAYQRadqLSGGQQQRVAIARALAQQPDL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 175 ICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:TIGR02315 167 ILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
39-242 |
3.99e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.21 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 39 ITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARGaVGLVLQDP---DSQTISAR 111
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDS-----GRILWNGQdltaLPPAERP-VSMLFQENnlfPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGddvafgaenLGVAP-----AEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:COG3840 92 IG---------LGLRPglkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 187 AgvpvLRDAAIT----AAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:COG3840 163 A----LRQEMLDlvdeLCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
283-484 |
4.03e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.85 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAgsGSAPWKW 362
Cdd:PRK11231 3 LRTENLTVGYGTKR-----------ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG--DKPISML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLATRIGTVfqdPEHQFVTG--TVLEELQLG--PKL-----VGVNADKRIEELLERLRLTALTKANPFSLSGGEKRR 433
Cdd:PRK11231 70 SSRQLARRLALL---PQHHLTPEgiTVRELVAYGrsPWLslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 434 LSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHD 484
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
307-498 |
4.08e-22 |
|
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: 94.51 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGSAPWKwpskklaTRIGTVFQDP---EH 380
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPER-------RNIGMVFQDYalfPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 381 QfvtgTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPtFGQ- 456
Cdd:cd03259 87 L----TVAENIAFGLKLRGVPKAeirARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP-LSAl 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081004564 457 DRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:cd03259 162 DAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVM 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
35-236 |
4.43e-22 |
|
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: 94.27 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT-PASARGAVGLVLQD----PDSqtis 109
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS-----GEVLFDGKPlDIAARNRIGYLPEErglyPKM---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 aRVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGV 189
Cdd:cd03269 86 -KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 190 PVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03269 165 ELLKD-VIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
35-235 |
5.09e-22 |
|
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: 92.88 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR--TPASARGAvglvlqdpdsqtisarv 112
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS-----GEILVDGKevSFASPRDA----------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 113 gddvafgaENLGVApaeignrvrasldLVgldlpldhptHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVL 192
Cdd:cd03216 73 --------RRAGIA-------------MV----------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081004564 193 RDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIAD 235
Cdd:cd03216 122 FK-VIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
32-238 |
5.79e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 32 KAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLLIEGRTpasargaVGLVLQD---- 102
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEgqifiDGEDVTHRSIQQRD-------ICMVFQSyalf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 PdsqtiSARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:PRK11432 91 P-----HMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 183 NIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAP 238
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
310-500 |
6.31e-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: 93.02 E-value: 6.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATRIGTVFQDPEhQFVTGTVLE 389
Cdd:cd03229 17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGMVFQDFA-LFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGpklvgvnadkrieellerlrltaltkanpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLR 469
Cdd:cd03229 96 NIALG-------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
170 180 190
....*....|....*....|....*....|..
gi 1081004564 470 QLAD-DGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:cd03229 145 SLQAqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
310-499 |
6.51e-22 |
|
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: 94.43 E-value: 6.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGsapwkWPSKKLATR-IGTVFQDPEhQFVTG 385
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGediTG-----LPPHEIARLgIGRTFQIPR-LFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPKLVGVN-------------ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEP 452
Cdd:cd03219 91 TVLENVMVAAQARTGSglllararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 453 TFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:cd03219 171 AAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLD 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
283-505 |
6.54e-22 |
|
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: 94.08 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKKSWFrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPWKW 362
Cdd:cd03293 1 LEVRNVSKTYGGGGGAV-------TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---EPVTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKklatRIGTVFQDPeHQFVTGTVLEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATM 439
Cdd:cd03293 71 PGP----DRGYVFQQD-ALLPWLTVLDNVALGLELQGVPkaeARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 440 LATAPDIVLLDEPtFG----QDRRTFTELltLLRQLADDGRTVISITHDplVVQA--MGDYVVDMDAfHPER 505
Cdd:cd03293 146 LAVDPDVLLLDEP-FSaldaLTREQLQEE--LLDIWRETGKTVLLVTHD--IDEAvfLADRVVVLSA-RPGR 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
35-244 |
7.45e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.33 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT----PASARgAVGLVLQD----Pdsq 106
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDS-----GRIMLDGQDithvPAENR-HVNTVFQSyalfP--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 tiSARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:PRK09452 100 --HMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 187 AgvpvLRDA---AITAAERT-GAALIVVEHRVDAWVDVVDRIIVLgRGGVIA-DGAPHRVLED 244
Cdd:PRK09452 178 K----LRKQmqnELKALQRKlGITFVFVTHDQEEALTMSDRIVVM-RDGRIEqDGTPREIYEE 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-238 |
7.83e-22 |
|
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: 94.10 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgEAT-GKLLIEGRTPAS---- 91
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV------ELSsGSILIDGVDISKiglh 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 -ARGAVGLVLQDPdsqtisarvgddVAFGA---ENL---GVAPAEignRVRASLDLV-----------GLDLPLDHPTHR 153
Cdd:cd03244 75 dLRSRISIIPQDP------------VLFSGtirSNLdpfGEYSDE---ELWQALERVglkefveslpgGLDTVVEEGGEN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 154 LSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGvpvlrDAAITAAERT---GAALIVVEHRVDAWVDvVDRIIVLGRG 230
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPET-----DALIQKTIREafkDCTVLTIAHRLDTIID-SDRILVLDKG 213
|
....*...
gi 1081004564 231 GVIADGAP 238
Cdd:cd03244 214 RVVEFDSP 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-236 |
7.89e-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: 92.76 E-value: 7.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASA----RGAVGLV 99
Cdd:cd03247 8 FSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQ-----GEITLDGVPVSDLekalSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 100 LQDPD--SQTISarvgddvafgaENLGVapaeignrvrasldlvgldlpldhpthRLSGGQKQRLALAGVLAMGARVICL 177
Cdd:cd03247 81 NQRPYlfDTTLR-----------NNLGR---------------------------RFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 178 DEPTANIDP-AGVPVLRDAAITAAERTgaaLIVVEHRVDAwVDVVDRIIVLGRGGVIADG 236
Cdd:cd03247 123 DEPTVGLDPiTERQLLSLIFEVLKDKT---LIWITHHLTG-IEHMDKILFLENGKIIMQG 178
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-238 |
7.98e-22 |
|
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: 94.11 E-value: 7.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEATgkllIEG----RTPASARG 94
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS-GTAY----INGysirTDRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 AVGLVLQDpdsqtisarvgdDVAF----GAENL-------GVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLA 163
Cdd:cd03263 76 SLGYCPQF------------DALFdeltVREHLrfyarlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 164 LAGVLAMGARVICLDEPTANIDPAGvpvlRDA--AITAAERTGAALIVVEHRVDAwVDVV-DRIIVLGRGGVIADGAP 238
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPAS----RRAiwDLILEVRKGRSIILTTHSMDE-AEALcDRIAIMSDGKLRCIGSP 216
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
35-237 |
8.00e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 94.13 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLliegRTPASARGAVGLVlqdPDSQTIS 109
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSgsirlDGEDITKL----PPHERARAGIAYV---PQGREIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 AR--VGDDVAFGAENLGVAPAEIGNRVrasLDLvgldLP-LDHPTHR----LSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:TIGR03410 88 PRltVEENLLTGLAALPRRSRKIPDEI---YEL----FPvLKEMLGRrggdLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 183 NIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGA 237
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-243 |
8.70e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 99.05 E-value: 8.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgeatgklliegrtpASARGAV-- 96
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW-------------------PPTAGSVrl 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 -GLVLQDPDSQTISARVG---DDVAF--G--AEN---LGVAPAEignRVRASLDLVG-----LDLPLDHPT------HRL 154
Cdd:COG4618 392 dGADLSQWDREELGRHIGylpQDVELfdGtiAENiarFGDADPE---KVVAAAKLAGvhemiLRLPDGYDTrigeggARL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 155 SGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRdAAITAAERTGAALIVVEHRVdAWVDVVDRIIVLGRGGVIA 234
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA-AAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQA 546
|
....*....
gi 1081004564 235 DGAPHRVLE 243
Cdd:COG4618 547 FGPRDEVLA 555
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-236 |
9.10e-22 |
|
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: 93.59 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARGAVGLVlq 101
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA-----GFATVDGfdvvKEPAEARRRLGFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 102 dPDSQTISAR--VGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:cd03266 84 -SDSTGLYDRltARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 180 PTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03266 163 PTTGLDVMATRALRE-FIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
318-512 |
1.52e-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: 93.13 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 318 SEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsaPWKWPSKKLAT-----RIGTVFQdpEHQ-FVTGTVLEEL 391
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---VLFDSRKKINLppqqrKIGLVFQ--QYAlFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 392 QLGPKLVGVNADK-RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQ 470
Cdd:cd03297 97 AFGLKRKRNREDRiSVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081004564 471 LADD-GRTVISITHDPLVVQAMGDYVVDMdafhpeRSGRAAPG 512
Cdd:cd03297 177 IKKNlNIPVIFVTHDLSEAEYLADRIVVM------EDGRLQYI 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
307-499 |
1.60e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPwkwPSKKLATR--IGTVFQDPEHQFVT 384
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGD---FSKLQGIRklVGIVFQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 385 GTVLEELQLGPK---LVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTF 461
Cdd:PRK13644 93 RTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081004564 462 TELLTLLRQLADDGRTVISITHDPLVVQAmGDYVVDMD 499
Cdd:PRK13644 173 IAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMD 209
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
307-500 |
1.73e-21 |
|
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: 92.70 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWkwPSKKLAT---RIGTVFQDpeHQFV 383
Cdd:TIGR02673 16 AALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRL--RGRQLPLlrrRIGVVFQD--FRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 -TGTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:TIGR02673 92 pDRTVYENVALPLEVRGKKEReiqRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081004564 460 TFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:TIGR02673 172 LSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-243 |
3.19e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.67 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 3 DEALTRGPSSSGNV--PAVSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATG 80
Cdd:PRK11607 2 NDAIPRPQAKTRKAltPLLEIRNLTKSFDGQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 81 KLLIEG----RTPASARgAVGLVLQdpdSQTI--SARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRL 154
Cdd:PRK11607 75 QIMLDGvdlsHVPPYQR-PINMMFQ---SYALfpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 155 SGGQKQRLALAGVLAMGARVICLDEPTANIDPAgvpvLRD----AAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKK----LRDrmqlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
250
....*....|...
gi 1081004564 231 GVIADGAPHRVLE 243
Cdd:PRK11607 227 KFVQIGEPEEIYE 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-213 |
3.21e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 97.05 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 16 VPAVSARGFGYRHAGrKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgDDSDGEatgkLLIEGRTPASARG- 94
Cdd:TIGR02868 332 KPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL-DPLQGE----VTLDGVPVSSLDQd 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 ----AVGLVLQDPdsQTISARVGDDVAFGAENlgVAPAEI---------GNRVRASLDlvGLDLPLDHPTHRLSGGQKQR 161
Cdd:TIGR02868 406 evrrRVSVCAQDA--HLFDTTVRENLRLARPD--ATDEELwaalervglADWLRALPD--GLDTVLGEGGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 162 LALAGVLAMGARVICLDEPTANIDP-AGVPVLRDAAITAAERTgaaLIVVEHR 213
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAeTADELLEDLLAALSGRT---VVLITHH 529
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
51-244 |
3.41e-21 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 94.48 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 51 LLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARGaVGLVLQD----PdsqtiSARVGDDVAFGAEN 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS-----GSIMLDGedvtNVPPHLRH-INMVFQSyalfP-----HMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 123 LGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAgvpvLRDAA----IT 198
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKK----LRDQMqlelKT 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081004564 199 AAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
26-263 |
3.48e-21 |
|
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: 94.35 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgdDSDGEATGKLLIEGR--TPASA------RGA-V 96
Cdd:COG0444 11 FPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLL--PPPGITSGEILFDGEdlLKLSEkelrkiRGReI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 GLVLQDPdsqtISA-----RVGDDVAFGAENLGVAP-AEIGNRVRASLDLVGLDLPLDH----PtHRLSGGQKQRLALAG 166
Cdd:COG0444 89 QMIFQDP----MTSlnpvmTVGDQIAEPLRIHGGLSkAEARERAIELLERVGLPDPERRldryP-HELSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 167 VLAMGARVICLDEPTANIDpagVPV-------LRDaaitAAERTGAALI-------VVEHrvdawvdVVDRIIVLGRGGV 232
Cdd:COG0444 164 ALALEPKLLIADEPTTALD---VTIqaqilnlLKD----LQRELGLAILfithdlgVVAE-------IADRVAVMYAGRI 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1081004564 233 IADGAPHRVLED----YGQALTDA-----GVW-----IPGAPPAL 263
Cdd:COG0444 230 VEEGPVEELFENprhpYTRALLSSiprldPDGrrlipIPGEPPSL 274
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
36-239 |
3.77e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.15 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLL-----IEGRTPA---SARGAVGLVLQDPDSQT 107
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLgrtvqREGRLARdirKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 iSARVGDDVAFGAenLGVAP----------AEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICL 177
Cdd:PRK09984 100 -RLSVLENVLIGA--LGSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 178 DEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPH 239
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
310-484 |
4.58e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.85 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKS---------TlaltlggllEPMAGTVQVAGSgsapwkwPSKKLATRIGTVFQDP-- 378
Cdd:COG1116 28 DDVSLTVAAGEFVALVGPSGCGKStllrliaglE---------KPTSGEVLVDGK-------PVTGPGPDRGVVFQEPal 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 -EHQfvtgTVLEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPtF 454
Cdd:COG1116 92 lPWL----TVLDNVALGLELRGVPkaeRRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP-F 166
|
170 180 190
....*....|....*....|....*....|..
gi 1081004564 455 GQ-DRRTFTELLTLLRQL-ADDGRTVISITHD 484
Cdd:COG1116 167 GAlDALTRERLQDELLRLwQETGKTVLFVTHD 198
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
313-498 |
5.11e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 313 SVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsapWKWPS--------KKLATRIGTVFQDPEHQFVT 384
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGD-----YAIPAnlkkikevKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 385 GTVLEELQLGPKLVGVNAD---KRIEELLERLRLTA-LTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQeayKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 461 FTELLTLLRQL-ADDGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK13645 186 EEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-246 |
5.73e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 91.91 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYrHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgdDSDGeatGKLLIEGR-----TPASARGAVGL 98
Cdd:cd03253 8 FAY-DPGRP--VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY--DVSS---GSILIDGQdirevTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 VLQDpdSQTISARVGDDVAFGaeNLGVAPAEIGNRVR-ASLDLVGLDLPLDHPTH------RLSGGQKQRLALAGVLAMG 171
Cdd:cd03253 80 VPQD--TVLFNDTIGYNIRYG--RPDATDEEVIEAAKaAQIHDKIMRFPDGYDTIvgerglKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 172 ARVICLDEPTANIDpagvpVLRDAAITAAER---TGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHRVLEDYG 246
Cdd:cd03253 156 PPILLLDEATSALD-----THTEREIQAALRdvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
307-490 |
6.88e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS---------GSAPWKWPskklATRIGTVfqd 377
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarvayvpqrSEVPDSLP----LTVRDLV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 378 pehqfVTGTVLEELQLGPklVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD 457
Cdd:NF040873 79 -----AMGRWARRGLWRR--LTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 458 RRTFTELLTLLRQLADDGRTVISITHDPLVVQA 490
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVRR 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
38-236 |
6.96e-21 |
|
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: 91.02 E-value: 6.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 38 DITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR----TPASARgAVGLVLQDPD---SQTISA 110
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS-----GRVLINGVdvtaAPPADR-PVSMLFQENNlfaHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 RVGddvafgaenLGVAP-----AEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:cd03298 90 NVG---------LGLSPglkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 186 PAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-240 |
6.99e-21 |
|
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: 91.73 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 12 SSGNVPAVSARGFGYRHAGRKAAV--LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLLI 84
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSgtvrlAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 85 EGRtpASARGA-VGLVLQD----PdsqTISARvgDDVAFGAENLGVAPAEigNRVRASLDLVGLDLPLDHPTHRLSGGQK 159
Cdd:COG4181 82 DAR--ARLRARhVGFVFQSfqllP---TLTAL--ENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 160 QRLALAGVLAMGARVICLDEPTANIDPA-GVPVLrDAAITAAERTGAALIVVEHrvdawvDVV-----DRIIVLGRGGVI 233
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAAtGEQII-DLLFELNRERGTTLVLVTH------DPAlaarcDRVLRLRAGRLV 225
|
....*..
gi 1081004564 234 ADGAPHR 240
Cdd:COG4181 226 EDTAATA 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
283-496 |
9.26e-21 |
|
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: 89.38 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsaPWKW 362
Cdd:cd03230 1 IEVRNLSKRYGKK-----------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---DIKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLATRIGTVFQDPehqfvtgTVLEELqlgpklvgvnadkRIEELLErlrltaltkanpfsLSGGEKRRLSVATMLAT 442
Cdd:cd03230 67 EPEEVKRRIGYLPEEP-------SLYENL-------------TVRENLK--------------LSGGMKQRLALAQALLH 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 443 APDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVA 166
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-251 |
1.05e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.44 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRT-------PASARGAVGLVLQDPDS-- 105
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNiyspdvdPIEVRREVGMVFQYPNPfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 -QTISarvgDDVAFGAE--NLGVAPAEIGNRVRASLDLVGL-----DLPLDHPTHrLSGGQKQRLALAGVLAMGARVICL 177
Cdd:PRK14267 99 hLTIY----DNVAIGVKlnGLVKSKKELDERVEWALKKAALwdevkDRLNDYPSN-LSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 178 DEPTANIDPAGVPVLRDAAITAaeRTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDYGQALTD 251
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-244 |
1.22e-20 |
|
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: 90.68 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARG 94
Cdd:cd03218 1 LRAENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS-----GKILLDGqditKLPMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 AVGLV-LQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGAR 173
Cdd:cd03218 74 RLGIGyLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 174 VICLDEPTANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-185 |
1.54e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.49 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRKAAVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgEAT-GKLLIEGRTPASARGA----- 95
Cdd:COG4608 21 GGLFGRTVGVVKAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE------EPTsGEILFDGQDITGLSGRelrpl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 ---VGLVLQDPDS-----QTisarVGDDVAFGAENLGVAP-AEIGNRVRASLDLVGLDlPlDH----PtHRLSGGQKQRL 162
Cdd:COG4608 94 rrrMQMVFQDPYAslnprMT----VGDIIAEPLRIHGLASkAERRERVAELLELVGLR-P-EHadryP-HEFSGGQRQRI 166
|
170 180
....*....|....*....|...
gi 1081004564 163 ALAGVLAMGARVICLDEPTANID 185
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALD 189
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-242 |
3.61e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 94.01 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASAR 93
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS-----GQILLDGHdladyTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GAVGLVLQD----PDSqtisarVGDDVAFGAENlGVAPAEIGNRVRAS--LDLV-----GLDLPLDHPTHRLSGGQKQRL 162
Cdd:TIGR02203 406 RQVALVSQDvvlfNDT------IANNIAYGRTE-QADRAEIERALAAAyaQDFVdklplGLDTPIGENGVLLSGGQRQRL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 163 ALAGVLAMGARVICLDEPTANIDPAGvpvlrDAAITAA------ERTGaalIVVEHRVDAwVDVVDRIIVLGRGGVIADG 236
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNES-----ERLVQAAlerlmqGRTT---LVIAHRLST-IEKADRIVVMDDGRIVERG 549
|
....*.
gi 1081004564 237 aPHRVL 242
Cdd:TIGR02203 550 -THNEL 554
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-498 |
3.70e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.15 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 13 SGNVPAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRTPA-- 90
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 91 -----------SARGA-VGLVLQDP-DSQTISARVGDDVAFGAE-NLGVAPAEIGNRVRASLDLVGL---DLPLDHPTHR 153
Cdd:PRK10261 89 elseqsaaqmrHVRGAdMAMIFQEPmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 154 LSGGQKQRLALAGVLAMGARVICLDEPTANIDPA-GVPVLRDAAITAAERTgAALIVVEHRVDAWVDVVDRIIVLGRGGV 232
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiQAQILQLIKVLQKEMS-MGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 233 IADGAP----HRVLEDYGQALTDA--------GVWIPGAPPAL----PDARSVACDQDGHPSGDIAIETRELDIGYGAKK 296
Cdd:PRK10261 248 VETGSVeqifHAPQHPYTRALLAAvpqlgamkGLDYPRRFPLIslehPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 297 SWF-RGSETVEPIARgVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwPSKKLATR--IGT 373
Cdd:PRK10261 328 GLLnRVTREVHAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS-PGKLQALRrdIQF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 374 VFQDP-----EHQFVTGTVLEELQLGPKLVGVNADKRIEELLERLRLTALTKAN-PFSLSGGEKRRLSVATMLATAPDIV 447
Cdd:PRK10261 406 IFQDPyasldPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVI 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 448 LLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVM 537
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
310-498 |
4.03e-20 |
|
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: 89.10 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPwkwPSKKLATRIGTVFQDpEHQFVTGTVLE 389
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT---DRKAARQSLGYCPQF-DALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVNADKRIEELLERLRLTALT-KANPFS--LSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTFTE 463
Cdd:cd03263 95 HLRFYARLKGLPKSEIKEEVELLLRVLGLTdKANKRArtLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDpasRRAIWD 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1081004564 464 LLTLLRQladdGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:cd03263 175 LILEVRK----GRSIILTTHSMDEAEALCDRIAIM 205
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-247 |
4.25e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 93.63 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 10 PSSSGNVpAVSARGFGYRHAGRkaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTP 89
Cdd:PRK10790 335 PLQSGRI-DIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE-----GEIRLDGRPL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 90 AS-----ARGAVGLVLQDP----DSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDlvGLDLPLDHPTHRLSGGQKQ 160
Cdd:PRK10790 406 SSlshsvLRQGVAMVQQDPvvlaDTFLANVTLGRDISEEQVWQALETVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 161 RLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTgaALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHR 240
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQ 560
|
....*..
gi 1081004564 241 VLEDYGQ 247
Cdd:PRK10790 561 LLAAQGR 567
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
306-501 |
4.61e-20 |
|
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: 88.30 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPWKWPSKKLATRIGTVFQDPEhqFVTG 385
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG---EPIRDAREDYRRRLAYLGHADG--LKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 -TVLEELQLGPKLVGVNADK-RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTE 463
Cdd:COG4133 90 lTVRENLRFWAALYGLRADReAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081004564 464 LLTLLRQLADDGRTVISITHDPLVVQAmgDYVVDMDAF 501
Cdd:COG4133 170 LAELIAAHLARGGAVLLTTHQPLELAA--ARVLDLGDF 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-270 |
5.15e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRKAA-----VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLLIEGR 87
Cdd:PRK10419 5 NVSGLSHHYAHGGLSGKhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQgnvswRGEPLAKLNRAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 tpASARGAVGLVLQDPdsqtISA-----RVGDDVAFGAENL-GVAPAEIGNRVRASLDLVGLDLP-LDHPTHRLSGGQKQ 160
Cdd:PRK10419 85 --KAFRRDIQMVFQDS----ISAvnprkTVREIIREPLRHLlSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 161 RLALAGVLAMGARVICLDEPTANIDpagvPVLRDAAITA----AERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIAD- 235
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLD----LVLQAGVIRLlkklQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETq 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 1081004564 236 --GAPHRVLEDYGQALTDAGVwipgapPALPDARSVA 270
Cdd:PRK10419 235 pvGDKLTFSSPAGRVLQNAVL------PAFPVRRRTT 265
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-242 |
5.80e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 40 TLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARgAVGLVLQDPD---SQTISARV 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS-----GSLTLNGqdhtTTPPSRR-PVSMLFQENNlfsHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 113 GddvafgaenLGVAP-----AEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:PRK10771 93 G---------LGLNPglklnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 188 gvpvLRDAAIT-----AAERtGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:PRK10771 164 ----LRQEMLTlvsqvCQER-QLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
259-485 |
5.82e-20 |
|
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: 93.19 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 259 APPALPDARSVACDQDGHPSGDIAIETRELDIGYgakkswfrgsETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALT 338
Cdd:TIGR02868 311 LDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGY----------PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 339 LGGLLEPMAGTVQVagSGSAPWKWPSKKLATRIGTVFQDPeHQFVTgTVLEELQLGPKLVgvnADKRIEELLERLRLTAL 418
Cdd:TIGR02868 381 LAGLLDPLQGEVTL--DGVPVSSLDQDEVRRRVSVCAQDA-HLFDT-TVRENLRLARPDA---TDEELWAALERVGLADW 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 419 TKANP-----------FSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQlADDGRTVISITHDP 485
Cdd:TIGR02868 454 LRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-236 |
6.86e-20 |
|
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: 88.02 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 31 RKAAVLNDITLDIERGEKVLLlGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARGAVGLVLQDPD-S 105
Cdd:cd03264 11 GKKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSS-----GTIRIDGqdvlKQPQKLRRRIGYLPQEFGvY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 QTISARvgDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:cd03264 85 PNFTVR--EFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 186 PAGVPVLRD-AAITAAERTgaaLIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03264 163 PEERIRFRNlLSELGEDRI---VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
289-485 |
1.08e-19 |
|
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: 87.22 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 289 DIGYGAKKSWFRGSETvepIARGVSVSIPSEASTCIVGHNGSGKST--LALTLGGLLEPMAGTVQVAGSGSAPWKWPSkk 366
Cdd:cd03213 8 NLTVTVKSSPSKSGKQ---LLKNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINGRPLDKRSFRK-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 367 latRIGTVFQDpEHQFVTGTVLEELQLGPKLVGvnadkrieellerlrltaltkanpfsLSGGEKRRLSVATMLATAPDI 446
Cdd:cd03213 83 ---IIGYVPQD-DILHPTLTVRETLMFAAKLRG--------------------------LSGGERKRVSIALELVSNPSL 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 447 VLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDP 485
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQP 171
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
36-244 |
1.14e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.45 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRTP----ASARGAVGLVLQDPDSQTISAR 111
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGDDVAFGAENLGVAPAEIGNRvrASLDLVGLDLPLD---HPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAG 188
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNY--AHRLLMDLGFSRDvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 189 VPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK13646 181 KRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
310-499 |
1.29e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 88.13 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPWKWPSKKLA---TRIGTVFQD----PeHQf 382
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDG---EDLTDSKKDINklrRKVGMVFQQfnlfP-HL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 vtgTVLEELQLGPKLV-GVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDR 458
Cdd:COG1126 93 ---TVLENVTLAPIKVkKMSkaeAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 459 RTFTELLTLLRQLADDGRTVISITHDplvvqaMG------DYVVDMD 499
Cdd:COG1126 170 ELVGEVLDVMRDLAKEGMTMVVVTHE------MGfarevaDRVVFMD 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
283-495 |
1.40e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEpMAGTVQVAGS----GSA 358
Cdd:PRK14247 4 IEIRDLKVSFGQVE-----------VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIE-LYPEARVSGEvyldGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 359 PWKWPSKKLATRIGTVFQDPeHQFVTGTVLEELQLGPKLVGVNADKRieELLERLRlTALTKANPF------------SL 426
Cdd:PRK14247 72 IFKMDVIELRRRVQMVFQIP-NPIPNLSIFENVALGLKLNRLVKSKK--ELQERVR-WALEKAQLWdevkdrldapagKL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 427 SGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDgRTVISITHDPLVVQAMGDYV 495
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYV 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
280-498 |
2.40e-19 |
|
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: 91.19 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 280 DIAIETRELDIGYGAKkswfrgsetvEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsAP 359
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGR----------RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV--PL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 360 WKWPSKKLATRIGTVFQDPehQFVTGTVLEELQLGPKlvgVNADKRIEELLERLRLTALTKANPFS-----------LSG 428
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHP--FLFAGTIAENIRLARP---DASDAEIREALERAGLDEFVAALPQGldtpigeggagLSG 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 429 GEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITHDPLVVQAMgDYVVDM 498
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
36-229 |
2.99e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.38 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgdDSDGEATGKLLIEGRT----PASARGaVGLVLQDP---DSQTi 108
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTL--SPAFSASGEVLLNGRRltalPAEQRR-IGILFQDDllfPHLS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 sarVGDDVAFGAenlgvaPAEIG-----NRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTAN 183
Cdd:COG4136 93 ---VGENLAFAL------PPTIGraqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081004564 184 IDPAGVPVLRDAAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGR 229
Cdd:COG4136 164 LDAALRAQFREFVFEQIRQRGIPALLVTHDEED-APAAGRVLDLGN 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-316 |
3.10e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.98 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR--TPAS------ARGAVG 97
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTS-----GSVLVDGVdlTALSerelraARRKIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 LVLQDP---DSQTisarVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDlplDH----PtHRLSGGQKQRLALAGVLAM 170
Cdd:COG1135 86 MIFQHFnllSSRT----VAENVALPLEIAGVPKAEIRKRVAELLELVGLS---DKadayP-SQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 171 GARVICLDEPTANIDPAG----VPVLRDaaitAAERTGAALIVVEHRvdawVDVV----DRIIVLGRGGVIADGAPHRVL 242
Cdd:COG1135 158 NPKVLLCDEATSALDPETtrsiLDLLKD----INRELGLTIVLITHE----MDVVrricDRVAVLENGRIVEQGPVLDVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 243 EDYGQALTDAgvWIPGAPPALPDARSVACDQDGHPSGDIaietreLDIGygakkswFRGSETVEPI----AR--GVSVSI 316
Cdd:COG1135 230 ANPQSELTRR--FLPTVLNDELPEELLARLREAAGGGRL------VRLT-------FVGESADEPLlselARrfGVDVNI 294
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
298-521 |
3.22e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 298 WFRGSEtvEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATRIGTVFQD 377
Cdd:PRK13638 8 WFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 378 PEHQFVTGTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTF 454
Cdd:PRK13638 86 PEQQIFYTDIDSDIAFSLRNLGVPEAeitRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 455 GQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMDafHPERSGRAAPGQ----RASEEQAG 521
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLR--QGQILTHGAPGEvfacTEAMEQAG 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
34-242 |
3.37e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.06 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA-----VGLVLQDPDsqtI 108
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDS-----GEVLVDGLDVATTPSRelakrLAILRQENH---I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SAR--VGDDVAFG-----AENLGVAPAEIGNRVRASLDLVGL-DLPLDhpthRLSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:COG4604 87 NSRltVRELVAFGrfpysKGRLTAEDREIIDEAIAYLDLEDLaDRYLD----ELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 181 TANIDPA-GVP---VLRDaaitAAERTGAALIVVEHrvdawvDV------VDRIIVLGRGGVIADGAPHRVL 242
Cdd:COG4604 163 LNNLDMKhSVQmmkLLRR----LADELGKTVVIVLH------DInfascyADHIVAMKDGRVVAQGTPEEII 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-212 |
3.44e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 27 RHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatgkllieGRTPASARGAVGLVLQ---DP 103
Cdd:NF040873 1 GYGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS-----------GTVRRAGGARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DsqTISARVGDDVAFG----AENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:NF040873 68 D--SLPLTVRDLVAMGrwarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 180 PTANIDPAGVPVLRDaAITAAERTGAALIVVEH 212
Cdd:NF040873 146 PTTGLDAESRERIIA-LLAEEHARGATVVVVTH 177
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
35-236 |
3.45e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.11 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRTPASA--------RGAVGLVLQD---- 102
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQqkglirqlRQHVGFVFQNfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 PDSQTISARVGDDVAFGAENLGVAPAeignRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:PRK11264 98 PHRTVLENIIEGPVIVKGEPKEEATA----RARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 183 NIDPAGV-PVLRDAAITAAERTgaALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:PRK11264 174 ALDPELVgEVLNTIRQLAQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
283-496 |
3.46e-19 |
|
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: 86.79 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsapwKW 362
Cdd:cd03261 1 IELRGLTKSFGGR-----------TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE-----DI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PS------KKLATRIGTVFQDPEhQFVTGTVLEELQLGPKLVGVNADKRIEEL-LERLRLTALTKAN---PFSLSGGEKR 432
Cdd:cd03261 65 SGlseaelYRLRRRMGMLFQSGA-LFDSLTVFENVAFPLREHTRLSEEEIREIvLEKLEAVGLRGAEdlyPAELSGGMKK 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 433 RLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVV 496
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIA 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-243 |
4.59e-19 |
|
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: 87.31 E-value: 4.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASA---------RGAV 96
Cdd:cd03294 31 LKKTGQTVGV-NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS-----GKVLIDGQDIAAMsrkelrelrRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 GLVLQD----PDSQtisarVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGA 172
Cdd:cd03294 105 SMVFQSfallPHRT-----VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 173 RVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
35-236 |
5.04e-19 |
|
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: 85.73 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT---PASARGAVGLVLQDPdsqtisar 111
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS-----GEITFDGKSyqkNIEALRRIGALIEAP-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 vgddvAF-----GAENLGVAPAEIG---NRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTAN 183
Cdd:cd03268 82 -----GFypnltARENLRLLARLLGirkKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 184 IDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03268 157 LDPDGIKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
298-499 |
5.31e-19 |
|
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: 84.36 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 298 WFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPWK-WPSKKLATRIGTVFQ 376
Cdd:cd03228 7 SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG---VDLRdLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 377 DPehQFVTGTVLEELqlgpklvgvnadkrieellerlrltaltkanpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQ 456
Cdd:cd03228 84 DP--FLFSGTIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081004564 457 DRRTFTELLTLLRQLAdDGRTVISITHDPLVVQAMgDYVVDMD 499
Cdd:cd03228 128 DPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLD 168
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
311-499 |
7.59e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.96 E-value: 7.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQV------AGSGSAPWKWPSKKLATRIGTVFQDpEHQFVT 384
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQLRQHVGFVFQN-FNLFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 385 GTVLEELQLGPKLVG----VNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:PRK11264 100 RTVLENIIEGPVIVKgepkEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 461 FTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:PRK11264 180 VGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMD 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
35-247 |
7.83e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 7.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRtPASARGAV-GLVLQDpDSQTISARVG 113
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH-----GSITLDGK-PVEGPGAErGVVFQN-EGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 114 DDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLR 193
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 194 DAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGgviadgaPHRVLE----DYGQ 247
Cdd:PRK11248 169 TLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVVErlplNFAR 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-230 |
1.31e-18 |
|
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: 84.82 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEGRtPASARGAVGLVLQDPDSQTISARVGDD 115
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-----AQPTSGGVILEGK-QITEPGPDRMVVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 116 VAFgAENLGVAPAEIGNR---VRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVL 192
Cdd:TIGR01184 75 IAL-AVDRVLPDLSKSERraiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081004564 193 RDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-235 |
1.45e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARGA-VGLVLQDP-----D 104
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDS-----GSILIDGkdvtKLPEYKRAKyIGRVFQDPmmgtaP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 105 SQTIsarvgddvafgAENL--------------GVAPAEIgNRVRASLDLVGLDLP--LDHPTHRLSGGQKQrlALAgvL 168
Cdd:COG1101 96 SMTI-----------EENLalayrrgkrrglrrGLTKKRR-ELFRELLATLGLGLEnrLDTKVGLLSGGQRQ--ALS--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 169 AM----GARVICLDEPTANIDPAgvpvlrdaaiTAA---ERTGAalIVVEHRV----------DAwVDVVDRIIVLGRGG 231
Cdd:COG1101 160 LMatltKPKLLLLDEHTAALDPK----------TAAlvlELTEK--IVEENNLttlmvthnmeQA-LDYGNRLIMMHEGR 226
|
....
gi 1081004564 232 VIAD 235
Cdd:COG1101 227 IILD 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
293-525 |
1.48e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 293 GAKKSWFRGSETVEpIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwpSKKLAT--- 369
Cdd:PRK10535 9 DIRRSYPSGEEQVE-VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD--ADALAQlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 370 -RIGTVFQDpEHQFVTGTVLEELQLGPKLVGVNADKRIE---ELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPD 445
Cdd:PRK10535 86 eHFGFIFQR-YHLLSHLTAAQNVEVPAVYAGLERKQRLLraqELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 446 IVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVqAMGDYVV---DMDAFHPERSGRAAPGQRASEEQAGP 522
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVA-AQAERVIeirDGEIVRNPPAQEKVNVAGGTEPVVNT 243
|
...
gi 1081004564 523 SSS 525
Cdd:PRK10535 244 ASG 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-236 |
1.73e-18 |
|
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: 84.69 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRKAAvLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA---- 95
Cdd:cd03267 22 SLKSLFKRKYREVEA-LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS-----GEVRVAGLVPWKRRKKflrr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 VGLVLQDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVI 175
Cdd:cd03267 96 IGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 176 CLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
305-484 |
2.22e-18 |
|
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: 84.66 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 305 VEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQD----PeH 380
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR--EQDPVELRRKIGYVIQQiglfP-H 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 381 QfvtgTVLEELQLGPKLVGV---NADKRIEELLERLRLTALTKAN--PFSLSGGEKRRLSVATMLATAPDIVLLDEPtFG 455
Cdd:cd03295 90 M----TVEENIALVPKLLKWpkeKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLMDEP-FG 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 456 ----------QDrrtftELLTLLRQLaddGRTVISITHD 484
Cdd:cd03295 165 aldpitrdqlQE-----EFKRLQQEL---GKTIVFVTHD 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-246 |
3.33e-18 |
|
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: 84.07 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASAR 93
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEN-----GRVLVDGHdlalaDPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GAVGLVLQDpdSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVgLDLPLDHPT------HRLSGGQKQRLALAGV 167
Cdd:cd03252 76 RQVGVVLQE--NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFI-SELPEGYDTivgeqgAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 168 LAMGARVICLDEPTANID-PAGVPVLRDAAITAAERTgaaLIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPHRVLEDYG 246
Cdd:cd03252 153 LIHNPRILIFDEATSALDyESEHAIMRNMHDICAGRT---VIIIAHRLST-VKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
34-236 |
3.86e-18 |
|
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: 82.60 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddSDGEATGKLLIEGR--TPASARGAVGLVLQdpdsqtisar 111
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR---TGLGVSGEVLINGRplDKRSFRKIIGYVPQ---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 vgDDVAFG----AENLGVApAEIgnrvrasldlvgldlpldhptHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:cd03213 90 --DDILHPtltvRETLMFA-AKL---------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 188 G----VPVLRDAAitaaeRTGAALIVVEHRVDAWV-DVVDRIIVLGRGGVIADG 236
Cdd:cd03213 146 SalqvMSLLRRLA-----DTGRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
278-496 |
5.23e-18 |
|
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: 83.49 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 278 SGDIAIETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG--- 354
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDR-----------VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdi 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 355 ---SGSApwkwpSKKLATRIGTVFQDpehqfvtG------TVLE--------ELQLGPKLVgvnaDKRIEELLERLRLTA 417
Cdd:COG1127 70 tglSEKE-----LYELRRRIGMLFQG-------GalfdslTVFEnvafplreHTDLSEAEI----RELVLEKLELVGLPG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 418 LTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVV 496
Cdd:COG1127 134 AADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVA 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
12-242 |
5.75e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 83.70 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 12 SSGNVPAVSARG----FGYRHagrkaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIaGVLGDDSDGEatgkLLIEGR 87
Cdd:COG4598 2 TDTAPPALEVRDlhksFGDLE------VLKGVSLTARKGDVISIIGSSGSGKSTFLRCI-NLLETPDSGE----IRVGGE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 TPASARGAVG-LVLQDPDS-QTISARVGddVAFGAENL------------------GVAPAEIGNRVRASLDLVGLDLPL 147
Cdd:COG4598 71 EIRLKPDRDGeLVPADRRQlQRIRTRLG--MVFQSFNLwshmtvlenvieapvhvlGRPKAEAIERAEALLAKVGLADKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 148 DH-PTHrLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGV-PVLRDAAITAAErtGAALIVVEHRVDAWVDVVDRII 225
Cdd:COG4598 149 DAyPAH-LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVgEVLKVMRDLAEE--GRTMLVVTHEMGFARDVSSHVV 225
|
250
....*....|....*..
gi 1081004564 226 VLGRGGVIADGAPHRVL 242
Cdd:COG4598 226 FLHQGRIEEQGPPAEVF 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
308-485 |
6.63e-18 |
|
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: 82.70 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMA---GTVQVAGSGSAPWKWPSkklatRIGTVFQDpeHQFVT 384
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQK-----CVAYVRQD--DILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 385 G-TVLEELQLGPKLVGVN--ADKRIEELLE--RLRLTALTK-ANPF--SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQ 456
Cdd:cd03234 95 GlTVRETLTYTAILRLPRksSDAIRKKRVEdvLLRDLALTRiGGNLvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....*....
gi 1081004564 457 DRRTFTELLTLLRQLADDGRTVISITHDP 485
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQP 203
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-495 |
8.07e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.35 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 282 AIETRELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLE-----PMAGTVQVAGSG 356
Cdd:PRK14267 4 AIETVNLRVYYGSNH-----------VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 357 SAPWKWPSKKLATRIGTVFQDPeHQFVTGTVLEELQLGPKLVGVNADKriEELLERLRLtALTKAN------------PF 424
Cdd:PRK14267 73 IYSPDVDPIEVRREVGMVFQYP-NPFPHLTIYDNVAIGVKLNGLVKSK--KELDERVEW-ALKKAAlwdevkdrlndyPS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 425 SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDgRTVISITHDPLVVQAMGDYV 495
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYV 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
283-484 |
1.05e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.82 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKW 362
Cdd:COG4604 2 IEIKNVSKRYGGK-----------VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA--TT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLATRIGTVFQDPehQFVTG-TVLEelqlgpkLVG-----------VNADKR-IEELLERLRLTALtkANPF--SLS 427
Cdd:COG4604 69 PSRELAKRLAILRQEN--HINSRlTVRE-------LVAfgrfpyskgrlTAEDREiIDEAIAYLDLEDL--ADRYldELS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 428 GGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHD 484
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHD 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
282-502 |
1.23e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 282 AIETRELDIGYGAKKSWFrgsetvepiarGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS----GS 357
Cdd:PRK11124 2 SIQLNGINCFYGAHQALF-----------DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 358 APWKWPSKKLATRIGTVFQDpEHQFVTGTVLEELQLGP-KLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRR 433
Cdd:PRK11124 71 TPSDKAIRELRRNVGMVFQQ-YNLWPHLTVQQNLIEAPcRVLGLSkdqALARAEKLLERLRLKPYADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 434 LSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMDAFH 502
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-242 |
1.24e-17 |
|
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: 82.44 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAG-----------VLGDDSDGEATGKLlie 85
Cdd:COG1119 2 PLLELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptygndvrLFGERRGGEDVWEL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 86 grtpasaRGAVGLV---LQDPDSQTISARvgdDV----AFGAenLG----VAPAEIgNRVRASLDLVGLDLPLDHPTHRL 154
Cdd:COG1119 77 -------RKRIGLVspaLQLRFPRDETVL---DVvlsgFFDS--IGlyrePTDEQR-ERARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 155 SGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIA 234
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
....*...
gi 1081004564 235 DGAPHRVL 242
Cdd:COG1119 224 AGPKEEVL 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
35-236 |
2.02e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.60 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLA-------------AIAGVLGDDSDG--EATGKLLiegrtpasaRGAVGLV 99
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRvlnlletpdsgqlNIAGHQFDFSQKpsEKAIRLL---------RQKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 100 LQD----PDSQTIsarvgddvafgaENLGVAPAEI------GNRVRASLDLVGLDL-------PLdhpthRLSGGQKQRL 162
Cdd:COG4161 88 FQQynlwPHLTVM------------ENLIEAPCKVlglskeQAREKAMKLLARLRLtdkadrfPL-----HLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 163 ALAGVLAMGARVICLDEPTANIDPagvpvlrdaAITAA--------ERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIA 234
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDP---------EITAQvveiirelSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
..
gi 1081004564 235 DG 236
Cdd:COG4161 222 QG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
35-236 |
2.61e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.60 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG------RTPASARGA-----VGLVLQD- 102
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRS-----GTLNIAGnhfdfsKTPSDKAIRelrrnVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 ---PD----SQTISA--RVgddvafgaenLGVAPAEIGNRVRASLDLVGLDLPLDH-PTHrLSGGQKQRLALAGVLAMGA 172
Cdd:PRK11124 92 nlwPHltvqQNLIEApcRV----------LGLSKDQALARAEKLLERLRLKPYADRfPLH-LSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 173 RVICLDEPTANIDPagvpvlrdaAITAA--------ERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:PRK11124 161 QVLLFDEPTAALDP---------EITAQivsiirelAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
35-242 |
2.69e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.60 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGddsdgEATGKLLIEGRTPAS------ARGAVGLVLQDPDSQTI 108
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT-----PQSGTVFLGDKPISMlssrqlARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SARvgDDVAFGAE---NL-GVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANI 184
Cdd:PRK11231 92 TVR--ELVAYGRSpwlSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 185 DPA-GVPVLRDAAITAAErtGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:PRK11231 170 DINhQVELMRLMRELNTQ--GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
310-498 |
2.88e-17 |
|
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: 81.23 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwPSKKlatRIGTVFQDpEHQFVTGTVLE 389
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKR---DISYVPQN-YALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVNA---DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLT 466
Cdd:cd03299 91 NIAYGLKKRKVDKkeiERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 467 LLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:cd03299 171 ELKKIRKEfGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
35-236 |
3.05e-17 |
|
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: 80.65 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGAVGLvlqDPDsqtISARvgD 114
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS-----GTVTVRGRVSSLLGLGGGF---NPE---LTGR--E 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 115 DVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTAnidpAGvpvlrD 194
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA----VG-----D 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081004564 195 AA--ITAAER------TGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03220 175 AAfqEKCQRRlrellkQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
36-238 |
3.18e-17 |
|
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: 80.49 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG----RTPASARGAVGLVLQDPDSqtisar 111
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS-----GRATVAGhdvvREPREVRRRIGIVFQDLSV------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 vgDDVAFGAENL-------GVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANI 184
Cdd:cd03265 85 --DDELTGWENLyiharlyGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 185 DPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAP 238
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-482 |
3.82e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPA- 90
Cdd:PRK09700 4 PYISMAGIGKSFGPVHA--LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK-----GTITINNInynklDHKl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 91 SARGAVGLVLQDpdsqtisARVGDDVAFgAENLGVAPAEIGN------------RVRAS--LDLVGLDLPLDHPTHRLSG 156
Cdd:PRK09700 77 AAQLGIGIIYQE-------LSVIDELTV-LENLYIGRHLTKKvcgvniidwremRVRAAmmLLRVGLKVDLDEKVANLSI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 157 GQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRdAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 237 APHRVLEDYGQALTdAGVWIPGAPPALPDARSvacdqdgHPSGDIAIETRELdIGYGAKKswfrgsetvepiARGVSVSI 316
Cdd:PRK09700 228 MVSDVSNDDIVRLM-VGRELQNRFNAMKENVS-------NLAHETVFEVRNV-TSRDRKK------------VRDISFSV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 317 PSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPwKWPSKKLATRIGTVfqdPEHQFVTG----------- 385
Cdd:PRK09700 287 CRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP-RSPLDAVKKGMAYI---TESRRDNGffpnfsiaqnm 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLG--PKLVGVNADKRIEELLERLR-LTALTKA----NPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDR 458
Cdd:PRK09700 363 AISRSLKDGgyKGAMGLFHEVDEQRTAENQReLLALKCHsvnqNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
490 500
....*....|....*....|....
gi 1081004564 459 RTFTELLTLLRQLADDGRTVISIT 482
Cdd:PRK09700 443 GAKAEIYKVMRQLADDGKVILMVS 466
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-236 |
4.31e-17 |
|
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: 80.03 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIE---RGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT----------PASARGaVGLVLQD 102
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDG-----GTIVLNGTVlfdsrkkinlPPQQRK-IGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 ----PdsqtiSARVGDDVAFGAEnlGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLD 178
Cdd:cd03297 84 yalfP-----HLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 179 EPTANIDPAgvpvLRDAAITAAERTGAAL----IVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:cd03297 157 EPFSALDRA----LRLQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
35-245 |
5.96e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGAVGLvlqDPDsqtISARvgD 114
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS-----GRVEVNGRVSALLELGAGF---HPE---LTGR--E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 115 DVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTAnidpAGvpvlrD 194
Cdd:COG1134 108 NIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLA----VG-----D 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 195 AA--------ITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDY 245
Cdd:COG1134 179 AAfqkkclarIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
283-483 |
6.82e-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: 79.57 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGsapWKW 362
Cdd:cd03268 1 LKTNDLTKTYGKK-----------RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS---YQK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLAtRIGTVFQDPEhqfVTG--TVLEELQLGPKLVGVNaDKRIEELLERLRLTALT--KANPFSLsgGEKRRLSVAT 438
Cdd:cd03268 67 NIEALR-RIGALIEAPG---FYPnlTARENLRLLARLLGIR-KKRIDEVLDVVGLKDSAkkKVKGFSL--GMKQRLGIAL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081004564 439 MLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITH 483
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH 184
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-254 |
6.87e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.34 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 33 AAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRT-----PASARGAVGLVLQDPDS-Q 106
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDifkmdVIELRRRVQMVFQIPNPiP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 TISarVGDDVAFGAE--NLGVAPAEIGNRVRASLDLVGL----DLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:PRK14247 96 NLS--IFENVALGLKlnRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 181 TANIDPAGVPVLRdaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDYGQALTDAGV 254
Cdd:PRK14247 174 TANLDPENTAKIE--SLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
26-187 |
8.41e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.77 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEGR--TPAS------ARGAVG 97
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-----ERPTSGRVLVDGQdlTALSekelrkARRQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 LVLQdpDSQTISAR-VGDDVAFGAENLGVAPAEIGNRVRASLDLVGL-DLPLDHPThRLSGGQKQRLALAGVLAMGARVI 175
Cdd:PRK11153 86 MIFQ--HFNLLSSRtVFDNVALPLELAGTPKAEIKARVTELLELVGLsDKADRYPA-QLSGGQKQRVAIARALASNPKVL 162
|
170
....*....|..
gi 1081004564 176 CLDEPTANIDPA 187
Cdd:PRK11153 163 LCDEATSALDPA 174
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
310-500 |
9.19e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKStlaltlggllEPMAGTVQVAG---SGSAPWKWPskklatrIGTVFQD----PeHQf 382
Cdd:COG3842 22 DDVSLSIEPGEFVALLGPSGCGKTtllrmiagfeTPDSGRILLDGrdvTGLPPEKRN-------VGMVFQDyalfP-HL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 vtgTVLEELQLGPKLVGVNA---DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPtFGQ-D- 457
Cdd:COG3842 93 ---TVAENVAFGLRMRGVPKaeiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP-LSAlDa 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081004564 458 ---RRTFTELLTLLRQLaddGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:COG3842 169 klrEEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMND 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-483 |
1.15e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAG----------VLGDD-SDgeatgkllieg 86
Cdd:NF033858 1 VARLEGVSHRYGKTVA--LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiqqgrveVLGGDmAD----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 87 rtpASARgavglvlqdpdsqtisARVGDDVAF-----G---------AENL-------GVAPAEIGNRVRASLDLVGLDL 145
Cdd:NF033858 68 ---ARHR----------------RAVCPRIAYmpqglGknlyptlsvFENLdffgrlfGQDAAERRRRIDELLRATGLAP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 146 PLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAG-------VPVLRdaaitaAERTGAALIVVEhrvdAWV 218
Cdd:NF033858 129 FADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSrrqfwelIDRIR------AERPGMSVLVAT----AYM 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 219 DVVDR---IIVLGRGGVIADGAPHRVLEDYGQA-LTDAGVWIpgappaLPDARsvacdQDGH-----------PSGDIAI 283
Cdd:NF033858 199 EEAERfdwLVAMDAGRVLATGTPAELLARTGADtLEAAFIAL------LPEEK-----RRGHqpvvipprpadDDDEPAI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 284 ETRELDIGYGA-----KKSwFRgsetvepIARGvsvsipsEastcI---VGHNGSGKSTLALTLGGLLEPMAGTVQVAGS 355
Cdd:NF033858 268 EARGLTMRFGDftavdHVS-FR-------IRRG-------E----IfgfLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 356 GSAPwkwpsKKLATR--IGTVFQdpehqfvtG-------TVLEELQLGPKLVGVNADK---RIEELLERLRLTALTKANP 423
Cdd:NF033858 329 PVDA-----GDIATRrrVGYMSQ--------AfslygelTVRQNLELHARLFHLPAAEiaaRVAEMLERFDLADVADALP 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 424 FSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTFTELL-TLLRQladDGRTV-ISiTH 483
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvaRDMFWRLLiELSRE---DGVTIfIS-TH 456
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
308-484 |
1.15e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.01 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS-------GSAPWKWPSKK----LATRIGTVFQ 376
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKVADKNqlrlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 377 DpEHQFVTGTVLEELQLGP-KLVGVN---ADKRIEELLERLRLTALTKAN-PFSLSGGEKRRLSVATMLATAPDIVLLDE 451
Cdd:PRK10619 100 H-FNLWSHMTVLENVMEAPiQVLGLSkqeARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 452 PTFGQDRRTFTELLTLLRQLADDGRTVISITHD 484
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-238 |
1.17e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 14 GNVPAVSARG----FGyrhaGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-- 87
Cdd:COG3845 1 MMPPALELRGitkrFG----GVVA--NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDS-----GEILIDGKpv 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 ---TPASARGA-VGLVLQDP---DSQTisarVGDDVAFGAENLG---VAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGG 157
Cdd:COG3845 70 rirSPRDAIALgIGMVHQHFmlvPNLT----VAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 158 QKQRLALAGVLAMGARVICLDEPTANIDPAGVP----VLRDAAitaaeRTGAALIVVEHRVDAWVDVVDRIIVLGRGGVI 233
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADelfeILRRLA-----AEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
....*
gi 1081004564 234 ADGAP 238
Cdd:COG3845 221 GTVDT 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-233 |
1.39e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 10 PSSSGNvPAVSARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEATgklliegrtp 89
Cdd:COG0488 308 PERLGK-KVLELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS-GTVK---------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 90 asaRGA---VGLVLQDPDSQTISARVGDDVAFGAENLGvaPAEI----------GNRVRAsldlvgldlpldhPTHRLSG 156
Cdd:COG0488 374 ---LGEtvkIGYFDQHQEELDPDKTVLDELRDGAPGGT--EQEVrgylgrflfsGDDAFK-------------PVGVLSG 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 157 GQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAItaaERTGaALIVVEHrvDAW-VD-VVDRIIVLGRGGVI 233
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD---DFPG-TVLLVSH--DRYfLDrVATRILEFEDGGVR 508
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
276-485 |
1.47e-16 |
|
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: 79.01 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 276 HPSGDIAIETRELDigygakKSWFRGSETVEpIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS 355
Cdd:COG4181 2 SSSSAPIIELRGLT------KTVGTGAGELT-ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 356 --------GSApwkwpsKKLATRIGTVFQDpEHQFVTGTVLEELQLGPKLVGV-NADKRIEELLERLRLTALTKANPFSL 426
Cdd:COG4181 75 dlfaldedARA------RLRARHVGFVFQS-FQLLPTLTALENVMLPLELAGRrDARARARALLERVGLGHRLDHYPAQL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 427 SGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDP 485
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDP 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
36-498 |
1.49e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.18 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddSDGEATGKLLIEGrTPASARG-----AVGLVLQDPDSQTI-S 109
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY---PHGTWDGEIYWSG-SPLKASNirdteRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDVAFGAE----NLGVAPAEIGNRVRASLDLVGLD-LPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANI 184
Cdd:TIGR02633 93 LSVAENIFLGNEitlpGGRMAYNAMYLRAKNLLRELQLDaDNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 185 DPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDygQALTD-AGVWIPGAPPAL 263
Cdd:TIGR02633 173 TEKETEILLD-IIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSED--DIITMmVGREITSLYPHE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 264 PdarsvacdqdgHPSGDIAIETRELdigygakKSWfrgsETVEP-IAR--GVSVSIPSEASTCIVGHNGSGKSTLALTLG 340
Cdd:TIGR02633 250 P-----------HEIGDVILEARNL-------TCW----DVINPhRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 341 GLLE-PMAGTVQVAGSGSAPwKWPSKKLATRIGTVFQDPEHQFVT-------GTVLEELQLGPKLVGVNADKRIEELLER 412
Cdd:TIGR02633 308 GAYPgKFEGNVFINGKPVDI-RNPAQAIRAGIAMVPEDRKRHGIVpilgvgkNITLSVLKSFCFKMRIDAAAELQIIGSA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 413 LRLTALTKANPF----SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVV 488
Cdd:TIGR02633 387 IQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEV 466
|
490
....*....|
gi 1081004564 489 QAMGDYVVDM 498
Cdd:TIGR02633 467 LGLSDRVLVI 476
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-244 |
1.53e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.92 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR--TPAS----AR 93
Cdd:COG1137 5 EAENLVKSYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS-----GRIFLDGEdiTHLPmhkrAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GAVGLVLQDPdsqTISAR--VGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMG 171
Cdd:COG1137 78 LGIGYLPQEA---SIFRKltVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 172 ARVICLDEPTANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNN 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
283-510 |
1.68e-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: 78.63 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAkkswfrgsetvEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGSAP 359
Cdd:cd03224 1 LEVENLNAGYGK-----------SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrdiTGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 360 WKwpskklATRIGTVFQdPEHQ--FVTGTVLEELQLGP-KLVGVNADKRIEELLERL-RLTALTKANPFSLSGGEKRRLS 435
Cdd:cd03224 70 HE------RARAGIGYV-PEGRriFPELTVEENLLLGAyARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 436 VATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMDAFHPERSGRAA 510
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
293-493 |
1.69e-16 |
|
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: 78.91 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 293 GAKKSWFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAgsGSAPWKwPSKKLATRIG 372
Cdd:cd03267 21 GSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA--GLVPWK-RRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 373 TVFQDPEHQFVTGTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLL 449
Cdd:cd03267 98 VVFGQKTQLWWDLPVIDSFYLLAAIYDLPPArfkKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081004564 450 DEPTFGQDRRTFTELLTLLRQL-ADDGRTVISITHDplvvqaMGD 493
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHY------MKD 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
35-212 |
1.71e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEGRT----PASARGAV-----GLVLQD--- 102
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPmsklSSAAKAELrnqklGFIYQFhhl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 -PDSQTIsarvgDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPT 181
Cdd:PRK11629 99 lPDFTAL-----ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|.
gi 1081004564 182 ANIDPAGVPVLRDAAITAAERTGAALIVVEH 212
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-252 |
2.35e-16 |
|
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: 82.04 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRKAAVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgEATGKLLIEGRTPASARGA------ 95
Cdd:COG4172 289 RGLFRRTVGHVKAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI------PSEGEIRFDGQDLDGLSRRalrplr 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 --VGLVLQDPDSqTISAR--VGDDVAFG--AENLGVAPAEIGNRVRASLDLVGLDLPLDH--PtHRLSGGQKQRLALAGV 167
Cdd:COG4172 362 rrMQVVFQDPFG-SLSPRmtVGQIIAEGlrVHGPGLSAAERRARVAEALEEVGLDPAARHryP-HEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 168 LAMGARVICLDEPTANIDpagVPV-------LRDaaitAAERTGAALIVVEHrvDawVDVV----DRIIVLGRGGVIADG 236
Cdd:COG4172 440 LILEPKLLVLDEPTSALD---VSVqaqildlLRD----LQREHGLAYLFISH--D--LAVVralaHRVMVMKDGKVVEQG 508
|
250 260
....*....|....*....|
gi 1081004564 237 APHRVLE----DYGQALTDA 252
Cdd:COG4172 509 PTEQVFDapqhPYTRALLAA 528
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-227 |
2.52e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.22 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASARGAV 96
Cdd:PRK10247 11 QNVGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS-----GTLLFEGEdistlKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 GLVLQDP----DSqtisarVGDDVAFGAENLGVAPAEigNRVRASLDLVGLDLP-LDHPTHRLSGGQKQRLALAGVLAMG 171
Cdd:PRK10247 84 SYCAQTPtlfgDT------VYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 172 ARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAwVDVVDRIIVL 227
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
31-236 |
2.64e-16 |
|
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: 78.21 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 31 RKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRtPASARG--AVGLVLQDPDS-QT 107
Cdd:TIGR03740 11 GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTS-----GEIIFDGH-PWTRKDlhKIGSLIESPPLyEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISARvgDDVAFGAENLGVAPAEIgNRVrasLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:TIGR03740 85 LTAR--ENLKVHTTLLGLPDSRI-DEV---LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081004564 188 GVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIivlgrgGVIADG 236
Cdd:TIGR03740 159 GIQELRE-LIRSFPEQGITVILSSHILSEVQQLADHI------GIISEG 200
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-254 |
2.96e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLG-DDSDGEATGKLLIEGRT-----PASARGAVGLVLQDPDSQT 107
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLYFGKDifqidAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 iSARVGDDVAFGAENLGVAPA-EIGNRVRASLDLVGL----DLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:PRK14246 104 -HLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 183 NIDPAGVPVLrDAAITAAERTgAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDYGQALTDAGV 254
Cdd:PRK14246 183 MIDIVNSQAI-EKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
311-508 |
3.05e-16 |
|
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: 78.05 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGSAPWKWPskklatrIGTVFQD----PeHQfv 383
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkdiTNLPPHKRP-------VNTVFQNyalfP-HL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 tgTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:cd03300 88 --TVFENIAFGLRLKKLPKAeikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081004564 461 FTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMDAFHPERSGR 508
Cdd:cd03300 166 RKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-233 |
4.05e-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: 77.70 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 29 AGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgdDSDGEATGKLLIEG--RTPASARGAVGLVLQDpDSQ 106
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNGqpRKPDQFQKCVAYVRQD-DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 TISARVGDDVAFGAENLGvaPAEIGNRVRASLDLVGL-----DLPLDHPTHR-LSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:cd03234 93 LPGLTVRETLTYTAILRL--PRKSSDAIRKKRVEDVLlrdlaLTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 181 TANIDPAG----VPVLRDAAitaaeRTGAALIVVEH--RVDAWvDVVDRIIVLGRGGVI 233
Cdd:cd03234 171 TSGLDSFTalnlVSTLSQLA-----RRNRIVILTIHqpRSDLF-RLFDRILLLSSGEIV 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
36-244 |
4.27e-16 |
|
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: 81.00 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVL-----------GDDSDGEATGKLLIEGRtpasARGAVGLVLQDPD 104
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLeptsgevnvrvGDEWVDMTKPGPDGRGR----AKRYIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 105 ---SQTISARVGDdvAFGAEnlgvAPAEIGnRVRA--SLDLVGLDLP-----LDHPTHRLSGGQKQRLALAGVLAMGARV 174
Cdd:TIGR03269 376 lypHRTVLDNLTE--AIGLE----LPDELA-RMKAviTLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 175 ICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
30-246 |
4.80e-16 |
|
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: 81.32 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRTPASARGAVGLVLQDPdsQTIS 109
Cdd:TIGR01193 484 GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEP--YIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDVAFGAeNLGVAPAEIGNRVR-ASLDL------VGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:TIGR01193 562 GSILENLLLGA-KENVSQDEIWAACEiAEIKDdienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 183 NIDPAGVPVLRDAAITAAERTgaaLIVVEHRVDAwVDVVDRIIVLGRGGVIADGApHRVLEDYG 246
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQDKT---IIFVAHRLSV-AKQSDKIIVLDHGKIIEQGS-HDELLDRN 699
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-208 |
8.21e-16 |
|
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: 75.86 E-value: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGAVGLV 99
Cdd:TIGR01189 2 AARNLACSRGER--MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS-----GEVRWNGTPLAEQRDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 100 L-----QDPDSQTISARvgDDVAFGAENLGVAPaeigNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARV 174
Cdd:TIGR01189 75 IlylghLPGLKPELSAL--ENLHFWAAIHGGAQ----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....
gi 1081004564 175 ICLDEPTANIDPAGVPVLRDAAITAAERTGAALI 208
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARGGIVLL 182
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
312-499 |
9.21e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKK----LATRIGTVFQDpEHQFVTGTV 387
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKairlLRQKVGMVFQQ-YNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGP-KLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTE 463
Cdd:COG4161 100 MENLIEAPcKVLGLSkeqAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081004564 464 LLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:COG4161 180 VVEIIRELSQTGITQVIVTHEVEFARKVASQVVYME 215
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-242 |
9.44e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 80.08 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGddsdgEATGKLLIEGrtpASARG--------AVG 97
Cdd:TIGR01842 324 IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP-----PTSGSVRLDG---ADLKQwdretfgkHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 LVLQDPD--SQTIS---ARVGDDVAfgAENLgVAPAEIgnrvrASLDLVGLDLPLDHPTH------RLSGGQKQRLALAG 166
Cdd:TIGR01842 396 YLPQDVElfPGTVAeniARFGENAD--PEKI-IEAAKL-----AGVHELILRLPDGYDTVigpggaTLSGGQRQRIALAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 167 VLAMGARVICLDEPTANIDPAGVPVLRdAAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALA-NAIKALKARGITVVVITHRPSL-LGCVDKILVLQDGRIARFGERDEVL 541
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
299-499 |
9.88e-16 |
|
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: 80.26 E-value: 9.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVagSGSAPWKWPSKKLATRIGTVFQDP 378
Cdd:COG2274 481 FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI--DGIDLRQIDPASLRRQIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 ehQFVTGTVLEELQLGpklvgvNADKRIEELLERLRLTALT---KANP-----------FSLSGGEKRRLSVATMLATAP 444
Cdd:COG2274 559 --FLFSGTIRENITLG------DPDATDEEIIEAARLAGLHdfiEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 445 DIVLLDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITHDP-LVVQAmgDYVVDMD 499
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLsTIRLA--DRIIVLD 683
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-214 |
1.01e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.38 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 16 VPAVSARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIagvlgdDSDGEATGKLLIEGRTP------ 89
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL------NRMNELESEVRVEGRVEffnqni 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 90 -------ASARGAVGLVLQDPDSQTISarVGDDVAFGAENLGVAPA-EIGNRVRASLDLVGLDLPLDHPTHR----LSGG 157
Cdd:PRK14258 77 yerrvnlNRLRRQVSMVHPKPNLFPMS--VYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKIHKsaldLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 158 QKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRV 214
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
310-499 |
1.04e-15 |
|
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: 76.25 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPwkwPSKKLATRIGTVFQDPE-HQFVTGTvl 388
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR---EPREVRRRIGIVFQDLSvDDELTGW-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 389 EELQLGPKLVGV---NADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL 465
Cdd:cd03265 92 ENLYIHARLYGVpgaERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1081004564 466 TLLRQL-ADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:cd03265 172 EYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-238 |
1.05e-15 |
|
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: 75.91 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgEA-TGKLLIEGRTPASA----- 92
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL------EAeEGKIEIDGIDISTIpledl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAVGLVLQDPD--SQTISArvgddvafgaeNLGVAPAEIGNRVRASLDLVGLDLpldhpthRLSGGQKQRLALAGVLAM 170
Cdd:cd03369 81 RSSLTIIPQDPTlfSGTIRS-----------NLDPFDEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 171 GARVICLDEPTANIDPAgvpvlRDAAITAAER---TGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAP 238
Cdd:cd03369 143 RPRVLVLDEATASIDYA-----TDALIQKTIReefTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-236 |
1.17e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.89 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 39 ITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgEATGKLLIEGR-----TPASARGAVGLVLQDPdsQTISARVG 113
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL------PYQGSLKINGIelrelDPESWRKHLSWVGQNP--QLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 114 DDVAFGAENLG-------VAPAEIGNRVRASLDlvGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDp 186
Cdd:PRK11174 441 DNVLLGNPDASdeqlqqaLENAWVSEFLPLLPQ--GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD- 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081004564 187 AGVPVLRDAAITAAERtGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADG 236
Cdd:PRK11174 518 AHSEQLVMQALNAASR-RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-485 |
1.28e-15 |
|
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: 76.09 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSapWKWPSKKLATRIGTVFQDPehQFVTGTVLEELQLGPKLVgvnAD 403
Cdd:cd03245 35 IIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI--RQLDPADLRRNIGYVPQDV--TLFYGTLRDNITLGAPLA---DD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 404 KRIEELLERLRLTALTKANP-----------FSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLA 472
Cdd:cd03245 108 ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL 187
|
170
....*....|...
gi 1081004564 473 DDgRTVISITHDP 485
Cdd:cd03245 188 GD-KTLIIITHRP 199
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
310-500 |
1.84e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.81 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKStlaltlggllEPMAGTVQVAG------SGsapwkwpsKKLAT---RIGTVFQdpeh 380
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKStlircinlleRPTSGSVLVDGvdltalSE--------RELRAarrKIGMIFQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 381 QF---VTGTVLE--ELQLgpKLVGVNA---DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEP 452
Cdd:COG1135 90 HFnllSSRTVAEnvALPL--EIAGVPKaeiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081004564 453 TFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:COG1135 168 TSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLEN 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
41-232 |
1.87e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 75.28 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 41 LDIERGEKVLLLGASGMGKSTLLAAIAGVLGddsdgEATGKLLIEG----RTPASARgAVGLVLQDPD---SQTISARVG 113
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIE-----PASGSIKVNDqshtGLAPYQR-PVSMLFQENNlfaHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 114 ddvafgaenLGVAP-----AEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAg 188
Cdd:TIGR01277 93 ---------LGLHPglklnAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081004564 189 vpvLRDAAIT----AAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGV 232
Cdd:TIGR01277 163 ---LREEMLAlvkqLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
298-484 |
1.91e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.44 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 298 WFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPWKWPSkklATRiGTVFQD 377
Cdd:COG4525 12 RYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG---VPVTGPG---ADR-GVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 378 pEHQFVTGTVLEELQLGPKLVGVNADKR---IEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPtF 454
Cdd:COG4525 85 -DALLPWLNVLDNVAFGLRLRGVPKAERrarAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP-F 162
|
170 180 190
....*....|....*....|....*....|....
gi 1081004564 455 GQ----DRRTFTELltLLRQLADDGRTVISITHD 484
Cdd:COG4525 163 GAldalTREQMQEL--LLDVWQRTGKGVFLITHS 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-520 |
2.20e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 16 VPAVSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTP--ASAR 93
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKA--LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA-----GSILIDGQEMrfASTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GA----VGLVLQD----PDsQTIsarvgddvafgAEN--LGVAPAEIG--------NRVRASLDLVGLDLPLDHPTHRLS 155
Cdd:PRK11288 75 AAlaagVAIIYQElhlvPE-MTV-----------AENlyLGQLPHKGGivnrrllnYEAREQLEHLGVDIDPDTPLKYLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 156 GGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRdAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIAD 235
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLF-RVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 236 -----GAPHRVL--EDYGQALTDAGVWIPgappalpdarsvacdqdgHPSGDIAIETRELDiGYGAKkswfrgsetvEPI 308
Cdd:PRK11288 222 fddmaQVDRDQLvqAMVGREIGDIYGYRP------------------RPLGEVRLRLDGLK-GPGLR----------EPI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 309 argvSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPWKWPSKKLATRIGTVFQdPEHQFVTG--- 385
Cdd:PRK11288 273 ----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIRAGIMLC-PEDRKAEGiip 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 --TVLEELQ-------------LGPKLVGVNADKRIeellERLRL-TALTKANPFSLSGGEKRRLSVATMLATAPDIVLL 449
Cdd:PRK11288 345 vhSVADNINisarrhhlragclINNRWEAENADRFI----RSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILL 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 450 DEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDMdafhpeRSGRAA---PGQRASEEQA 520
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM------REGRIAgelAREQATERQA 488
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
26-233 |
2.25e-15 |
|
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: 76.38 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAG-----RKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLLIEGRTpaSARGA 95
Cdd:TIGR02769 12 YRTGGlfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQgtvsfRGQDLYQLDRKQRR--AFRRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 96 VGLVLQD-PDSQTISARVGDDVAFGAENL-GVAPAEIGNRVRASLDLVGLDLP-LDHPTHRLSGGQKQRLALAGVLAMGA 172
Cdd:TIGR02769 90 VQLVFQDsPSAVNPRMTVRQIIGEPLRHLtSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 173 RVICLDEPTANIDpagvPVLRDAAITAAE----RTGAALIVVEHRVDAWVDVVDRIIVLGRGGVI 233
Cdd:TIGR02769 170 KLIVLDEAVSNLD----MVLQAVILELLRklqqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-242 |
2.33e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 39 ITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgdDSDGEAT--GKLLIEGRTPASARGAVGLVLQDPDS------QTISA 110
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL--PGSGSIQfaGQPLEAWSAAELARHRAYLSQQQTPPfampvfQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 RVGDdvafgaenlGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAM-------GARVICLDEPTAN 183
Cdd:PRK03695 93 HQPD---------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 184 IDPAGVPVLrDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:PRK03695 164 LDVAQQAAL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
310-500 |
2.59e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.15 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLAT---RIGTVFQdpeHqF---V 383
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT--ALSEKELRKarrQIGMIFQ---H-FnllS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 TGTVLEELQLGPKLVGVNA---DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:PRK11153 96 SRTVFDNVALPLELAGTPKaeiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081004564 461 FTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:PRK11153 176 TRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDA 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-246 |
2.98e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 76.30 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTpasargavg 97
Cdd:COG4152 1 MLELKGLTKRFGDKTA--VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS-----GEVLWDGEP--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 lvLQDPDSQTI-----------SARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAG 166
Cdd:COG4152 65 --LDPEDRRRIgylpeerglypKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 167 VLAMGARVICLDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDYG 246
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKD-VIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
312-500 |
3.61e-15 |
|
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: 77.07 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG----SGSAPWKWPSKKlaTRIGTVFQDPEhQFVTGTV 387
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfDSRKGIFLPPEK--RRIGYVFQEAR-LFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKLVGVnADKRI--EELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL 465
Cdd:TIGR02142 93 RGNLRYGMKRARP-SERRIsfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081004564 466 TLLRQLADDGRT-VISITHDPLVVQAMGDYVVDMDA 500
Cdd:TIGR02142 172 PYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLED 207
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
310-510 |
3.77e-15 |
|
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: 75.07 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwkwpSKKLATR-IGTVFQdpeHQ--FVTGT 386
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-----DVPVQERnVGFVFQ---HYalFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VLEELQLG----PKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:cd03296 91 VFDNVAFGlrvkPRSERPPEAeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 460 TFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMDAFHPERSGRAA 510
Cdd:cd03296 171 VRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
323-485 |
3.77e-15 |
|
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: 75.76 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 323 CIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKL----ATRIGTVFQD----PeHQfvtgTVLEELQLG 394
Cdd:cd03294 54 VIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA--AMSRKELrelrRKKISMVFQSfallP-HR----TVLENVAFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 395 PKLVGVNADKRIE---ELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTF-TELLTL 467
Cdd:cd03294 127 LEVQGVPRAEREEraaEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpliRREMqDELLRL 206
|
170
....*....|....*...
gi 1081004564 468 LRQLaddGRTVISITHDP 485
Cdd:cd03294 207 QAEL---QKTIVFITHDL 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
35-231 |
3.98e-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: 72.48 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDsdgeatgklliEGRTPASARGAVGLVLQdpdsqtisarvgd 114
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD-----------EGIVTWGSTVKIGYFEQ------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 115 dvafgaenlgvapaeignrvrasldlvgldlpldhpthrLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRD 194
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 195 aAITAAERTgaaLIVVEHrvDAW-VD-VVDRIIVLGRGG 231
Cdd:cd03221 112 -ALKEYPGT---VILVSH--DRYfLDqVATKIIELEDGK 144
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
34-212 |
4.36e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEAT--GKLLI----EGRTPASARGaVGLVLQD----P 103
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAG-LDDGSSGEVSlvGQPLHqmdeEARAKLRAKH-VGFVFQSfmliP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 dsqTISARvgDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTAN 183
Cdd:PRK10584 102 ---TLNAL--ENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180
....*....|....*....|....*....
gi 1081004564 184 IDPAGVPVLRDAAITAAERTGAALIVVEH 212
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-232 |
4.58e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEatgklLIEGRTP-ASARGAVGLVL 100
Cdd:PRK11247 16 NAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGE-----LLAGTAPlAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 101 QDpdsqtisAR------VGDDVAFGAEnlgvapaeiGN---RVRASLDLVGL-DLPLDHPThRLSGGQKQRLALAGVLAM 170
Cdd:PRK11247 88 QD-------ARllpwkkVIDNVGLGLK---------GQwrdAALQALAAVGLaDRANEWPA-ALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 171 GARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGV 232
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
30-230 |
4.73e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 74.39 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAG--------VLGDDSDG-----EATGKLLIEGRtpasaRGAV 96
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsILVRHDGGwvdlaQASPREILALR-----RRTI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 GLVlqdpdSQTISA--RVG--DDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPL-DHPTHRLSGGQKQRLALAGVLAMG 171
Cdd:COG4778 96 GYV-----SQFLRVipRVSalDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 172 ARVICLDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVE-LIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
324-491 |
6.51e-15 |
|
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: 74.12 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsapwkwPSKKLATRIGTVFQdpEHQF-------VTGTVL--EELQLG 394
Cdd:TIGR03771 11 LLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-------SPGKGWRHIGYVPQ--RHEFawdfpisVAHTVMsgRTGHIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 395 PKLVGVNADKR-IEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLAD 473
Cdd:TIGR03771 82 WLRRPCVADFAaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAG 161
|
170
....*....|....*...
gi 1081004564 474 DGRTVISITHDplVVQAM 491
Cdd:TIGR03771 162 AGTAILMTTHD--LAQAM 177
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-244 |
6.56e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 11 SSSGNVPAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDsdgeaTGKLLIEG-RTP 89
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-----AGKITVLGvPVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 90 ASARGA---VGLVLQ-DPDSQTISARvgddvafgaENL-------GVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQ 158
Cdd:PRK13536 107 ARARLArarIGVVPQfDNLDLEFTVR---------ENLlvfgryfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 159 KQRLALAGVLAMGARVICLDEPTANIDPAGVPVL--RDAAITAaerTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIweRLRSLLA---RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
....*...
gi 1081004564 237 APHRVLED 244
Cdd:PRK13536 255 RPHALIDE 262
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-243 |
8.78e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 14 GNVPAVSARGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLIEGRTPaSAR 93
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 94 GAVGLVLQ----DPDSQtisarVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLA 169
Cdd:PRK13537 80 QRVGVVPQfdnlDPDFT-----VRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 170 MGARVICLDEPTANIDPAGVPVL--RDAAITAAERTgaaLIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMweRLRSLLARGKT---ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
38-244 |
8.90e-15 |
|
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: 75.92 E-value: 8.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 38 DITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARG---------AVGLVLQDpdsqti 108
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDE-----GEIVLNGRTLFDSRKgiflppekrRIGYVFQE------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 sAR------VGDDVAFGAENlgVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:TIGR02142 84 -ARlfphlsVRGNLRYGMKR--ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 183 NIDPAgvpvLRDAAITAAER----TGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:TIGR02142 161 ALDDP----RKYEILPYLERlhaeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
307-483 |
9.35e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 9.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPeHQFvTGT 386
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA--DYSEAALRQAISVVSQRV-HLF-SAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VLEELQLGPKLVGvnaDKRIEELLERLRLTALTKANP----------FSLSGGEKRRLSVA-TMLATAPdIVLLDEPTFG 455
Cdd:PRK11160 430 LRDNLLLAAPNAS---DEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIArALLHDAP-LLLLDEPTEG 505
|
170 180
....*....|....*....|....*...
gi 1081004564 456 QDRRTFTELLTLLRQLADDgRTVISITH 483
Cdd:PRK11160 506 LDAETERQILELLAEHAQN-KTVLMITH 532
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-246 |
9.86e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 9.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASARGAVGL 98
Cdd:PRK11160 346 FTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ-----GEILLNGQpiadySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 VLQDPD--SQTIsarvgddvafgAENLGVA-PAEIGNRVRASLDLVGLDLPLDHPT----------HRLSGGQKQRLALA 165
Cdd:PRK11160 419 VSQRVHlfSATL-----------RDNLLLAaPNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 166 GVLAMGARVICLDEPTANIDPAG----VPVLRDaaiTAAERTgaaLIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPHRV 241
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETerqiLELLAE---HAQNKT---VLMITHRLTG-LEQFDRICVMDNGQIIEQGTHQEL 560
|
....*
gi 1081004564 242 LEDYG 246
Cdd:PRK11160 561 LAQQG 565
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
310-500 |
1.09e-14 |
|
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: 73.76 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLAT---RIGTVFQD---PEHQFV 383
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN--KLKGKALRQlrrQIGMIFQQfnlIERLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 TGTVL-------EELQLGPKLVGVNADKRIEELLERLRLT--ALTKANpfSLSGGEKRRLSVATMLATAPDIVLLDEPTF 454
Cdd:cd03256 96 LENVLsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGLLdkAYQRAD--QLSGGQQQRVAIARALMQQPKLILADEPVA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 455 GQDRRTFTELLTLLRQLA-DDGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:cd03256 174 SLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKD 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
308-495 |
1.11e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.93 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS----GSAPWKWPSKKLATRIGTVFQDPeHQFV 383
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfGKDIFQIDAIKLRKEVGMVFQQP-NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 TGTVLEELQLGPKLVGVNADKRIEELLER-LRLTALTKA------NPFS-LSGGEKRRLSVATMLATAPDIVLLDEPTFG 455
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEEcLRKVGLWKEvydrlnSPASqLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081004564 456 QDRRTFTELLTLLRQLADDgRTVISITHDPLVVQAMGDYV 495
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYV 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
310-496 |
1.12e-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: 73.08 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwpskklATRIGTVfqdPEHQ--FVTGTV 387
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------RNRIGYL---PEERglYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:cd03269 88 IDQLVYLAQLKGLKkeeARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190
....*....|....*....|....*....|..
gi 1081004564 465 LTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:cd03269 168 KDVIRELARAGKTVILSTHQMELVEELCDRVL 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
311-484 |
1.21e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATRIGTVFQDpEHQFVTGTVLEE 390
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQ-FYLFPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 391 LQLGPKLV----GVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLT 466
Cdd:PRK09493 98 VMFGPLRVrgasKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170
....*....|....*...
gi 1081004564 467 LLRQLADDGRTVISITHD 484
Cdd:PRK09493 178 VMQDLAEEGMTMVIVTHE 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-267 |
1.30e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.36 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 9 GPSSSGNV----PAVSARGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGKLLI 84
Cdd:PRK14271 8 GQSGAADVdaaaPAMAAVNLTLGFAGK--TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 85 EGRTPASARGA------VGLVLQDPDSQTISarVGDDVAFGAENLGVAP-AEIGNRVRASLDLVGL-----DLPLDHPtH 152
Cdd:PRK14271 86 GGRSIFNYRDVlefrrrVGMLFQRPNPFPMS--IMDNVLAGVRAHKLVPrKEFRGVAQARLTEVGLwdavkDRLSDSP-F 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 153 RLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTgaALIVVEHRVDAWVDVVDRIIVLGRGGV 232
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRL 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1081004564 233 IADGAPHRVLEDYGQALTdaGVWIPGAPPALPDAR 267
Cdd:PRK14271 241 VEEGPTEQLFSSPKHAET--ARYVAGLSGDVKDAK 273
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
312-500 |
1.30e-14 |
|
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: 75.14 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS---GSAPWKWpskkLAT---RIGTVFQDP---EHQf 382
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIF----LPPhrrRIGYVFQEArlfPHL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 vtgTVLEELQLGPKLVGVNADK-RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTF 461
Cdd:COG4148 93 ---SVRGNLLYGRKRAPRAERRiSFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081004564 462 TELLTLLRQLADDGRT-VISITHDPLVVQAMGDYVVDMDA 500
Cdd:COG4148 170 AEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQ 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
35-242 |
1.65e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.46 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIaGVLGDDSDG-------------EATGKLLI-EGRTPASARGAVGLVL 100
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGsivvngqtinlvrDKDGQLKVaDKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 101 QDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLD--LPLDHPTHrLSGGQKQRLALAGVLAMGARVICLD 178
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDerAQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 179 EPTANIDPAGV-PVLRDAAITAAErtGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:PRK10619 178 EPTSALDPELVgEVLRIMQQLAEE--GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-245 |
1.98e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 73.23 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEAT--GKLLIEGRTPASARGAVGLVLQDP---D 104
Cdd:COG4674 22 GFKA--LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDS-GSVLfgGTDLTGLDEHEIARLGIGRKFQKPtvfE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 105 SQTIsarvgddvafgAENLGVA---------------PAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLA 169
Cdd:COG4674 99 ELTV-----------FENLELAlkgdrgvfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 170 MGARVICLDEPTanidpagvpvlrdAAITAAE--RTGA---------ALIVVEHRVDAWVDVVDRIIVLGRGGVIADG-- 236
Cdd:COG4674 168 QDPKLLLLDEPV-------------AGMTDAEteRTAEllkslagkhSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGsl 234
|
250
....*....|...
gi 1081004564 237 ----APHRVLEDY 245
Cdd:COG4674 235 devqADPRVIEVY 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-208 |
2.31e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS------DGEATGKLLIEGRTPASARGAVGLVLQdpdsqt 107
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAgtikldGGDIDDPDVAEACHYLGHRNAMKPALT------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 isarVGDDVAFGAENLGVAPAEIgnrvRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:PRK13539 90 ----VAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|.
gi 1081004564 188 GVPVLRDAAITAAERTGAALI 208
Cdd:PRK13539 162 AVALFAELIRAHLAQGGIVIA 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
35-242 |
2.52e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDsdgeaTGKLLIEGR--TPASARGAVGLVLQDPDSQTISA-- 110
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-----AGTVLVAGDdvEALSARAASRRVASVPQDTSLSFef 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 RVGDDVAFG----AENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:PRK09536 93 DVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 187 AGVPVLRDAAITAAErTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:PRK09536 173 NHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
15-249 |
2.54e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 15 NVPAVSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS--------DGEATGKL-LIE 85
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKG--CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAgevhyrmrDGQLRDLYaLSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 86 GRTPASARGAVGLVLQDPdsqtisaRVG--DDVAFGAeNLGVAPAEIGNR----VRAS----LDLVGLDLPL--DHPThR 153
Cdd:PRK11701 81 AERRRLLRTEWGFVHQHP-------RDGlrMQVSAGG-NIGERLMAVGARhygdIRATagdwLERVEIDAARidDLPT-T 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 154 LSGGQKQRLALAGVLAMGARVICLDEPTANIDpagVPV---LRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD---VSVqarLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250 260
....*....|....*....|...
gi 1081004564 231 GVIADGAPHRVLED----YGQAL 249
Cdd:PRK11701 229 RVVESGLTDQVLDDpqhpYTQLL 251
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
255-483 |
3.13e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 255 WIPGAPPALPDARSvacdqdghpsgDIAIETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKST 334
Cdd:PRK13536 25 GISEAKASIPGSMS-----------TVAIDLAGVSKSYGDK-----------AVVNGLSFTVASGECFGLLGPNGAGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 335 LALTLGGLLEPMAGTVQVAGsgsAPWKWPSKKLATRIGTV--FQDPEHQFvtgTVLEELQLGPKLVGVNAdKRIEE---- 408
Cdd:PRK13536 83 IARMILGMTSPDAGKITVLG---VPVPARARLARARIGVVpqFDNLDLEF---TVRENLLVFGRYFGMST-REIEAvips 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 409 LLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITH 483
Cdd:PRK13536 156 LLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
306-484 |
3.20e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.81 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsaPWKWPSkklATRiGTVFQDpEHQFVTG 385
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPG---AER-GVVFQN-EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPKLVGVNADKRIEELLERLRLTALTKAN---PFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFT 462
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEkryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|...
gi 1081004564 463 ELLTLLRQL-ADDGRTVISITHD 484
Cdd:PRK11248 166 QMQTLLLKLwQETGKQVLLITHD 188
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-263 |
4.21e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 29 AGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVL--GDDSDGEA-TGKLLIEGRtPASARGAVGL-----VL 100
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgGGAPRGARvTGDVTLNGE-PLAAIDAPRLarlraVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 101 QDPDSQTISARVGDDVAFG----AENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAM------ 170
Cdd:PRK13547 89 PQAAQPAFAFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 171 ---GARVICLDEPTANIDPAGVPVLRDA--AITAAERTGAALIVveHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED- 244
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTvrRLARDWNLGVLAIV--HDPNLAARHADRIAMLADGAIVAHGAPADVLTPa 246
|
250 260
....*....|....*....|....*.
gi 1081004564 245 -----YGQA--LTDAGvwiPGAPPAL 263
Cdd:PRK13547 247 hiarcYGFAvrLVDAG---DGVPPVI 269
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
310-507 |
4.41e-14 |
|
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: 71.46 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPsEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsaPWKWPSKKLATRIGTVFQDPEH--QFvtgTV 387
Cdd:cd03264 17 DGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLRRRIGYLPQEFGVypNF---TV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:cd03264 90 REFLDYIAWLKGIPskeVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081004564 465 LTLLRQLADDgRTVISITHDPLVVQAMGDYVVDMDAFHPERSG 507
Cdd:cd03264 170 RNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
36-244 |
4.52e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.91 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgEAT-GKLLIEGRTPASA---------RGAVGLVLQDpDS 105
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI------EPTrGQVLIDGVDIAKIsdaelrevrRKKIAMVFQS-FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 QTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 186 PAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
303-499 |
5.80e-14 |
|
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: 70.03 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 303 ETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwpsKKLATRIGTVFQDPeHQF 382
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE---KALSSLISVLNQRP-YLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 VTgTVLEelqlgpklvgvNADKRieellerlrltaltkanpfsLSGGEKRRLSVA-TMLATAPdIVLLDEPTFGQDRRTF 461
Cdd:cd03247 88 DT-TLRN-----------NLGRR--------------------FSGGERQRLALArILLQDAP-IVLLDEPTVGLDPITE 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081004564 462 TELLTLLRQLADDgRTVISITHDPLVVQAMgDYVVDMD 499
Cdd:cd03247 135 RQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLE 170
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
34-231 |
6.22e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.46 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEATgklliegrTPASARgavGLVL-QDPDSQTISARv 112
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGSGRIA--------RPAGAR---VLFLpQRPYLPLGTLR- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 113 gDDVAFGAENLGVAPAEIgnrvRASLDLVGLDLPLDHP------THRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:COG4178 444 -EALLYPATAEAFSDAEL----REALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 187 AgvpvLRDA--AITAAERTGAALIVVEHRvDAWVDVVDRIIVLGRGG 231
Cdd:COG4178 519 E----NEAAlyQLLREELPGTTVISVGHR-STLAAFHDRVLELTGDG 560
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-483 |
6.33e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsaPWKWPSKKLATRIGTVFQ----DPEHqfvtgTVLEELQLGPKLVG 399
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE---PVPSRARHARQRVGVVPQfdnlDPDF-----TVRENLLVFGRYFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 400 VNA---DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGR 476
Cdd:PRK13537 110 LSAaaaRALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK 189
|
....*..
gi 1081004564 477 TVISITH 483
Cdd:PRK13537 190 TILLTTH 196
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-499 |
6.53e-14 |
|
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: 74.39 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 277 PSGDIAIETRELDIGYGAkkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSG 356
Cdd:TIGR01193 470 LNGDIVINDVSYSYGYGS------------NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 357 SApwKWPSKKLATRIGTVFQDPehQFVTGTVLEELQLGPKlVGVNADK-----RIEEL---LERLRL---TALTKANpFS 425
Cdd:TIGR01193 538 LK--DIDRHTLRQFINYLPQEP--YIFSGSILENLLLGAK-ENVSQDEiwaacEIAEIkddIENMPLgyqTELSEEG-SS 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 426 LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADdgRTVISITHDpLVVQAMGDYVVDMD 499
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHR-LSVAKQSDKIIVLD 682
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-242 |
6.90e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgEATGKLLIEGRTPASARGAVGLVLQDPDSQTISARVGDD 115
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL------PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 116 V----AFGAENlGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAM-------GARVICLDEPTANI 184
Cdd:COG4138 86 VfqylALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 185 DPAGVPVLrDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:COG4138 165 DVAQQAAL-DRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
402-501 |
7.94e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 70.93 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 402 ADKRIEELLERLRL-TALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVIS 480
Cdd:COG4778 128 ARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIG 207
|
90 100
....*....|....*....|.
gi 1081004564 481 ITHDPLVVQAMGDYVVDMDAF 501
Cdd:COG4778 208 IFHDEEVREAVADRVVDVTPF 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
280-501 |
8.07e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.74 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 280 DIAIETRELDIGYGAKKSwfrgsetvepiARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGtVQVAGS---- 355
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLA-----------VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKvtfh 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 356 GS---APWKWPSKkLATRIGTVFQDPeHQFvTGTVLEELQLGPKLVGVNADkrIEELLER-LRLTAL-------TKANPF 424
Cdd:PRK14243 76 GKnlyAPDVDPVE-VRRRIGMVFQKP-NPF-PKSIYDNIAYGARINGYKGD--MDELVERsLRQAALwdevkdkLKQSGL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 425 SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDgRTVISITHDplVVQAmgDYVVDMDAF 501
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHN--MQQA--ARVSDMTAF 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-233 |
1.04e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 20 SARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDdsdgeatgklliegrTPASARGAVgLV 99
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG---------------TPVAGCVDV-PD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 100 LQDPDSQTISARVGDDVAFGAenlgvapaeignrVRASLDLVGL-DLPL-DHPTHRLSGGQKQRLALAGVLAMGARVICL 177
Cdd:COG2401 94 NQFGREASLIDAIGRKGDFKD-------------AVELLNAVGLsDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 178 DEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVV-DRIIVLGRGGVI 233
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
30-186 |
1.08e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.96 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAAvLNDITLDIERGEKVLLLGASGMGKSTLLAAIaGVLGD-DSDGEATGKLLIEGRTPASA-------RGAVGLVLQ 101
Cdd:PRK14239 16 NKKKA-LNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDlNPEVTITGSIVYNGHNIYSPrtdtvdlRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 102 DPDSQTISarVGDDVAFGAENLGVAPAEIGNR-VRASLDLVGL-DLPLDHpTHR----LSGGQKQRLALAGVLAMGARVI 175
Cdd:PRK14239 94 QPNPFPMS--IYENVVYGLRLKGIKDKQVLDEaVEKSLKGASIwDEVKDR-LHDsalgLSGGQQQRVCIARVLATSPKII 170
|
170
....*....|.
gi 1081004564 176 CLDEPTANIDP 186
Cdd:PRK14239 171 LLDEPTSALDP 181
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
35-236 |
1.09e-13 |
|
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: 70.65 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASARGAVGLVLQDPdsQTIS 109
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTS-----GEILLDGVdirdlNLRWLRSQIGLVSQEP--VLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDVAFGAENLGVAPAEIGNRVRASLDLVgLDLPLDHPTH------RLSGGQKQRLALAGVLAMGARVICLDEPTAN 183
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVEEAAKKANIHDFI-MSLPDGYDTLvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 184 IDPAGVPVLRDAAITAAE-RTgaaLIVVEHRVDAwVDVVDRIIVLGRGGVIADG 236
Cdd:cd03249 170 LDAESEKLVQEALDRAMKgRT---TIVIAHRLST-IRNADLIAVLQNGQVVEQG 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
402-499 |
1.86e-13 |
|
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: 70.45 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 402 ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFG---QDRRtftELLTLLRQLADD-GRT 477
Cdd:COG0411 129 ARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGlnpEETE---ELAELIRRLRDErGIT 205
|
90 100
....*....|....*....|..
gi 1081004564 478 VISITHDPLVVQAMGDYVVDMD 499
Cdd:COG0411 206 ILLIEHDMDLVMGLADRIVVLD 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
28-244 |
2.06e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 28 HAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKLLIEGRtpasARGAVGLVLQD 102
Cdd:PRK10895 13 YKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAgniiiDDEDISLLPLHAR----ARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 PdsqTISAR--VGDDVAFGAE-NLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:PRK10895 87 A---SIFRRlsVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 180 PTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED 244
Cdd:PRK10895 164 PFAGVDPISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-216 |
2.21e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.41 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 26 YRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDsdgeatGKLLIEGRTPASA-----RGAVGLVL 100
Cdd:TIGR01271 1227 YTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE------GEIQIDGVSWNSVtlqtwRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 101 QDPDSQTISARVGDD--VAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLD 178
Cdd:TIGR01271 1299 QKVFIFSGTFRKNLDpyEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081004564 179 EPTANIDPAGVPVLRDAAITAAerTGAALIVVEHRVDA 216
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQSF--SNCTVILSEHRVEA 1414
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-254 |
2.41e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.06 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 7 TRGPSSSGNVPAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdGEATGKLLIEG 86
Cdd:TIGR00957 1273 TAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN-----ESAEGEIIIDG 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 87 RTPA-----SARGAVGLVLQDPDSQTISARVGDD--VAFGAENLGVA--PAEIGNRVRASLDlvGLDLPLDHPTHRLSGG 157
Cdd:TIGR00957 1348 LNIAkiglhDLRFKITIIPQDPVLFSGSLRMNLDpfSQYSDEEVWWAleLAHLKTFVSALPD--KLDHECAEGGENLSVG 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 158 QKQRLALAGVLAMGARVICLDEPTANIDpagvpVLRDAAITAAERT---GAALIVVEHRVDAWVDVVdRIIVLGRGGVIA 234
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVD-----LETDNLIQSTIRTqfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAE 1499
|
250 260
....*....|....*....|....
gi 1081004564 235 DGAPHRVLED----YGQAlTDAGV 254
Cdd:TIGR00957 1500 FGAPSNLLQQrgifYSMA-KDAGL 1522
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
277-483 |
2.48e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.07 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 277 PSGDIAIETRELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKStlaltlggllepmagT------- 349
Cdd:COG1117 6 STLEPKIEVRNLNVYYGDKQ-----------ALKDINLDIPENKVTALIGPSGCGKS---------------Tllrclnr 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 350 -------VQVAGS----G---SAPwKWPSKKLATRIGTVFQDPeHQFVTgTVLEELQLGPKLVGVNADKRIEELLER-LR 414
Cdd:COG1117 60 mndlipgARVEGEilldGediYDP-DVDVVELRRRVGMVFQKP-NPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEEsLR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 415 LTAL-------TKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTFTElltLLRQLADDgRTVISITH 483
Cdd:COG1117 137 KAALwdevkdrLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKIEE---LILELKKD-YTIVIVTH 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
34-240 |
2.55e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAaIAGVLGDDSDGE--ATGKLLIEGRTPASA---RGAVGLVLQDPDSQT- 107
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKPTSGTyrVAGQDVATLDADALAqlrREHFGFIFQRYHLLSh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISArvGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP- 186
Cdd:PRK10535 101 LTA--AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSh 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 187 AGVPVLrdAAITAAERTGAALIVVEHrvDAWVDV-VDRIIVLGRGGVIADGAPHR 240
Cdd:PRK10535 179 SGEEVM--AILHQLRDRGHTVIIVTH--DPQVAAqAERVIEIRDGEIVRNPPAQE 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
35-246 |
2.63e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.45 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDsdgeaTGKLLIEGRtPASA------RGAVGLVLQDPdsQTI 108
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT-----GGQVLLDGV-PLVQydhhylHRQVALVGQEP--VLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SARVGDDVAFGaenLGVAP-AEIGNRVRASL--DLV-----GLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:TIGR00958 568 SGSVRENIAYG---LTDTPdEEIMAAAKAANahDFImefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 181 TANIDpAGVPVLRDAAITAAERTgaaLIVVEHRVDAwVDVVDRIIVLGRGGVIADGAPHRVLEDYG 246
Cdd:TIGR00958 645 TSALD-AECEQLLQESRSRASRT---VLLIAHRLST-VERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
310-498 |
2.82e-13 |
|
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: 68.93 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKlatRIGtVFQDPEHQFVTGTVLE 389
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR---RLG-FVSDSTGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVNADK---RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLT 466
Cdd:cd03266 98 NLEYFAGLYGLKGDEltaRLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180 190
....*....|....*....|....*....|..
gi 1081004564 467 LLRQLADDGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:cd03266 178 FIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
310-500 |
2.82e-13 |
|
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: 68.82 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKlatR-IGTVFQD----PeHQfvt 384
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKD---RdIAMVFQNyalyP-HM--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 385 gTVLEELQLGPKLVGV---NADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---- 457
Cdd:cd03301 88 -TVYDNIAFGLKLRKVpkdEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklr 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081004564 458 RRTFTELLTLLRQLaddGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:cd03301 167 VQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-242 |
2.86e-13 |
|
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: 72.16 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYrHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgdDSDGeatGKLLIEGR-----TPASARGAVGL 98
Cdd:COG5265 365 FGY-DPERP--ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY--DVTS---GRILIDGQdirdvTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 VLQDP----DSqtisarVGDDVAFGaeNLGVAPAEIGNRVR-ASLDLVGLDLPLDHPTH------RLSGGQKQRLALAGV 167
Cdd:COG5265 437 VPQDTvlfnDT------IAYNIAYG--RPDASEEEVEAAARaAQIHDFIESLPDGYDTRvgerglKLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 168 LAMGARVICLDEPTANIDPAgvpvlRDAAITAA------ERTgaaLIVVEHR----VDAwvdvvDRIIVLGRGGVIADGA 237
Cdd:COG5265 509 LLKNPPILIFDEATSALDSR-----TERAIQAAlrevarGRT---TLVIAHRlstiVDA-----DEILVLEAGRIVERGT 575
|
....*
gi 1081004564 238 pHRVL 242
Cdd:COG5265 576 -HAEL 579
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
293-484 |
2.94e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 293 GAKKSWFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIG 372
Cdd:COG1101 6 NLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYKRAKYIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 373 TVFQDPehqfVTGT-----VLEELQL--------GPKLvGVNADKR--IEELLERL------RLTALTKanpfSLSGGEK 431
Cdd:COG1101 84 RVFQDP----MMGTapsmtIEENLALayrrgkrrGLRR-GLTKKRRelFRELLATLglglenRLDTKVG----LLSGGQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 432 RRLSV--ATMlaTAPDIVLLDEPTFGQDRRTFTELLTLLRQL-ADDGRTVISITHD 484
Cdd:COG1101 155 QALSLlmATL--TKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHN 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
36-186 |
3.24e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.81 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIaGVLGDDSDG-EATGKLLIEGRT-------PASARGAVGLVLQDPDSqt 107
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCF-NRLNDLIPGfRVEGKVTFHGKNlyapdvdPVEVRRRIGMVFQKPNP-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISARVGDDVAFGAENLG------------VAPAEIGNRVRASLDLVGLDLpldhpthrlSGGQKQRLALAGVLAMGARVI 175
Cdd:PRK14243 103 FPKSIYDNIAYGARINGykgdmdelversLRQAALWDEVKDKLKQSGLSL---------SGGQQQRLCIARAIAVQPEVI 173
|
170
....*....|.
gi 1081004564 176 CLDEPTANIDP 186
Cdd:PRK14243 174 LMDEPCSALDP 184
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
51-244 |
3.39e-13 |
|
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: 70.90 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 51 LLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT----------PASARgAVGLVLQDpdsqtisAR------VGD 114
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDS-----GRIRLGGEVlqdsargiflPPHRR-RIGYVFQE-------ARlfphlsVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 115 DVAFGAENLGVAPAEIG-NRVrasLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAgvpvlR 193
Cdd:COG4148 97 NLLYGRKRAPRAERRISfDEV---VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA-----R 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 194 DAAI-----TAAERTGAALIVVEHRVDawvDVV---DRIIVLGRGGVIADGAPHRVLED 244
Cdd:COG4148 169 KAEIlpyleRLRDELDIPILYVSHSLD---EVArlaDHVVLLEQGRVVASGPLAEVLSR 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
310-498 |
3.86e-13 |
|
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: 70.47 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAgtvQVAGS----GSAPWKWPSKKL----ATRIGTVFQDP--- 378
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG---ITSGEilfdGEDLLKLSEKELrkirGREIQMIFQDPmts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 -------EHQFVtgtvlEELQLGPKLVGVNADKRIEELLERLRLT-ALTKAN--PFSLSGGEKRRLSVATMLATAPDIVL 448
Cdd:COG0444 99 lnpvmtvGDQIA-----EPLRIHGGLSKAEARERAIELLERVGLPdPERRLDryPHELSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 449 LDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-238 |
4.59e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.41 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSARGFGYRHAGRKaaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDS-----DGEATGKL----LIEGRTP 89
Cdd:PRK11831 8 VDMRGVSFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHgeilfDGENIPAMsrsrLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 90 ASARGAVGLVLQDpdsqtisARVGDDVAFG-AENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVL 168
Cdd:PRK11831 86 MSMLFQSGALFTD-------MNVFDNVAYPlREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 169 AMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAP 238
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
307-484 |
4.85e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwpSKKLATRIGTVFQDPEHQF-VTG 385
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS--ARAASRRVASVPQDTSLSFeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPKL----VGVNADKR-IEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:PRK09536 95 RQVVEMGRTPHRsrfdTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180
....*....|....*....|....
gi 1081004564 461 FTELLTLLRQLADDGRTVISITHD 484
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
34-212 |
6.30e-13 |
|
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: 67.90 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASARGAVGLVLQDPDSQTI 108
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA-----GRVLLNGGpldfqRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SARvgddvafgaENLGVAPAEIGN-RVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:cd03231 89 SVL---------ENLRFWHADHSDeQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*
gi 1081004564 188 GVPVLRDAAITAAERTGAALIVVEH 212
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
289-499 |
6.75e-13 |
|
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: 69.06 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 289 DIGYGAKKSWFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLA 368
Cdd:TIGR02769 7 DVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 369 TR-IGTVFQDPEHQF-----VTGTVLEELQLGPKLVGVNADKRIEELLERLRLTA-LTKANPFSLSGGEKRRLSVATMLA 441
Cdd:TIGR02769 87 RRdVQLVFQDSPSAVnprmtVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 442 TAPDIVLLDEPTFGQDRRTFTELLTLLRQL-ADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMD 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
307-483 |
7.11e-13 |
|
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: 68.34 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPehQFVTGT 386
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR--DLNLRWLRSQIGLVSQEP--VLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VLEELQLGpklvgvnADKRIEELLERlrltALTKAN--------P-----------FSLSGGEKRRLSVATMLATAPDIV 447
Cdd:cd03249 93 IAENIRYG-------KPDATDEEVEE----AAKKANihdfimslPdgydtlvgergSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081004564 448 LLDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITH 483
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAH 196
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
307-483 |
8.92e-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: 68.03 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSkkLATRIGTVFQDpehqfvtgT 386
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS--LRRAIGVVPQD--------T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VL------EELQLGpklvGVNA-DKRIEELLERLRLTALTKANPFS-----------LSGGEKRRLSVATMLATAPDIVL 448
Cdd:cd03253 85 VLfndtigYNIRYG----RPDAtDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1081004564 449 LDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITH 483
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVS-KGRTTIVIAH 194
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-484 |
1.07e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 23 GFGYrhagrkAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAG-VLGDDsdgeatGKLLIEGRT---------PASA 92
Cdd:PRK11147 12 SFSD------APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGeVLLDD------GRIIYEQDLivarlqqdpPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAV----------------------GLVLQDPDSQTIS--ARVGDDVafgaENLGVAPAEigNRVRASLDLVGLDLplD 148
Cdd:PRK11147 80 EGTVydfvaegieeqaeylkryhdisHLVETDPSEKNLNelAKLQEQL----DHHNLWQLE--NRINEVLAQLGLDP--D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 149 HPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDpagvpvlrdaaITAAE-------RTGAALIVVEHRVDAWVDVV 221
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-----------IETIEwlegflkTFQGSIIFISHDRSFIRNMA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 222 DRIIVLGRGGVIA---------DGAPH--RVLED----YGQALTDAGVWI-----------PG---APPALPDARSVACD 272
Cdd:PRK11147 221 TRIVDLDRGKLVSypgnydqylLEKEEalRVEELqnaeFDRKLAQEEVWIrqgikarrtrnEGrvrALKALRRERSERRE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 273 ---------QDGHPSGDIAIETRELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLL 343
Cdd:PRK11147 301 vmgtakmqvEEASRSGKIVFEMENVNYQIDGKQ-----------LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 344 EPMAGTVqvagsgsapwkwpskklatRIGTVFQ-----------DPEHqfvtgTVLEELQLGPKLVGVNADKRieELLER 412
Cdd:PRK11147 370 QADSGRI-------------------HCGTKLEvayfdqhraelDPEK-----TVMDNLAEGKQEVMVNGRPR--HVLGY 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 413 LR------LTALT--KAnpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDrrtfTELLTLLRQLADDGR-TVISITH 483
Cdd:PRK11147 424 LQdflfhpKRAMTpvKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQgTVLLVSH 495
|
.
gi 1081004564 484 D 484
Cdd:PRK11147 496 D 496
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-185 |
1.07e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.49 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 32 KAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEatgkLLIEGRT-----PASaRGaVGLVLQD---- 102
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERITSGE----IWIGGRVvnelePAD-RD-IAMVFQNyaly 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 PdsqtiSARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRlalagvLAMGaRVIC------ 176
Cdd:PRK11650 89 P-----HMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR------VAMG-RAIVrepavf 156
|
170
....*....|
gi 1081004564 177 -LDEPTANID 185
Cdd:PRK11650 157 lFDEPLSNLD 166
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
299-498 |
1.10e-12 |
|
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: 66.47 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWpsKKLATRIGTVFQDP 378
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP--NELGDHVGYLPQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 EhqFVTGTVLEELqlgpklvgvnadkrieellerlrltaltkanpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDR 458
Cdd:cd03246 86 E--LFSGSIAENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081004564 459 RTFTELLTLLRQLADDGRTVISITHDPLVVQAMgDYVVDM 498
Cdd:cd03246 130 EGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVL 168
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-187 |
1.16e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.59 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEG--------RTPASARGAVGLVLQ 101
Cdd:PRK10908 14 GRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGhditrlknREVPFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 102 DpDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGL-DLPLDHPThRLSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:PRK10908 87 D-HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLlDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
....*..
gi 1081004564 181 TANIDPA 187
Cdd:PRK10908 165 TGNLDDA 171
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
307-475 |
1.21e-12 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 67.68 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATR-IGTVFQDPEhQFVTG 385
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIT--HLPMHERARLgIGYLPQEAS-IFRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEE----LQLGPKLVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTF 461
Cdd:TIGR04406 92 TVEENimavLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAV 171
|
170
....*....|....
gi 1081004564 462 TELLTLLRQLADDG 475
Cdd:TIGR04406 172 GDIKKIIKHLKERG 185
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-236 |
1.34e-12 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 70.37 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEGRTPAS-----A 92
Cdd:TIGR03797 453 EVDRVTFRYRPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGF-----ETPESGSVFYDGQDLAGldvqaV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAVGLVLQDpdSQTISARVGDDVAfGAENLGVapaeigNRVRASLDLVGL-----DLPLDHPT------HRLSGGQKQR 161
Cdd:TIGR03797 526 RRQLGVVLQN--GRLMSGSIFENIA-GGAPLTL------DEAWEAARMAGLaedirAMPMGMHTviseggGTLSGGQRQR 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 162 LALAGVLAMGARVICLDEPTANIDPagvpvlRDAAITAA--ERTGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADG 236
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDN------RTQAIVSEslERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
38-242 |
1.66e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 38 DITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPA-------SARgaVGLVLQDP-DSQTIS 109
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS-----GELLIDDHPLHfgdysyrSQR--IRMIFQDPsTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDVAFGAE-NLGVAPAEIGNRVRASLDLVGLdLPlDHPT---HRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:PRK15112 104 QRISQILDFPLRlNTDLEPEQREKQIIETLRQVGL-LP-DHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 186 PAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-484 |
1.76e-12 |
|
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: 69.58 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlGDDSDGEAtgkLLIEGRTpasargaVGLVLQDP---DSQTISAR 111
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNGEA---RPQPGIK-------VGYLPQEPqldPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGDDVA---------------FGAEN-----LGVAPAEIGNRVRASlDLVGLDL------------PLDHPTHRLSGGQK 159
Cdd:TIGR03719 89 VEEGVAeikdaldrfneisakYAEPDadfdkLAAEQAELQEIIDAA-DAWDLDSqleiamdalrcpPWDADVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 160 QRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAaitAAERTGAALIVVEHR-----VDAWVDVVDRiivlGRgGVIA 234
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH---LQEYPGTVVAVTHDRyfldnVAGWILELDR----GR-GIPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 235 DGAPHRVLEDYGQAL-----TDAGV---------WI---PGAPPALPDARSVACDQ------------------DGHPSG 279
Cdd:TIGR03719 240 EGNYSSWLEQKQKRLeqeekEESARqktlkreleWVrqsPKGRQAKSKARLARYEEllsqefqkrnetaeiyipPGPRLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 280 DIAIETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsap 359
Cdd:TIGR03719 320 DKVIEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET---- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 360 wkwpskklaTRIGTVFQDPEHQFVTGTVLEE-------LQLGPKLV------------GVNADKRIEEllerlrltaltk 420
Cdd:TIGR03719 385 ---------VKLAYVDQSRDALDPNKTVWEEisggldiIKLGKREIpsrayvgrfnfkGSDQQKKVGQ------------ 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 421 anpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTftelltlLRQLAD-----DGRTVIsITHD 484
Cdd:TIGR03719 444 -----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET-------LRALEEallnfAGCAVV-ISHD 499
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
322-495 |
2.08e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.43 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 322 TCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsapwkwpsKKLATRIGTVFQD----PEHQ--FVTGTVLEELQLGP 395
Cdd:TIGR01257 959 TAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----------KDIETNLDAVRQSlgmcPQHNilFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 396 KLVGVNADK---RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTFTELLTLLR 469
Cdd:TIGR01257 1029 QLKGRSWEEaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpysRRSIWDLLLKYR 1108
|
170 180
....*....|....*....|....*.
gi 1081004564 470 QladdGRTVISITHDPLVVQAMGDYV 495
Cdd:TIGR01257 1109 S----GRTIIMSTHHMDEADLLGDRI 1130
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
283-483 |
2.18e-12 |
|
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: 66.87 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKKswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKW 362
Cdd:cd03254 3 IEFENVNFSYDEKK----------PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR--DI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKLATRIGTVFQDPeHQFvTGTVLEELQLGPKLvgvNADKRIEELLERLRLTALTKANP-----------FSLSGGEK 431
Cdd:cd03254 71 SRKSLRSMIGVVLQDT-FLF-SGTIMENIRLGRPN---ATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGER 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 432 RRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITH 483
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAH 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
370-507 |
2.48e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.19 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 370 RIGTVFQdpeHQ--FVTGTVLEELQLG----PKLVGVNA---DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATML 440
Cdd:PRK10851 75 KVGFVFQ---HYalFRHMTVFDNIAFGltvlPRRERPNAaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 441 ATAPDIVLLDEPtFGQ-DRRTFTELLTLLRQLADDGR-TVISITHDPLVVQAMGDYVVDMDAFHPERSG 507
Cdd:PRK10851 152 AVEPQILLLDEP-FGAlDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
308-485 |
2.66e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKL--ATRIGTVFQdpehQFV-- 383
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrAKHVGFVFQ----SFMli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 -TGTVLEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:PRK10584 101 pTLNALENVELPALLRGESsrqSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*..
gi 1081004564 460 TFTELLTLLRQLADD-GRTVISITHDP 485
Cdd:PRK10584 181 TGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
310-496 |
2.97e-12 |
|
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: 64.76 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwPSKKLATRIGTVFQdpehqfvtgtvle 389
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS-PRDARRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 elqlgpklvgvnadkrieellerlrltaltkanpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLR 469
Cdd:cd03216 83 ------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
170 180
....*....|....*....|....*..
gi 1081004564 470 QLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:cd03216 127 RLRAQGVAVIFISHRLDEVFEIADRVT 153
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
298-483 |
3.06e-12 |
|
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: 65.98 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 298 WFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQD 377
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS--KIGLHDLRSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 378 PehQFVTGTVLEelQLGPKlvGVNADKRIEELLERLRLTALTKANPFSL-----------SGGEKRRLSVATMLATAPDI 446
Cdd:cd03244 87 P--VLFSGTIRS--NLDPF--GEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081004564 447 VLLDEPTFGQDRRTFTELLTLLRQlADDGRTVISITH 483
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAH 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
35-230 |
3.10e-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: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRtpasargaVGLVlqdpdSQT---ISAR 111
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLS-----GSVSVPGS--------IAYV-----SQEpwiQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGDDVAFGAE-NlgvapAEignRVRASLDLVGLDLPLDHPTHR-----------LSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:cd03250 82 IRENILFGKPfD-----EE---RYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 180 PTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRG 230
Cdd:cd03250 154 PLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNG 203
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
310-498 |
3.37e-12 |
|
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: 65.04 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLlepmAGTVQVAGSGSAPWKWPskklatrigTVFQDpEHQFVTGTVLE 389
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNK---------LIFID-QLQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVgvnadkrieellerlrltaltkanpfSLSGGEKRRLSVATMLA--TAPDIVLLDEPTFGQDRRTFTELLTL 467
Cdd:cd03238 78 YLTLGQKLS--------------------------TLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190
....*....|....*....|....*....|.
gi 1081004564 468 LRQLADDGRTVISITHDPLVVQAmGDYVVDM 498
Cdd:cd03238 132 IKGLIDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
6-228 |
3.46e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 6 LTRGPSSSGnvPAVSARGFGYrhAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIE 85
Cdd:PRK13543 1 MIEPLHTAP--PLLAAHALAF--SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVES-----GQIQID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 86 G---RTPASARGAVGLVLQDPDSQTISArvgddvafgAENLGVAPAEIGNRVR----ASLDLVGLDLPLDHPTHRLSGGQ 158
Cdd:PRK13543 72 GktaTRGDRSRFMAYLGHLPGLKADLST---------LENLHFLCGLHGRRAKqmpgSALAIVGLAGYEDTLVRQLSAGQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 159 KQRLALAGVLAMGARVICLDEPTANIDPAGVPVLrDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLG 228
Cdd:PRK13543 143 KKRLALARLWLSPAPLWLLDEPYANLDLEGITLV-NRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-238 |
3.75e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAaIAGVLGDDSDGEA--TGKLLIEGRTPASARGAVGLV 99
Cdd:PRK10575 15 RNVSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGEIllDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 100 LQDPDSQTISAR----VGDDVAFGAenLGVAPAEIGNRVRASLDLVGLDlPLDHP-THRLSGGQKQRLALAGVLAMGARV 174
Cdd:PRK10575 92 QQLPAAEGMTVRelvaIGRYPWHGA--LGRFGAADREKVEEAISLVGLK-PLAHRlVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 175 ICLDEPTANIDPA-GVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAP 238
Cdd:PRK10575 169 LLLDEPTSALDIAhQVDVLALVHRLSQER-GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-498 |
3.77e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddSDGEATGKLLIEGRtPASARGavglvLQDPDSQTIS 109
Cdd:PRK13549 17 GVKA--LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY---PHGTYEGEIIFEGE-ELQASN-----IRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 -----------ARVGDDVAFGAEnlgVAPAEIGN------RVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGA 172
Cdd:PRK13549 86 iihqelalvkeLSVLENIFLGNE---ITPGGIMDydamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 173 RVICLDEPTANIDPAGVPVLRDAaITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED------YG 246
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDI-IRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDdiitmmVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 247 QALTDAgvwIPGAPpalpdarsvacdqdgHPSGDIAIETREL---DIGYGAKKswfrgsetvepIARGVSVSIPSEASTC 323
Cdd:PRK13549 242 RELTAL---YPREP---------------HTIGEVILEVRNLtawDPVNPHIK-----------RVDDVSFSLRRGEILG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTlaltlggllepmagTVQvAGSGSAPWKW---------------PSKKLATRIGTVFQDPEH-------- 380
Cdd:PRK13549 293 IAGLVGAGRTE--------------LVQ-CLFGAYPGRWegeifidgkpvkirnPQQAIAQGIAMVPEDRKRdgivpvmg 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 381 --QFVTGTVLEELQLGPKLVGVNADKRIEELLERLRLTAltkANPF----SLSGGEKRRLSVATMLATAPDIVLLDEPTF 454
Cdd:PRK13549 358 vgKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKT---ASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1081004564 455 GQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
405-485 |
3.96e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 405 RIEELLERLRLT--ALTK----ANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTV 478
Cdd:TIGR00955 140 RVDEVLQALGLRkcANTRigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTI 219
|
....*..
gi 1081004564 479 ISITHDP 485
Cdd:TIGR00955 220 ICTIHQP 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
278-498 |
4.18e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.30 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 278 SGDIAIETRELDIGYGAKKSWFRGSETVEPIArGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGS 357
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKPERLVKALD-GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 358 A-PWKWPSKKLATRIGTVFQDP-----EHQFVtGTVLEE-LQLGPKLvgvNADKRIEELLERLRLTAL----TKANPFSL 426
Cdd:PRK11308 80 LkADPEAQKLLRQKIQIVFQNPygslnPRKKV-GQILEEpLLINTSL---SAAERREKALAMMAKVGLrpehYDRYPHMF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 427 SGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
30-242 |
4.28e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.51 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAAVLNDITLDIERGEKVLLLGASGMGKSTllaaIAGVLGDDSDGEaTGKLLIEGR-----TPASARGAVGLVlqdpd 104
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFYDID-EGEILLDGHdlrdyTLASLRNQVALV----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 105 SQTI---SARVGDDVAFGAENLgVAPAEIGNRVRAS--LDLV-----GLDLPLDHPTHRLSGGQKQRLALAGVLAMGARV 174
Cdd:PRK11176 423 SQNVhlfNDTIANNIAYARTEQ-YSREQIEEAARMAyaMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 175 ICLDEPTANIDPAGvpvlrDAAITAA------ERTgaaLIVVEHRVDAwVDVVDRIIVLGRGGVIADGApHRVL 242
Cdd:PRK11176 502 LILDEATSALDTES-----ERAIQAAldelqkNRT---SLVIAHRLST-IEKADEILVVEDGEIVERGT-HAEL 565
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
387-452 |
4.40e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.82 E-value: 4.40e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 387 VLEELQLGPKlvgvNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEP 452
Cdd:COG1137 102 VLELRKLSKK----EREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
34-232 |
4.99e-12 |
|
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: 66.42 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEATGkLLIEGRTPASARGAVGLVLQDPD--SQTISAR 111
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDG-VSWNSVPLQKWRKAFGVIPQKVFifSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPV 191
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081004564 192 LRDAAITAAerTGAALIVVEHRVDAWVDvVDRIIVLGRGGV 232
Cdd:cd03289 177 IRKTLKQAF--ADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
307-484 |
5.77e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.95 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVfqdPEHQFVTG- 385
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA--DWSPAELARRRAVL---PQHSSLSFp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 -TVLEELQLG--PKLVGVNADKRI-EELLERLRLTALTKANPFSLSGGEKRRLSVATMLA--TAPD----IVLLDEPTFG 455
Cdd:PRK13548 91 fTVEEVVAMGraPHGLSRAEDDALvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlWEPDgpprWLLLDEPTSA 170
|
170 180 190
....*....|....*....|....*....|
gi 1081004564 456 QDRRTFTELLTLLRQLADD-GRTVISITHD 484
Cdd:PRK13548 171 LDLAHQHHVLRLARQLAHErGLAVIVVLHD 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-230 |
6.93e-12 |
|
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: 63.99 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 33 AAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEG-----RTPASARGA-VGLVLQDP--- 103
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAS-----GEITLDGkpvtrRSPRDAIRAgIAYVPEDRkre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 ---DSQTIsarvgddvafgAENLGVApaeignrvrasldlvgldlpldhptHRLSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:cd03215 88 glvLDLSV-----------AENIALS-------------------------SLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081004564 181 TANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
34-257 |
7.40e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.65 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 34 AVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEAT--GKLLIEGRTPA--SARGAVGLVLQDPDSqTIS 109
Cdd:PRK15079 36 AV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIG-LVKATDGEVAwlGKDLLGMKDDEwrAVRSDIQMIFQDPLA-SLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 AR--VGDDVAfgaENLGV-----APAEIGNRVRASLDLVGLdLP--LDHPTHRLSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:PRK15079 113 PRmtIGEIIA---EPLRTyhpklSRQEVKDRVKAMMLKVGL-LPnlINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 181 TANIDPA----GVPVLRDaaitAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED----YGQALTDA 252
Cdd:PRK15079 189 VSALDVSiqaqVVNLLQQ----LQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNplhpYTKALMSA 264
|
....*
gi 1081004564 253 gVWIP 257
Cdd:PRK15079 265 -VPIP 268
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-498 |
7.44e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGrkAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPAS 91
Cdd:PRK15439 10 PLLCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS-----GTLEIGGNpcarlTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 ARgAVG--LVLQDP---DSQTisarVGDDVAFGAENlgvaPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAG 166
Cdd:PRK15439 83 AH-QLGiyLVPQEPllfPNLS----VKENILFGLPK----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 167 VLAMGARVICLDEPTANIDPAGVPVLRdAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED-- 244
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLF-SRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDdi 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 245 --------YGQALTDAGV-W--IPGAPPALPDARSV--ACDQDGHPSGDIAIETRELDI-GY----GAKKSWFrgSETVe 306
Cdd:PRK15439 233 iqaitpaaREKSLSASQKlWleLPGNRRQQAAGAPVltVEDLTGEGFRNISLEVRAGEIlGLagvvGAGRTEL--AETL- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 piargVSVSIPSEASTCIVGHNGSGKSTLALTLggllepmAGTV------QVAGSG-SAPWKWPSKKLATRIGTVFQDPE 379
Cdd:PRK15439 310 -----YGLRPARGGRIMLNGKEINALSTAQRLA-------RGLVylpedrQSSGLYlDAPLAWNVCALTHNRRGFWIKPA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 380 HQfvtGTVLEEL--QLGPKLVGVNADKRieellerlrltaltkanpfSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD 457
Cdd:PRK15439 378 RE---NAVLERYrrALNIKFNHAEQAAR-------------------TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1081004564 458 RRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
324-484 |
8.41e-12 |
|
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: 67.52 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS--GSAPWKWPSKklatRIGTVFQDPeHQFvtgtvlEELqLGPklVGVN 401
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQpvTADNREAYRQ----LFSAVFSDF-HLF------DRL-LGL--DGEA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 402 ADKRIEELLERLRLTALT--KANPFS---LSGGEKRRLSVATMLATAPDIVLLDE------PTFgqdRRTF-TELLTLLR 469
Cdd:COG4615 429 DPARARELLERLELDHKVsvEDGRFSttdLSQGQRKRLALLVALLEDRPILVFDEwaadqdPEF---RRVFyTELLPELK 505
|
170
....*....|....*
gi 1081004564 470 QLaddGRTVISITHD 484
Cdd:COG4615 506 AR---GKTVIAISHD 517
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
310-484 |
9.40e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.84 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG------SGSAPWKWPSKKLatriGTVFQDpEHQFV 383
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklSSAAKAELRNQKL----GFIYQF-HHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 TGTVLEELQLgPKLVG----VNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:PRK11629 101 DFTALENVAM-PLLIGkkkpAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180
....*....|....*....|....*.
gi 1081004564 460 TFTELLTLLRQL-ADDGRTVISITHD 484
Cdd:PRK11629 180 NADSIFQLLGELnRLQGTAFLVVTHD 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
310-484 |
1.05e-11 |
|
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: 64.79 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsapwkwpskKLATRIG----TVFQDpEHQFVTG 385
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-----------KQITEPGpdrmVVFQN-YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPKLVGVNADKR-----IEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSerraiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180
....*....|....*....|....*
gi 1081004564 461 FTELLTLLRQLADDGR-TVISITHD 484
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRvTVLMVTHD 174
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
324-484 |
1.21e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATR-IGTVFQDpEHQFVTGTVLEELQLGPKLVGVNA 402
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRqIGMIFQD-HHLLMDRTVYDNVAIPLIIAGASG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 403 D---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVI 479
Cdd:PRK10908 112 DdirRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVL 191
|
....*
gi 1081004564 480 SITHD 484
Cdd:PRK10908 192 MATHD 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
307-483 |
1.39e-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: 64.49 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLAtRIGTVFQDPEHQ-FVTG 385
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT--KLPMHKRA-RLGIGYLPQEASiFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFT 462
Cdd:cd03218 91 TVEENILAVLEIRGLSKKereEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
170 180 190
....*....|....*....|....*....|.
gi 1081004564 463 ELLTLLRQLADDG----------RTVISITH 483
Cdd:cd03218 171 DIQKIIKILKDRGigvlitdhnvRETLSITD 201
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-267 |
1.74e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTL---LAAIagvlgddsDGEATGKLLIEGR--------TPA 90
Cdd:PRK11308 19 RGLFKPERLVKA--LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMI--------ETPTGGELYYQGQdllkadpeAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 91 SARGAVGLVLQDPDS-----QTISARVGDDVAFgaeNLGVAPAEIGNRVRASLDLVGLDlP--LDHPTHRLSGGQKQRLA 163
Cdd:PRK11308 89 LLRQKIQIVFQNPYGslnprKKVGQILEEPLLI---NTSLSAAERREKALAMMAKVGLR-PehYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 164 LAGVLAMGARVICLDEPTANIDpagVPV----------LRDAAITAAERTGAALIVVEHrvdawvdVVDRIIVLGRGGVI 233
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALD---VSVqaqvlnlmmdLQQELGLSYVFISHDLSVVEH-------IADEVMVMYLGRCV 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 1081004564 234 ADGAPHRVLED----YGQALTDAgvwipgAPPALPDAR 267
Cdd:PRK11308 235 EKGTKEQIFNNprhpYTQALLSA------TPRLNPDDR 266
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
363-500 |
1.78e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 363 PSKKlatRIGTVFQD----PeHQfvtgTVLEELQLGPKLVGVN---ADKRIEELLERLRLTALTKANPFSLSGGEKRRLS 435
Cdd:PRK11000 72 PAER---GVGMVFQSyalyP-HL----SVAENMSFGLKLAGAKkeeINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVA 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 436 VATMLATAPDIVLLDEPTFGQDR----RTFTELLTLLRQLaddGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
287-484 |
1.78e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 287 ELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVagSGSAPWKWPSKK 366
Cdd:PRK10253 12 QLTLGYGKYT-----------VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL--DGEHIQHYASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 367 LATRIGTVFQDPEhqfVTG--TVLEELQLGP---KLVGVNADKRIEELLER-LRLTALT---KANPFSLSGGEKRRLSVA 437
Cdd:PRK10253 79 VARRIGLLAQNAT---TPGdiTVQELVARGRyphQPLFTRWRKEDEEAVTKaMQATGIThlaDQSVDTLSGGQRQRAWIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081004564 438 TMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQL-ADDGRTVISITHD 484
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHD 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-250 |
1.89e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRKAaVLNDITLDIERGEKVLLLGASGMGKST----LLAAIAGVLGDDSDGEATGKLLIEGRTPASARGAVg 97
Cdd:PRK15134 289 KGILKRTVDHNV-VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQV- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 lVLQDPDSqTISARVgDDVAFGAENLGV-----APAEIGNRVRASLDLVGLDLPLDH--PThRLSGGQKQRLALAGVLAM 170
Cdd:PRK15134 367 -VFQDPNS-SLNPRL-NVLQIIEEGLRVhqptlSAAQREQQVIAVMEEVGLDPETRHryPA-EFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 171 GARVICLDEPTANIDPAgvpvlRDAAITA-----AERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDY 245
Cdd:PRK15134 443 KPSLIILDEPTSSLDKT-----VQAQILAllkslQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
....*
gi 1081004564 246 GQALT 250
Cdd:PRK15134 518 QQEYT 522
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
311-498 |
2.18e-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: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATRIGtvfqdpeHQ---FVTGTV 387
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG-------HApgiKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLgpkLVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTL 467
Cdd:cd03231 91 LENLRF---WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180 190
....*....|....*....|....*....|.
gi 1081004564 468 LRQLADDGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:cd03231 168 MAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-246 |
2.30e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.11 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 32 KAAVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAsargavglvlqdPDSQTISAR 111
Cdd:COG4586 35 VEAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTS-----GEVRVLGYVPF------------KRRKEFARR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGddVAFG-----------AENL-------GVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGAR 173
Cdd:COG4586 97 IG--VVFGqrsqlwwdlpaIDSFrllkaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 174 VICLDEPTANIDpagVPV---LRDAAITAAERTGAALIVVEHRVDawvDVV---DRIIVLGRGGVIADGAPHRVLEDYG 246
Cdd:COG4586 175 ILFLDEPTIGLD---VVSkeaIREFLKEYNRERGTTILLTSHDMD---DIEalcDRVIVIDHGRIIYDGSLEELKERFG 247
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
283-483 |
2.51e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKKSwfrgsetvepiARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLE-----PMAGTVQVAGSGS 357
Cdd:PRK14239 6 LQVSDLSVYYNKKKA-----------LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 358 APWKWPSKKLATRIGTVFQDPeHQFVTgTVLEELQLGPKLVGVNADKRIEELLER-LRLTAL-------TKANPFSLSGG 429
Cdd:PRK14239 75 YSPRTDTVDLRKEIGMVFQQP-NPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEKsLKGASIwdevkdrLHDSALGLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 430 EKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDgRTVISITH 483
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTR 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
312-496 |
2.51e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwpSKKLATRIGTVFQD-PEHQFVTgtVLEE 390
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS--SKAFARKVAYLPQQlPAAEGMT--VREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 391 LQLGP-------KLVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTE 463
Cdd:PRK10575 106 VAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190
....*....|....*....|....*....|....
gi 1081004564 464 LLTLLRQLADD-GRTVISITHDPLVVQAMGDYVV 496
Cdd:PRK10575 186 VLALVHRLSQErGLTVIAVLHDINMAARYCDYLV 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
313-499 |
2.91e-11 |
|
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: 62.90 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 313 SVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS--GSAPwkwPSKKlatRIGTVFQDpEHQFVTGTVLEE 390
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvTAAP---PADR---PVSMLFQE-NNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 391 LQLG--PKLVGVNAD-KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTL 467
Cdd:cd03298 91 VGLGlsPGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 468 LRQL-ADDGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:cd03298 171 VLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
313-485 |
3.08e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.24 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 313 SVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGSAPWKWPskklatrIGTVFQdpEHQ-FVTGTVL 388
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAERP-------VSMLFQ--ENNlFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 389 EELQLG--PKLVGVNADK-RIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPtfgqdrrtFT--- 462
Cdd:COG3840 90 QNIGLGlrPGLKLTAEQRaQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP--------FSald 161
|
170 180
....*....|....*....|....*....
gi 1081004564 463 -----ELLTLLRQLADD-GRTVISITHDP 485
Cdd:COG3840 162 palrqEMLDLVDELCRErGLTVLMVTHDP 190
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
36-235 |
3.40e-11 |
|
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: 65.62 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsDGEATGKLLIEG-----RTPASA-RGAVGLVLQDPDSQTIS 109
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY----PGKFEGNVFINGkpvdiRNPAQAiRAGIAMVPEDRKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 AR--VGDDVAFGAEN----LGV--APAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPT 181
Cdd:TIGR02633 352 PIlgVGKNITLSVLKsfcfKMRidAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 182 ANIDpAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIAD 235
Cdd:TIGR02633 432 RGVD-VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-236 |
3.52e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRKAAVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR-----TPASA 92
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS-----GRILIDGTdirtvTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 RGAVGLVLQDPD--SQTISA--RVGDDVAFGAENLGVAPAEignrvrASLDLV-----GLDLPLDHPTHRLSGGQKQRLA 163
Cdd:PRK13657 408 RRNIAVVFQDAGlfNRSIEDniRVGRPDATDEEMRAAAERA------QAHDFIerkpdGYDTVVGERGRQLSGGERQRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 164 LAGVLAMGARVICLDEPTANIDpagvpVLRDAAITAA---ERTGAALIVVEHRVdAWVDVVDRIIVLGRGGVIADG 236
Cdd:PRK13657 482 IARALLKDPPILILDEATSALD-----VETEAKVKAAldeLMKGRTTFIIAHRL-STVRNADRILVFDNGRVVESG 551
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
370-499 |
3.68e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 64.78 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 370 RIGTVFQDP---EHQfvtgTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATA 443
Cdd:COG1118 76 RVGFVFQHYalfPHM----TVAENIAFGLRVRPPSKAeirARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 444 PDIVLLDEPtFGQ-DRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:COG1118 152 PEVLLLDEP-FGAlDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMN 208
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
411-485 |
4.72e-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: 4.72e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 411 ERLRLTALTKAnpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDP 485
Cdd:cd03232 98 EALRFSALLRG----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQP 168
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
307-486 |
4.80e-11 |
|
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: 61.99 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVqvagsgsapwKWPSKKLATrigTVFQDPEHQFVTG- 385
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV----------RWNGTPLAE---QRDEPHENILYLGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 --------TVLEELQLGPKLVGvNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD 457
Cdd:TIGR01189 81 lpglkpelSALENLHFWAAIHG-GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....*....
gi 1081004564 458 RRTFTELLTLLRQLADDGRTVISITHDPL 486
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
310-496 |
4.86e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLAltlggllEPMAGTVQVAGSGSAPWKWPSKKLATR--IGTVFQDPEHQFVTGTV 387
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLF-------KALMGFVRLASGKISILGQPTRQALQKnlVAYVPQSEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEEL-------QLGPKLVGVNADKRI-EELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:PRK15056 97 VEDVvmmgrygHMGWLRRAKKRDRQIvTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081004564 460 TFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:PRK15056 177 TEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-238 |
5.57e-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: 65.81 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 14 GNVPAVSARGFG--YRHAGRKAAVLNDITLdiERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAS 91
Cdd:TIGR01257 924 GLVPGVCVKNLVkiFEPSGRPAVDRLNITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTS-----GTVLVGGKDIET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 ARGAVGLVLQDPDSQTI---SARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVL 168
Cdd:TIGR01257 997 NLDAVRQSLGMCPQHNIlfhHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 169 AMGARVICLDEPTANIDPAGVPVLRDAAITAaeRTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAP 238
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
310-498 |
5.87e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.28 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATR--IGTVFQD----PEHqfv 383
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRkkIAMVFQSfalmPHM--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 384 tgTVLEELQLGPKLVGVNADKRIEELLERLRLTAL---TKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:PRK10070 122 --TVLDNTAFGMELAGINAEERREKALDALRQVGLenyAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 461 FTELLTLLRQL-ADDGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK10070 200 RTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-249 |
6.09e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.59 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 28 HAGrKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlGDDSDGEAT--GKLLIEGRTPASARGAVGLVlqdPDS 105
Cdd:PRK11614 14 HYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVfdGKDITDWQTAKIMREAVAIV---PEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 QTISAR--VGDDVAFGAenLGVAPAEIGNRVRASLDLvgldLP--LDHPTHR---LSGGQKQRLALAGVLAMGARVICLD 178
Cdd:PRK11614 89 RRVFSRmtVEENLAMGG--FFAERDQFQERIKWVYEL----FPrlHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 179 EPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGgviadgapHRVLEDYGQAL 249
Cdd:PRK11614 163 EPSLGLAPIIIQQIFD-TIEQLREQGMTIFLVEQNANQALKLADRGYVLENG--------HVVLEDTGDAL 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-498 |
8.61e-11 |
|
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: 64.65 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 129 EIGNRVRASLDlVGLD-LPLDHPTHRLSGGQKQRLALA--------GVLAMgarvicLDEPTANIDP-------AGVPVL 192
Cdd:TIGR00630 464 EIRERLGFLID-VGLDyLSLSRAAGTLSGGEAQRIRLAtqigsgltGVLYV------LDEPSIGLHQrdnrrliNTLKRL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 193 RDaaitaaerTGAALIVVEHRVDAwVDVVDRIIVLGRGG------VIADGAPHRVLEDyGQALTdaGVWIPGAPP-ALPD 265
Cdd:TIGR00630 537 RD--------LGNTLIVVEHDEDT-IRAADYVIDIGPGAgehggeVVASGTPEEILAN-PDSLT--GQYLSGRKKiEVPA 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 266 ARSVAcdqdghpsgdiaiETRELDIgYGAKKSWFRGsetvepiargVSVSIPSEASTCIVGHNGSGKS---------TLA 336
Cdd:TIGR00630 605 ERRPG-------------NGKFLTL-KGARENNLKN----------ITVSIPLGLFTCITGVSGSGKStlindtlypALA 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 337 LTLGGLLEPMAGTVQVAG----------SGSAPWKWPSKKLATRIGtVFQD--------P-------------------- 378
Cdd:TIGR00630 661 NRLNGAKTVPGRYTSIEGlehldkvihiDQSPIGRTPRSNPATYTG-VFDEirelfaetPeakvrgytpgrfsfnvkggr 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 -EHQFVTGTVLEELQLGPKlVGVNAD----KRI-EELLE----------RLRLTALTKANPF------------------ 424
Cdd:TIGR00630 740 cEACQGDGVIKIEMHFLPD-VYVPCEvckgKRYnRETLEvkykgkniadVLDMTVEEAYEFFeavpsisrklqtlcdvgl 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 425 ----------SLSGGEKRRLSVATML---ATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDpLVVQAM 491
Cdd:TIGR00630 819 gyirlgqpatTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHN-LDVIKT 897
|
....*..
gi 1081004564 492 GDYVVDM 498
Cdd:TIGR00630 898 ADYIIDL 904
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
284-479 |
9.36e-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: 61.92 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 284 ETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGSAPW 360
Cdd:COG0410 5 EVENLHAGYGGI-----------HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGediTGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 361 KwpskkLATR-IGTVfqdPEHQ--FVTGTVLEELQLGPKLVGVNAD--KRIEE-------LLERLRltalTKANpfSLSG 428
Cdd:COG0410 74 R-----IARLgIGYV---PEGRriFPSLTVEENLLLGAYARRDRAEvrADLERvyelfprLKERRR----QRAG--TLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 429 GEKRRLSVATMLATAPDIVLLDEPTFG------QdrrtftELLTLLRQLADDGRTVI 479
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGlaplivE------EIFEIIRRLNREGVTIL 190
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
312-499 |
1.04e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG-----SGSAPWKWPSKKlatRIGTVFQD----PeHQF 382
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKR---RIGYVFQDarlfP-HYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 VTGTvleeLQLGPK------------LVGvnadkrIEELLERLrltaltkanPFSLSGGEKRRLSVATMLATAPDIVLLD 450
Cdd:PRK11144 93 VRGN----LRYGMAksmvaqfdkivaLLG------IEPLLDRY---------PGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 451 EPTFGQD---RRtftELLTLLRQLADDGRT-VISITHDPLVVQAMGDYVVDMD 499
Cdd:PRK11144 154 EPLASLDlprKR---ELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLE 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-226 |
1.21e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIE-----RGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEATGKLLIegrtpasargavglvlqdpdS---QT 107
Cdd:PRK13409 350 LGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDE-GEVDPELKI--------------------SykpQY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISA----RVGDDVAFGAENLGVAP--AEIGNRVrasldlvGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPT 181
Cdd:PRK13409 409 IKPdydgTVEDLLRSITDDLGSSYykSEIIKPL-------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 182 ANIDpagvpVLRDAAIT-----AAERTGAALIVVEHRVdAWVD-VVDRIIV 226
Cdd:PRK13409 482 AHLD-----VEQRLAVAkairrIAEEREATALVVDHDI-YMIDyISDRLMV 526
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
310-500 |
1.44e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 62.78 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKStlaltlggllEPMAGTVQVAG---SGSAPWKwpskklatR-IGTVFQDP---EHQf 382
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKStllrmiagleDPTSGEILIGGrdvTDLPPKD--------RnIAMVFQSYalyPHM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 vtgTVLEELQLGPKLVGVNA---DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRR 459
Cdd:COG3839 91 ---TVYENIAFPLKLRKVPKaeiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081004564 460 ----TFTELLTLLRQLaddGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:COG3839 168 lrveMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMND 209
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-494 |
1.59e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 282 AIETRELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLE-----PMAGTVQVAGSG 356
Cdd:PRK14258 7 AIKVNNLSFYYDTQK-----------ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 357 SAPWKWPSKKLATRIGTVFqdPEHQFVTGTVLEELQLGPKLVGVNADKRIEELLErlrlTALTKAN------------PF 424
Cdd:PRK14258 76 IYERRVNLNRLRRQVSMVH--PKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVE----SALKDADlwdeikhkihksAL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 425 SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGR-TVISITHDPLVVQAMGDY 494
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDF 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
324-484 |
1.62e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.45 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPS-KKLatrIGTVFQDpEHQFvtgtvlEELqLGPKlvGVNA 402
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKL---FSAVFTD-FHLF------DQL-LGPE--GKPA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 403 D-KRIEELLERLRLT-ALTKANPF----SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTF-TELLTLLRQLa 472
Cdd:PRK10522 421 NpALVEKWLERLKMAhKLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfRREFyQVLLPLLQEM- 499
|
170
....*....|..
gi 1081004564 473 ddGRTVISITHD 484
Cdd:PRK10522 500 --GKTIFAISHD 509
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-484 |
1.71e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.04 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 269 VACDQDGHPSG--DI-----AIETRELDIGYGAKKswfrgsetvepIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGG 341
Cdd:PRK14271 1 MACERLGGQSGaaDVdaaapAMAAVNLTLGFAGKT-----------VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 342 LLEPMAG---TVQVAGSGSAPWKWPSK-KLATRIGTVFQDPE-------HQFVTGTVLEELQLGPKLVGVnADKRIEELL 410
Cdd:PRK14271 70 MNDKVSGyrySGDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNpfpmsimDNVLAGVRAHKLVPRKEFRGV-AQARLTEVG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 411 ERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDgRTVISITHD 484
Cdd:PRK14271 149 LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHN 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-233 |
1.88e-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: 60.35 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 27 RHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGddsdgeatGKLLIEGRtpasargavgLVLQDPDSQ 106
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE--------GNVSVEGD----------IHYNGIPYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 TISARVGDDVAF-GAENLGVAPAEIGNRVRASLDLVGldlplDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:cd03233 76 EFAEKYPGEIIYvSEEDVHFPTLTVRETLDFALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 186 PAG----VPVLRdaAITAAERTGAALIVVEHRVDAWvDVVDRIIVLGRGGVI 233
Cdd:cd03233 151 SSTaleiLKCIR--TMADVLKTTTFVSLYQASDEIY-DLFDKVLVLYEGRQI 199
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
324-484 |
2.53e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.01 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTlggllepMAGTVQVAGS----GSAPWKWPSKKLATRIGTVFQDPEHQFVTgTVLEELQLG--PKL 397
Cdd:COG4138 27 LIGPNGAGKSTLLAR-------MAGLLPGQGEillnGRPLSDWSAAELARHRAYLSQQQSPPFAM-PVFQYLALHqpAGA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 398 VGVNADKRIEELLERLRLTA-LTKanPFS-LSGGEKRRLS-VATMLATAPDI------VLLDEPTFGQDRRTFTELLTLL 468
Cdd:COG4138 99 SSEAVEQLLAQLAEALGLEDkLSR--PLTqLSGGEWQRVRlAAVLLQVWPTInpegqlLLLDEPMNSLDVAQQAALDRLL 176
|
170
....*....|....*.
gi 1081004564 469 RQLADDGRTVISITHD 484
Cdd:COG4138 177 RELCQQGITVVMSSHD 192
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
35-232 |
3.58e-10 |
|
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: 60.18 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLlAAIAGVLGDDSDGEatgkLLIEGRtPASA------RGAVGLVLQDPdsqTI 108
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTV-VALLENFYQPQGGQ----VLLDGK-PISQyehkylHSKVSLVGQEP---VL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SAR-VGDDVAFGaenLGVAPAEignRVRASLDLV-----------GLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVIC 176
Cdd:cd03248 100 FARsLQDNIAYG---LQSCSFE---CVKEAAQKAhahsfiselasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 177 LDEPTANIDPAGVPVLRDAAITAAERTgaALIVVEHRVDAwVDVVDRIIVLGRGGV 232
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLST-VERADQILVLDGGRI 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-226 |
4.96e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIE-----RGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEATGKLLIEGRtP----ASARGAVGLVLqdpdSQ 106
Cdd:COG1245 351 YGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDE-GEVDEDLKISYK-PqyisPDYDGTVEEFL----RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 TISARVGDDVAFgaenlgvapAEIGNRVrasldlvGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDp 186
Cdd:COG1245 425 ANTDDFGSSYYK---------TEIIKPL-------GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD- 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081004564 187 agvpV-LRDAAITA----AERTGAALIVVEHRVdAWVD-VVDRIIV 226
Cdd:COG1245 488 ----VeQRLAVAKAirrfAENRGKTAMVVDHDI-YLIDyISDRLMV 528
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
306-486 |
5.34e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.12 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSkkLATRIGTvfQDPEHQFVtg 385
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--ACHYLGH--RNAMKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPKLVGvNADKRIEELLERLRLTALTKAnPF-SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:PRK13539 89 TVAENLEFWAAFLG-GEELDIAAALEAVGLAPLAHL-PFgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|..
gi 1081004564 465 LTLLRQLADDGRTVISITHDPL 486
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATHIPL 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-249 |
6.47e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAS-----ARGAVGLVLQDPDSQTIS 109
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEK-----GRIMIDDCDVAKfgltdLRRVLSIIPQSPVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDvAFGAEN-----LGVAPAEIGNRVRASLdlVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANI 184
Cdd:PLN03232 1326 VRFNID-PFSEHNdadlwEALERAHIKDVIDRNP--FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 185 DpagvpVLRDAAITAAER---TGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHRVLEDYGQAL 249
Cdd:PLN03232 1403 D-----VRTDSLIQRTIReefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
403-499 |
7.15e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 403 DKRIEELLERLRLTALTKANpfSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRqlaDDGRTVISIT 482
Cdd:PRK11147 136 ENRINEVLAQLGLDPDAALS--SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK---TFQGSIIFIS 210
|
90
....*....|....*..
gi 1081004564 483 HDPLVVQAMGDYVVDMD 499
Cdd:PRK11147 211 HDRSFIRNMATRIVDLD 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
370-503 |
8.06e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 58.65 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 370 RIGTVFQDPeHQFVTGTVLEELQLG--PKLVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIV 447
Cdd:COG4136 77 RIGILFQDD-LLFPHLSVGENLAFAlpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 448 LLDEPtfgqdrrtFTELLTLLR---------QLADDGRTVISITHDPLVVQAMGDyVVDMDAFHP 503
Cdd:COG4136 156 LLDEP--------FSKLDAALRaqfrefvfeQIRQRGIPALLVTHDEEDAPAAGR-VLDLGNWQH 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
35-243 |
8.41e-10 |
|
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: 58.69 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvlgdDSDGEAT-GKLLIEGR--TPAS----ARGAVGLVLQDPdsqt 107
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEVTeGEILFKGEdiTDLPpeerARLGIFLAFQYP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 isarvgddvafgAENLGVApaeIGNRVRaSLDlVGldlpldhpthrLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:cd03217 87 ------------PEIPGVK---NADFLR-YVN-EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 188 GVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:cd03217 139 ALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
300-500 |
1.01e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.32 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 300 RGSETVepiARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATR-IGTVFQDP 378
Cdd:PRK10419 22 HQHQTV---LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRdIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 ----EHQFVTGTVLEElqlgP--KLVGVNADKRIEELLERLRLTALTKAN----PFSLSGGEKRRLSVATMLATAPDIVL 448
Cdd:PRK10419 99 isavNPRKTVREIIRE----PlrHLLSLDKAERLARASEMLRAVDLDDSVldkrPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 449 LDEPTFGQDRRTFTELLTLLRQLADDGRTV-ISITHDPLVVQAMGDYVVDMDA 500
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDN 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
404-483 |
1.10e-09 |
|
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: 58.94 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 404 KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDG-RTVISIT 482
Cdd:COG1119 121 ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVT 200
|
.
gi 1081004564 483 H 483
Cdd:COG1119 201 H 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-242 |
1.21e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.88 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 18 AVSARGFGYRHAGRkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgDDSDGEAT------GKLLIEgrtpaS 91
Cdd:PRK10789 315 DVNIRQFTYPQTDH--PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF-DVSEGDIRfhdiplTKLQLD-----S 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 ARGAVGLVLQDPdsQTISARVGDDVAFGAENlgVAPAEIGNRVR-ASLDLVGLDLPLDHPTH------RLSGGQKQRLAL 164
Cdd:PRK10789 387 WRSRLAVVSQTP--FLFSDTVANNIALGRPD--ATQQEIEHVARlASVHDDILRLPQGYDTEvgergvMLSGGQKQRISI 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 165 AGVLAMGARVICLDEPTANID-PAGVPVLRDAAITAAERTgaaLIVVEHRVDAWVDvVDRIIVLGRGGVIADGaPHRVL 242
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDgRTEHQILHNLRQWGEGRT---VIISAHRLSALTE-ASEILVMQHGHIAQRG-NHDQL 536
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
324-500 |
1.27e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLlepMAGTVQVAGS----GSAPWKWPSKKL----ATRIGTVFQDP-----EHQFVTGTVLEE 390
Cdd:PRK09473 47 IVGESGSGKSQTAFALMGL---LAANGRIGGSatfnGREILNLPEKELnklrAEQISMIFQDPmtslnPYMRVGEQLMEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 391 LQLGPKLVGVNAdkrIEELLERLRLTALTKAN------PFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:PRK09473 124 LMLHKGMSKAEA---FEESVRMLDAVKMPEARkrmkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 200
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081004564 465 LTLLRQLADDGRT-VISITHDPLVVQAMGDYVVDMDA 500
Cdd:PRK09473 201 MTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYA 237
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
355-483 |
1.31e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 355 SGSAPWK---WPSKKLATR--IGT----------VFQDPEHQFVTGTVLEelqlgpkLVGVNADKRIEELLERLRLTALT 419
Cdd:NF000106 66 AGRRPWRf*tWCANRRALRrtIG*hrpvr*grreSFSGRENLYMIGR*LD-------LSRKDARARADELLERFSLTEAA 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 420 KANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITH 483
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
403-513 |
1.32e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 403 DKRIEELLERLRLTALTKA----NPFS--LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGr 476
Cdd:COG4178 457 DAELREALEAVGLGHLAERldeeADWDqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT- 535
|
90 100 110
....*....|....*....|....*....|....*..
gi 1081004564 477 TVISITHDPlVVQAMGDYVVDMDAFHPERSGRAAPGQ 513
Cdd:COG4178 536 TVISVGHRS-TLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-213 |
1.42e-09 |
|
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: 57.16 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGV--LGddsdgeaTGKLLIegrtPAsaRGAVGLVLQDPdsqtisarv 112
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpWG-------SGRIGM----PE--GEDLLFLPQRP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 113 gddvAFGAENLgvapAEIgnrvrasldlvgLDLPLDHpthRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAgvpvL 192
Cdd:cd03223 74 ----YLPLGTL----REQ------------LIYPWDD---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE----S 126
|
170 180
....*....|....*....|.
gi 1081004564 193 RDAAITAAERTGAALIVVEHR 213
Cdd:cd03223 127 EDRLYQLLKELGITVISVGHR 147
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
38-252 |
1.66e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 38 DITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEAtGKLLIEGR--TPASARG-AVGLVLQDPDS-----QTIS 109
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTA-GRVLLDGKpvAPCALRGrKIATIMQNPRSafnplHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDVAfgaeNLGVAPAEigNRVRASLDLVGLDLP---LDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP 186
Cdd:PRK10418 100 THARETCL----ALGKPADD--ATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 187 AGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLEDYGQALTDA 252
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRS 239
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
35-242 |
1.87e-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: 58.38 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgDDSDGeatgKLLIEG----RTP-ASARGAVGLVLQDPDSQTIS 109
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV-DIFDG----KIVIDGidisKLPlHTLRSRLSIILQDPILFSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVG--------DDVAFGAENLgvapAEIGNRVRASLDlvGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPT 181
Cdd:cd03288 111 IRFNldpeckctDDRLWEALEI----AQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 182 ANIDPAGVPVLRDAAITA-AERTgaaLIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHRVL 242
Cdd:cd03288 185 ASIDMATENILQKVVMTAfADRT---VVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
35-238 |
1.92e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.56 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAA---IAGVLGddsdgeatGKLLIEGRTPAS-----ARGAVGLVLQDPDSQ 106
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTfmrMVEVCG--------GEIRVNGREIGAyglreLRRQFSMIPQDPVLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 TISARVGDDvAFgaenLGVAPAEignrVRASLDLVGL-----------DLPLDHPTHRLSGGQKQRLALA-GVLAMGARV 174
Cdd:PTZ00243 1397 DGTVRQNVD-PF----LEASSAE----VWAALELVGLrervasesegiDSRVLEGGSNYSVGQRQLMCMArALLKKGSGF 1467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 175 ICLDEPTANIDPAgvpvlRDAAITAAERTGAA---LIVVEHRVDAwVDVVDRIIVLGRGGVIADGAP 238
Cdd:PTZ00243 1468 ILMDEATANIDPA-----LDRQIQATVMSAFSaytVITIAHRLHT-VAQYDKIIVMDHGAVAEMGSP 1528
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-234 |
2.16e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEkVL----LLGAsgmGKSTLLAAIAGVLGDDSdgeatGKLLIEG-----RTPASA-----------RG 94
Cdd:COG1129 267 VVRDVSFSVRAGE-ILgiagLVGA---GRTELARALFGADPADS-----GEIRLDGkpvriRSPRDAiragiayvpedRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 95 AVGLVLQDPDSQTISARVGDDVAfgaeNLGV----APAEIGNRVRASLDLVGLDLplDHPTHRLSGGQKQRLALAGVLAM 170
Cdd:COG1129 338 GEGLVLDLSIRENITLASLDRLS----RGGLldrrRERALAEEYIKRLRIKTPSP--EQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 171 GARVICLDEPTANIDpagvpV---------LRDAAitaaeRTGAALIVV-----EhrvdawvdVV---DRIIVLGRGGVI 233
Cdd:COG1129 412 DPKVLILDEPTRGID-----VgakaeiyrlIRELA-----AEGKAVIVIsselpE--------LLglsDRILVMREGRIV 473
|
.
gi 1081004564 234 A 234
Cdd:COG1129 474 G 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
266-483 |
2.54e-09 |
|
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: 60.41 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 266 ARSVACDQDGhpsgDIAiETRELDIGYGAKKSWFRGSE-------TVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALT 338
Cdd:TIGR01257 1910 AKEPIFDEDD----DVA-EERQRIISGGNKTDILRLNEltkvysgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKM 1984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 339 LGGLLEPMAGTVQVAGsgsapwkwpsKKLATRIGTVFQ--------DPEHQFVTGTvlEELQLGPKLVGVNAdKRIEEL- 409
Cdd:TIGR01257 1985 LTGDTTVTSGDATVAG----------KSILTNISDVHQnmgycpqfDAIDDLLTGR--EHLYLYARLRGVPA-EEIEKVa 2051
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 410 ---LERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITH 483
Cdd:TIGR01257 2052 nwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
306-483 |
2.61e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 59.79 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKStlaltlggllEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPeHQFvTG 385
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKStlvnlllrfyDPTSGRILIDGVDIR--DLTLESLRRQIGVVPQDT-FLF-SG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPKlvgvNA-DKRIEELLERLRLTALTKANPF-----------SLSGGEKRRLSVATMLATAPDIVLLDEPT 453
Cdd:COG1132 429 TIRENIRYGRP----DAtDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190
....*....|....*....|....*....|
gi 1081004564 454 FGQDRRTFTELLTLLRQLAdDGRTVISITH 483
Cdd:COG1132 505 SALDTETEALIQEALERLM-KGRTTIVIAH 533
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-243 |
2.68e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 27 RHAGRKAaVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGEatGKLLIEGRtPASA---RGAVGLVLQDp 103
Cdd:TIGR00955 33 RERPRKH-LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGS--GSVLLNGM-PIDAkemRAISAYVQQD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DSQTISARVGDDVAFGAE-NLG--VAPAEIGNRVRASLDLVGL--------DLPLDHPThrLSGGQKQRLALAGVLAMGA 172
Cdd:TIGR00955 108 DLFIPTLTVREHLMFQAHlRMPrrVTKKEKRERVDEVLQALGLrkcantriGVPGRVKG--LSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 173 RVICLDEPTANIDPAG----VPVLRDAAitaaeRTGAALIVVEHRVDAWV-DVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMaysvVQVLKGLA-----QKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-185 |
2.95e-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: 57.34 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 25 GYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAG----VLGDDSDGEATGKLLIEGRTPASARGAVGLVL 100
Cdd:cd03290 6 GYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtLEGKVHWSNKNESEPSFEATRSRNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 101 QDPdsQTISARVGDDVAFGAenlgvaPAEiGNRVRASLDLVGLD-----LPLDHPTH------RLSGGQKQRLALAGVLA 169
Cdd:cd03290 86 QKP--WLLNATVEENITFGS------PFN-KQRYKAVTDACSLQpdidlLPFGDQTEigergiNLSGGQRQRICVARALY 156
|
170
....*....|....*.
gi 1081004564 170 MGARVICLDEPTANID 185
Cdd:cd03290 157 QNTNIVFLDDPFSALD 172
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
24-212 |
3.16e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.82 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYRhagrkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLliegRTPASARgaVGLVLQ-- 101
Cdd:PRK09544 14 FGQR------RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE-----GVI----KRNGKLR--IGYVPQkl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 102 --DPdsqTISARVGddvAFGAENLGVAPAEIGnrvrASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDE 179
Cdd:PRK09544 77 ylDT---TLPLTVN---RFLRLRPGTKKEDIL----PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 180 PTANIDPAGVPVLRDAAITAAERTGAALIVVEH 212
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
297-498 |
4.17e-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: 56.96 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 297 SWFRGSETVEPIargvSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSKKLATRIGTVFQ 376
Cdd:cd03290 9 SWGSGLATLSNI----NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 377 DPEHQFVTGTVLEELQLGPKLvgvnADKRIEELLERLRLTALTKANPF-----------SLSGGEKRRLSVATMLATAPD 445
Cdd:cd03290 85 AQKPWLLNATVEENITFGSPF----NKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 446 IVLLDEPTFGQDRRTFTELLT--LLRQLADDGRTVISITHDpLVVQAMGDYVVDM 498
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK-LQYLPHADWIIAM 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-250 |
4.74e-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: 57.03 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIE-----RGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTpasargavglVLQDPdsQTISA 110
Cdd:cd03237 10 LGEFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDE-----GDIEIELDT----------VSYKP--QYIKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 111 ----RVGDDVAFGAENLGVAP---AEIgnrvrasLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTAN 183
Cdd:cd03237 73 dyegTVRDLLSSITKDFYTHPyfkTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 184 IDPAGvpvlRDAAITA----AERTGAALIVVEHRVDAWVDVVDRIIVLgrggviaDGAPHRvledYGQALT 250
Cdd:cd03237 146 LDVEQ----RLMASKVirrfAENNEKTAFVVEHDIIMIDYLADRLIVF-------EGEPSV----NGVANP 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
324-498 |
4.85e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGsapWKWPSKKLATR--IGTVFQdpEHQFVTG-TVLEELQLG----PK 396
Cdd:PRK09700 36 LLGENGAGKSTLMKVLSGIHEPTKGTITINNIN---YNKLDHKLAAQlgIGIIYQ--ELSVIDElTVLENLYIGrhltKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 397 LVGVNA------DKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQ 470
Cdd:PRK09700 111 VCGVNIidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQ 190
|
170 180
....*....|....*....|....*...
gi 1081004564 471 LADDGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK09700 191 LRKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
307-483 |
5.59e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.97 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGsgsAPW-KWPSKKLATRIGTVFQDPehQFVTG 385
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG---VPLvQYDHHYLHRQVALVGQEP--VLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGPK----------LVGVNADKRIEELLERLRLTALTKANpfSLSGGEKRRLSVATMLATAPDIVLLDEPTFG 455
Cdd:TIGR00958 570 SVRENIAYGLTdtpdeeimaaAKAANAHDFIMEFPNGYDTEVGEKGS--QLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180
....*....|....*....|....*...
gi 1081004564 456 QDRRTfTELLTLLRQLADdgRTVISITH 483
Cdd:TIGR00958 648 LDAEC-EQLLQESRSRAS--RTVLLIAH 672
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-252 |
5.79e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 24 FGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgdDSDGEATG-KLLIEGR-----TPASARGAVG 97
Cdd:PRK11022 13 FGDESAPFRA--VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI--DYPGRVMAeKLEFNGQdlqriSEKERRNLVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 ----LVLQDP-DSQTISARVGDDVAfgaENLGVAPAeiGN----RVRAS--LDLVGLDLP---LDHPTHRLSGGQKQRLA 163
Cdd:PRK11022 89 aevaMIFQDPmTSLNPCYTVGFQIM---EAIKVHQG--GNkktrRQRAIdlLNQVGIPDPasrLDVYPHQLSGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 164 LAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLE 243
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
250
....*....|...
gi 1081004564 244 D----YGQALTDA 252
Cdd:PRK11022 244 AprhpYTQALLRA 256
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
426-484 |
6.01e-09 |
|
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: 54.76 E-value: 6.01e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 426 LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTfteLLTLLRQLADDGRTVISITHD 484
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHD 126
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-499 |
6.02e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.92 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG---SGSAPWKWPskklatrIGTVFQDpEHQFVTGTVL 388
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlSHVPPYQRP-------INMMFQS-YALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 389 EELQLG---PKLVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDR----RTF 461
Cdd:PRK11607 110 QNIAFGlkqDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQ 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081004564 462 TELLTLLRQLaddGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:PRK11607 190 LEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-485 |
6.21e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTlggllepMAGTVQ---VAGSGSAPWKWPSKKLATRIGTVFQDP---EHQFVTGTVL--EELQLGP 395
Cdd:PLN03211 99 VLGPSGSGKSTLLNA-------LAGRIQgnnFTGTILANNRKPTKQILKRTGFVTQDDilyPHLTVRETLVfcSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 396 KLVGVNADKRIEELLERLRLTALTK---ANPF--SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQ 470
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCENtiiGNSFirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170
....*....|....*
gi 1081004564 471 LADDGRTVISITHDP 485
Cdd:PLN03211 252 LAQKGKTIVTSMHQP 266
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-250 |
6.24e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPAS-----ARGAVGLVLQDPDSQTIS 109
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELER-----GRILIDGCDISKfglmdLRKVLGIIPQAPVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDvAFGAENlgvaPAEIGNRV-RASL-DLV-----GLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:PLN03130 1329 VRFNLD-PFNEHN----DADLWESLeRAHLkDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 183 NIDpagvpVLRDAAITAAER---TGAALIVVEHRVDAWVDvVDRIIVLGRGGVIADGAPHRVLEDYGQALT 250
Cdd:PLN03130 1404 AVD-----VRTDALIQKTIReefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-244 |
6.30e-09 |
|
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: 58.80 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 4 EALTRGPSSSGNVPAVSARGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgDDSDGEATGKll 83
Cdd:TIGR00957 622 DSIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM-DKVEGHVHMK-- 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 84 iegrtpasarGAVGLVLQDPDSQTISARvgDDVAFGAEnlgVAPAEIGNRVRASLDLVGLD-LPLDHPTH------RLSG 156
Cdd:TIGR00957 699 ----------GSVAYVPQQAWIQNDSLR--ENILFGKA---LNEKYYQQVLEACALLPDLEiLPSGDRTEigekgvNLSG 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 157 GQKQRLALAGVLAMGARVICLDEPTANIDP-AGVPVLRDAAITAAERTGAALIVVEHRVdAWVDVVDRIIVLGrGGVIAD 235
Cdd:TIGR00957 764 GQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMS-GGKISE 841
|
....*....
gi 1081004564 236 GAPHRVLED 244
Cdd:TIGR00957 842 MGSYQELLQ 850
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
36-230 |
6.54e-09 |
|
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: 56.50 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLL-----------------AAIAGVLGDDSDGEATgklLIEGRTPA-------- 90
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsAYARQFLGQMDKPDVD---SIEGLSPAiaidqktt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 91 --SARGAVGLVLQDPDS-QTISARVGddvafgaenlgvapaeIGNRVRASLDlVGLD-LPLDHPTHRLSGGQKQRLALAG 166
Cdd:cd03270 88 srNPRSTVGTVTEIYDYlRLLFARVG----------------IRERLGFLVD-VGLGyLTLSRSAPTLSGGEAQRIRLAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 167 VLAMGARVIC--LDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRG 230
Cdd:cd03270 151 QIGSGLTGVLyvLDEPSIGLHPRDNDRLIE-TLKRLRDLGNTVLVVEHDEDT-IRAADHVIDIGPG 214
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
425-498 |
7.38e-09 |
|
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: 56.11 E-value: 7.38e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081004564 425 SLSGGEKRRLSVATMLATAPDIVL--LDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAmGDYVVDM 498
Cdd:cd03270 137 TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDI 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
307-491 |
7.55e-09 |
|
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: 58.22 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVagSGSAPWKWPSKKLATRIGTVFQDPEhqFVTGT 386
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL--DGADLSQWDREELGRHIGYLPQDVE--LFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 V------LEElqlgpklvgVNADKRIE--------ELLERLRL---TALTkANPFSLSGGEKRRLSVATMLATAPDIVLL 449
Cdd:COG4618 422 IaeniarFGD---------ADPEKVVAaaklagvhEMILRLPDgydTRIG-EGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081004564 450 DEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAM 491
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV 533
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
388-498 |
8.06e-09 |
|
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: 58.49 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKLVGVnADKRIEELLERLR------LTALTKANPF-SLSGGEKRRLSVATMLATAPDIVL--LDEPTFGQDR 458
Cdd:TIGR00630 445 FNQLTLTPEEKKI-AEEVLKEIRERLGflidvgLDYLSLSRAAgTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQ 523
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1081004564 459 RTFTELLTLLRQLADDGRTVISITHDPlvvQAM--GDYVVDM 498
Cdd:TIGR00630 524 RDNRRLINTLKRLRDLGNTLIVVEHDE---DTIraADYVIDI 562
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-236 |
8.37e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 6 LTRGPSSSGNVPAVSARGfGYRHAGRKAA--VLNDITLDIERGEKVLLLGASGMGKSTLLAAIagvLGDDSDGEATGKLL 83
Cdd:PLN03232 602 LAQNPPLQPGAPAISIKN-GYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM---LGELSHAETSSVVI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 84 iegrtpasaRGAVGLVLQDPdsQTISARVGDDVAFGAEnlgVAPAEIGNRVRAS-----LDLV-GLDLP-LDHPTHRLSG 156
Cdd:PLN03232 678 ---------RGSVAYVPQVS--WIFNATVRENILFGSD---FESERYWRAIDVTalqhdLDLLpGRDLTeIGERGVNISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 157 GQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITaAERTGAALIVVEHRVDaWVDVVDRIIVLGRGGVIADG 236
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLH-FLPLMDRIILVSEGMIKEEG 821
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-483 |
1.06e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 323 CIVGHNGSGKStlaltlggllEPMAGTVQVAGsgsAPWKWPSKKLATR--IGTVFQDPE--HQFvtgTVLEELQLG---P 395
Cdd:COG3845 35 ALLGENGAGKStlmkilyglyQPDSGEILIDG---KPVRIRSPRDAIAlgIGMVHQHFMlvPNL---TVAENIVLGlepT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 396 KLVGVN---ADKRIEELLERLRLtaltKANPF----SLSGGEKRRLSVATMLATAPDIVLLDEPTFG---QDRRtftELL 465
Cdd:COG3845 109 KGGRLDrkaARARIRELSERYGL----DVDPDakveDLSVGEQQRVEILKALYRGARILILDEPTAVltpQEAD---ELF 181
|
170
....*....|....*...
gi 1081004564 466 TLLRQLADDGRTVISITH 483
Cdd:COG3845 182 EILRRLAAEGKSIIFITH 199
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
36-238 |
1.14e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.08 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLL-----AAIAGVL---------GDDSDG-EATGKLL-IE----GRT----PAS 91
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLhlkkeqpgnHDRIEGlEHIDKVIvIDqspiGRTprsnPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 92 ARGAVGLVLQ---------DPDSQTISARVG----DDV----AFGAENLGVAPAEIGNRVRASLDlVGLD-LPLDHPTHR 153
Cdd:cd03271 91 YTGVFDEIRElfcevckgkRYNRETLEVRYKgksiADVldmtVEEALEFFENIPKIARKLQTLCD-VGLGyIKLGQPATT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 154 LSGGQKQRLALAGVLAMGAR---VICLDEPTANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAwVDVVDRIIVLG-- 228
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDV-IKCADWIIDLGpe 247
|
250
....*....|....
gi 1081004564 229 ---RGG-VIADGAP 238
Cdd:cd03271 248 ggdGGGqVVASGTP 261
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
35-213 |
1.17e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGA-------VGLVLQDPDSQT 107
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK-----GEILFERQSIKKDLCTyqkqlcfVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 108 ISARVGDDVAFGAENLGvapaeIGNRVRasldLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPA 187
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-----ITELCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*.
gi 1081004564 188 GVPVLRdAAITAAERTGAALIVVEHR 213
Cdd:PRK13540 162 SLLTII-TKIQEHRAKGGAVLLTSHQ 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-185 |
1.27e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 1 MTDE-ALTRGPSSSGNVPAVSARGfGYRHAGRKA--AVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSDGE 77
Cdd:PLN03130 596 LAEErVLLPNPPLEPGLPAISIKN-GYFSWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAS 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 78 ATgklliegrtpasARGAVGLVLQdpDSQTISARVGDDVAFGAEnlgVAPAeignRVRASLDLVGLDLPLDH-PTHRL-- 154
Cdd:PLN03130 675 VV------------IRGTVAYVPQ--VSWIFNATVRDNILFGSP---FDPE----RYERAIDVTALQHDLDLlPGGDLte 733
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 155 --------SGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:PLN03130 734 igergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
299-484 |
1.41e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.67 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEpiarGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATR-IGTVFQD 377
Cdd:PRK10895 13 YKGRRVVE----DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIS--LLPLHARARRgIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 378 P---EHQFVTGTVLEELQLGPKLVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTF 454
Cdd:PRK10895 87 AsifRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190
....*....|....*....|....*....|
gi 1081004564 455 GQDRRTFTELLTLLRQLADDGRTVISITHD 484
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
313-481 |
1.45e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 313 SVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQvaGSGSAPWKWPSKKLATRIGTVFQDPEHQFV------TG- 385
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ--SQFSHITRLSFEQLQKLVSDEWQRNNTDMLspgeddTGr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLGpklvgVNADKRIEELLERLRLTALTkANPFS-LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTEL 464
Cdd:PRK10938 101 TTAEIIQDE-----VKDPARCEQLAQQFGITALL-DRRFKyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170
....*....|....*..
gi 1081004564 465 LTLLRQLADDGRTVISI 481
Cdd:PRK10938 175 AELLASLHQSGITLVLV 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
426-489 |
1.48e-08 |
|
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: 54.08 E-value: 1.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 426 LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDrrtFTELLTLLRQLADDGRTVISITHDPLVVQ 489
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALD---EESEDRLYQLLKELGITVISVGHRPSLWK 152
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
324-495 |
1.87e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.45 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS---------GSAPWKWPSKKLATRIgTVFQDPEH-----QFVTGTVLE 389
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdeildefrGSELQNYFTKLLEGDV-KVIVKPQYvdlipKAVKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQlgpklvgvNADKR--IEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTL 467
Cdd:cd03236 110 LLK--------KKDERgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181
|
170 180
....*....|....*....|....*...
gi 1081004564 468 LRQLADDGRTVISITHDPLVVQAMGDYV 495
Cdd:cd03236 182 IRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
323-498 |
1.96e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 323 CIVGHNGSGKSTLALTLGGLLEPMAGTVQ----------VAGSGSAPWKWpskKLATRIGTVFQDPEhQFVTGTVLEELQ 392
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlrdLYALSEAERRR---LLRTEWGFVHQHPR-DGLRMQVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 393 LGPKL--VGVNADKRIEEL----LERLRL-TALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL 465
Cdd:PRK11701 112 IGERLmaVGARHYGDIRATagdwLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLL 191
|
170 180 190
....*....|....*....|....*....|....
gi 1081004564 466 TLLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK11701 192 DLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVM 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
139-497 |
2.10e-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: 56.72 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 139 DLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDP----AGVPVLRDAAitaaeRTGAALIVVEHrv 214
Cdd:COG1245 198 EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrlNVARLIRELA-----EEGKYVLVVEH-- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 215 D-AWVDVVDRIIVLGRG-----GVIADGAPHRV-----LEDYgqaLTDAGVWIpgappalpdaRSVACDQDGHPSGDIai 283
Cdd:COG1245 271 DlAILDYLADYVHILYGepgvyGVVSKPKSVRVginqyLDGY---LPEENVRI----------RDEPIEFEVHAPRRE-- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 284 ETRELDIGYGA-KKSWFRGSETVEP--IARGVSVSIpseastciVGHNGSGKSTLALTLGGLLEPMAGTVQvagsgsapw 360
Cdd:COG1245 336 KEEETLVEYPDlTKSYGGFSLEVEGgeIREGEVLGI--------VGPNGIGKTTFAKILAGVLKPDEGEVD--------- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 361 kwPSKKLATRigtvfqdPehQFVT----GTVlEELqlgpkLVGVNADKR-----IEELLERLRLTALTKANPFSLSGGEK 431
Cdd:COG1245 399 --EDLKISYK-------P--QYISpdydGTV-EEF-----LRSANTDDFgssyyKTEIIKPLGLEKLLDKNVKDLSGGEL 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 432 RRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVqamgDYVVD 497
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLI----DYISD 524
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
283-500 |
2.13e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 283 IETRELDIGYGAKKSWFRgSETVEPIaRGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS----GSA 358
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFR-RQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 359 PWKwpskklATRIGTVFQDPEHQF----VTGTVLE-ELQLGPKLVGVNADKRIEELLERLRLTAlTKAN--PFSLSGGEK 431
Cdd:PRK15112 83 SYR------SQRIRMIFQDPSTSLnprqRISQILDfPLRLNTDLEPEQREKQIIETLRQVGLLP-DHASyyPHMLAPGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 432 RRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-233 |
2.20e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRKAAVlNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRtPASArgavglvlQ 101
Cdd:PRK10522 326 RNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-----GEILLDGK-PVTA--------E 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 102 DPDS--QTISARVGD----DVAFGAENLGVAPAeignRVRASLDLVGLDLPLDHPTHR-----LSGGQKQRLALAGVLAM 170
Cdd:PRK10522 391 QPEDyrKLFSAVFTDfhlfDQLLGPEGKPANPA----LVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 171 GARVICLDEPTANIDPAG--------VPVLRDAAITaaertgaaLIVVEHRvDAWVDVVDRIIvLGRGGVI 233
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFrrefyqvlLPLLQEMGKT--------IFAISHD-DHYFIHADRLL-EMRNGQL 527
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
277-498 |
2.25e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 55.89 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 277 PSGDIAIETRELDIGYGAKKSWF-RGSETVEPIArGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAG- 354
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGLFgRTVGVVKAVD-GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 355 -----SGSAPwkwpsKKLATRIGTVFQDP-----EHQFVTGTVLEELQLGPKLVGVNADKRIEELLERLRLTAlTKAN-- 422
Cdd:COG4608 81 ditglSGREL-----RPLRRRMQMVFQDPyaslnPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRP-EHADry 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 423 PFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
299-522 |
2.30e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLePMAGTVQVAG----SGSAPWKWPSKKL----ATR 370
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSPPVVYPSGdirfHGESLLHASEQTLrgvrGNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 371 IGTVFQDP----------EHQFVtgtvlEELQLGPKLVGVNADKRIEELLERL-------RLTALtkanPFSLSGGEKRR 433
Cdd:PRK15134 94 IAMIFQEPmvslnplhtlEKQLY-----EVLSLHRGMRREAARGEILNCLDRVgirqaakRLTDY----PHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 434 LSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDMdafhpeRSGRAAPG 512
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVM------QNGRCVEQ 238
|
250
....*....|
gi 1081004564 513 QRASEEQAGP 522
Cdd:PRK15134 239 NRAATLFSAP 248
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
425-498 |
2.56e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.93 E-value: 2.56e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 425 SLSGGEKRRLSVATML---ATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDpLVVQAMGDYVVDM 498
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN-LDVIKCADWIIDL 244
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
324-497 |
2.80e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.00 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLAtRIGTV--FQDPEhQFVTGTVLEEL------QLGP 395
Cdd:PRK11300 36 LIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGHQIA-RMGVVrtFQHVR-LFREMTVIENLlvaqhqQLKT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 396 KLVG------------VNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTE 463
Cdd:PRK11300 112 GLFSgllktpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKE 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081004564 464 LLTLLRQLADD-GRTVISITHDPLVVQAMGD--YVVD 497
Cdd:PRK11300 192 LDELIAELRNEhNVTVLLIEHDMKLVMGISDriYVVN 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
297-500 |
3.67e-08 |
|
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: 53.63 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 297 SWFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgsapwkwpskklatrIGTVFQ 376
Cdd:cd03250 9 TWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------------IAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 377 DPEHQfvTGTVLEELQLGPKLvgvnaDKriEELLERLRLTALTK--------------ANPFSLSGGEKRRLSVATMLAT 442
Cdd:cd03250 74 EPWIQ--NGTIRENILFGKPF-----DE--ERYEKVIKACALEPdleilpdgdlteigEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 443 APDIVLLDEPTFGQDRRTFTELLT-LLRQLADDGRTVISITHD-PLVVQAmgDYVVDMDA 500
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQlQLLPHA--DQIVVLDN 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-243 |
4.38e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 22 RGFGYRHAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgDDSDGEATGKLLIEGRTPASA----RGAVg 97
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNT-DGFHIGVEGVITYDGITPEEIkkhyRGDV- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 98 LVLQDPDSQTISARVGDDVAFGA-------ENLGVAPAEIGNRVRaslDLVGLDLPLDHPTHR---------LSGGQKQR 161
Cdd:TIGR00956 141 VYNAETDVHFPHLTVGETLDFAArcktpqnRPDGVSREEYAKHIA---DVYMATYGLSHTRNTkvgndfvrgVSGGERKR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 162 LALAGVLAMGARVICLDEPTANIDPAG----VPVLRDAA-ITAAERTGAALIVVEhrvDAWvDVVDRIIVLGRGGVIADG 236
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATalefIRALKTSAnILDTTPLVAIYQCSQ---DAY-ELFDKVIVLYEGYQIYFG 293
|
....*..
gi 1081004564 237 APHRVLE 243
Cdd:TIGR00956 294 PADKAKQ 300
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
36-231 |
4.42e-08 |
|
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: 53.10 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIagvlgddsdGEATGKLLIEGRTPASARGAVGLVLQdpdSQTISArvgdd 115
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---------LYASGKARLISFLPKFSRNKLIFIDQ---LQFLID----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 116 vafgaenlgvapaeignrvrasldlVGLD-LPLDHPTHRLSGGQKQRLALAGVLAMGAR--VICLDEPTANIDPAGVPVL 192
Cdd:cd03238 74 -------------------------VGLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081004564 193 RDaAITAAERTGAALIVVEHRVDAwVDVVDRIIVLGRGG 231
Cdd:cd03238 129 LE-VIKGLIDLGNTVILIEHNLDV-LSSADWIIDFGPGS 165
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
381-496 |
6.89e-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: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 381 QFVTGTVLEELQlgpklvgvNADKR--IEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDR 458
Cdd:COG1245 174 KVFKGTVRELLE--------KVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
90 100 110
....*....|....*....|....*....|....*...
gi 1081004564 459 RTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVH 283
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
371-507 |
7.35e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.57 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 371 IGTVFQD----PeHQfvtgTVLEELQLGPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATA 443
Cdd:PRK09452 88 VNTVFQSyalfP-HM----TVFENVAFGLRMQKTPAAeitPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 444 PDIVLLDEPTFGQD---RRTF-TELLTLLRQLaddGRTVISITHDPLVVQAMGDYVVDMDAFHPERSG 507
Cdd:PRK09452 163 PKVLLLDESLSALDyklRKQMqNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
421-484 |
8.63e-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: 52.43 E-value: 8.63e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 421 ANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHD 484
Cdd:cd03215 100 ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE 163
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-230 |
1.02e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeATGKLLIEGRTPAS-ARGAVGLVLQD----------- 102
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTILANNRKPTKqILKRTGFVTQDdilyphltvre 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 103 ----------PDSQT--ISARVGDDVafgAENLGVAPAE---IGNR-VRAsldlvgldlpldhpthrLSGGQKQRLALAG 166
Cdd:PLN03211 160 tlvfcsllrlPKSLTkqEKILVAESV---ISELGLTKCEntiIGNSfIRG-----------------ISGGERKRVSIAH 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 167 VLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERtGAALIVVEHRVDAWV-DVVDRIIVLGRG 230
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVyQMFDSVLVLSEG 283
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
298-483 |
1.05e-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: 53.00 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 298 WFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSkkLATRIGTVFQD 377
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS--LRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 378 PeHQFvTGTVLEELQLGPKLVG----------VNADKRIEELLERLRltALTKANPFSLSGGEKRRLSVATMLATAPDIV 447
Cdd:cd03251 85 V-FLF-NDTVAENIAYGRPGATreeveeaaraANAHEFIMELPEGYD--TVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081004564 448 LLDEPTFGQDRRTFTELLTLLRQLADDgRTVISITH 483
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKN-RTTFVIAH 195
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
402-496 |
1.21e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 53.57 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 402 ADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISI 481
Cdd:COG4152 106 AKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFS 185
|
90
....*....|....*
gi 1081004564 482 THDPLVVQAMGDYVV 496
Cdd:COG4152 186 SHQMELVEELCDRIV 200
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
411-499 |
1.54e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 411 ERLRLTALTKANPFS--LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGR--TVISITHDPL 486
Cdd:cd03233 102 ETLDFALRCKGNEFVrgISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKttTFVSLYQASD 181
|
90
....*....|...
gi 1081004564 487 VVQAMGDYVVDMD 499
Cdd:cd03233 182 EIYDLFDKVLVLY 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
324-484 |
1.78e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.24 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTlggllepMAGTVQVAGS----GSAPWKWPSKKLATRIG-------TVFQDPEHQFVTgtvleeLQ 392
Cdd:PRK03695 27 LVGPNGAGKSTLLAR-------MAGLLPGSGSiqfaGQPLEAWSAAELARHRAylsqqqtPPFAMPVFQYLT------LH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 393 LGPKLVGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLS-VATMLATAPDI------VLLDEPTFGQDRRTFTELL 465
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRlAAVVLQVWPDInpagqlLLLDEPMNSLDVAQQAALD 173
|
170
....*....|....*....
gi 1081004564 466 TLLRQLADDGRTVISITHD 484
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHD 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-224 |
1.81e-07 |
|
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: 53.79 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 21 ARGFGYRhagrkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIeGRTPAsargaVGLVL 100
Cdd:TIGR03719 329 TKAFGDK------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS-----GTIEI-GETVK-----LAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 101 QDPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASL---------DLVGLdlpldhpthrLSGGQKQRLALAGVLAMG 171
Cdd:TIGR03719 392 QSRDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRfnfkgsdqqKKVGQ----------LSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 172 ARVICLDEPTANIDPAGVPVLRDAAITAAertGAAlIVVEHrvDAWvdVVDRI 224
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFA---GCA-VVISH--DRW--FLDRI 506
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
383-496 |
1.82e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 383 VTGTVLEELQlgpklvgvNADKR--IEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT 460
Cdd:PRK13409 176 FKGKVRELLK--------KVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
90 100 110
....*....|....*....|....*....|....*.
gi 1081004564 461 FTELLTLLRQLAdDGRTVISITHDPLVVQAMGDYVV 496
Cdd:PRK13409 248 RLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVH 282
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
311-478 |
1.90e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 311 GVSVSIPSEASTCIVGHNGSGKSTLALTLGGllEPMAGTVQVAGSGSAPWKWPSKKLATRIGTVFQDPEHQFVTGTVLEE 390
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 391 LQLGpklvGVNADK--------RIEELLERLRLTALTKANpfSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFT 462
Cdd:PRK11614 101 LAMG----GFFAERdqfqerikWVYELFPRLHERRIQRAG--TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170
....*....|....*.
gi 1081004564 463 ELLTLLRQLADDGRTV 478
Cdd:PRK11614 175 QIFDTIEQLREQGMTI 190
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
401-484 |
1.95e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 401 NADKRIEELLERLRL----TALTKanpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTfteLLTLLRQLADDGR 476
Cdd:PRK11819 140 DLDSQLEIAMDALRCppwdAKVTK-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG 211
|
....*...
gi 1081004564 477 TVISITHD 484
Cdd:PRK11819 212 TVVAVTHD 219
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-225 |
1.99e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEAT-----GKLLIEGRTPASARGAVGLVLQ-DPDSQTI 108
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADG-GSYTfpgnwQLAWVNQETPALPQPALEYVIDgDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 109 SARVGDDvafGAENLGVAPAEIGN----------RVRASLDLVGLDLP---LDHPTHRLSGGQKQRLALAGVLAMGARVI 175
Cdd:PRK10636 95 EAQLHDA---NERNDGHAIATIHGkldaidawtiRSRAASLLHGLGFSneqLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 176 CLDEPTANIDpagvpvlRDAAITaAER-----TGaALIVVEHRVDAWVDVVDRII 225
Cdd:PRK10636 172 LLDEPTNHLD-------LDAVIW-LEKwlksyQG-TLILISHDRDFLDPIVDKII 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
426-483 |
2.06e-07 |
|
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: 51.37 E-value: 2.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 426 LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITH 483
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
282-538 |
2.19e-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: 53.80 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 282 AIETRELDIGYG----AKKSWFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS-G 356
Cdd:TIGR00957 623 SIERRTIKPGEGnsitVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 357 SAPWKWPSKKLATRIGTVFQDPEHQFVTGTVLEELQLGPKLvgvnadkrieELLERLRLTALTKANpFSLSGGEKRRLSV 436
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDL----------EILPSGDRTEIGEKG-VNLSGGQKQRVSL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 437 ATMLATAPDIVLLDEPTFGQD----RRTFTELLTLLRQLAddGRTVISITH--------DPLVVQAMGDyVVDMDAFHP- 503
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDahvgKHIFEHVIGPEGVLK--NKTRILVTHgisylpqvDVIIVMSGGK-ISEMGSYQEl 848
|
250 260 270
....*....|....*....|....*....|....*...
gi 1081004564 504 -ERSGRAAPGQR--ASEEQAGPSSSKGSRGQGEAGGKS 538
Cdd:TIGR00957 849 lQRDGAFAEFLRtyAPDEQQGHLEDSWTALVSGEGKEA 886
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
138-497 |
2.68e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 138 LDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDpagvpvLRD---AAITAAERT-GAALIVVEHr 213
Cdd:PRK13409 197 VERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQrlnVARLIRELAeGKYVLVVEH- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 214 vD-AWVDVVDRIIVLGRG-----GVIADGAPHRV-----LEDYgqaLTDAGVWIpgappalpdaRSVACDQDGHP----- 277
Cdd:PRK13409 270 -DlAVLDYLADNVHIAYGepgayGVVSKPKGVRVgineyLKGY---LPEENMRI----------RPEPIEFEERPprdes 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 278 SGDIAIETRELDIGYGAkkswFrgSETVEP--IARGVSVSIpseastciVGHNGSGKSTLALTLGGLLEPMAGTVQvags 355
Cdd:PRK13409 336 ERETLVEYPDLTKKLGD----F--SLEVEGgeIYEGEVIGI--------VGPNGIGKTTFAKLLAGVLKPDEGEVD---- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 356 gsapwkwPSKKLATRIGTVFQDPEhqfvtGTVLEEL-QLGPKLvgvNADKRIEELLERLRLTALTKANPFSLSGGEKRRL 434
Cdd:PRK13409 398 -------PELKISYKPQYIKPDYD-----GTVEDLLrSITDDL---GSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRV 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 435 SVATMLATAPDIVLLDEPTFGQD---RRTFTElltLLRQLADD-GRTVISITHDPLvvqaMGDYVVD 497
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHLDveqRLAVAK---AIRRIAEErEATALVVDHDIY----MIDYISD 522
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-230 |
2.82e-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: 53.86 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 28 HAGRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdGEATgkllIEGRtpaSARGAVGLVLQD----P 103
Cdd:TIGR01257 1947 YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS-GDAT----VAGK---SILTNISDVHQNmgycP 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DSQTIsarvgDDVAFGAENL-------GVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVIC 176
Cdd:TIGR01257 2019 QFDAI-----DDLLTGREHLylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 177 LDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWN-TIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
370-485 |
3.21e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 370 RIGTVFQDPEHqFVTGTVLEELQLG-----PKLVGV-NADKRIEELLERLRLTALTKA---NPFS-LSGGEKRRLSVATM 439
Cdd:TIGR00956 837 SIGYVQQQDLH-LPTSTVRESLRFSaylrqPKSVSKsEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVE 915
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1081004564 440 LATAPD-IVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDP 485
Cdd:TIGR00956 916 LVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQP 962
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
306-500 |
3.26e-07 |
|
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: 50.87 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPehQFVTG 385
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS--TIPLEDLRSSLTIIPQDP--TLFSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVleELQLGPklVGVNADKRIEELLErlrltalTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL 465
Cdd:cd03369 97 TI--RSNLDP--FDEYSDEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081004564 466 TLLRQLADDGrTVISITHDplvVQAMGDY--VVDMDA 500
Cdd:cd03369 166 KTIREEFTNS-TILTIAHR---LRTIIDYdkILVMDA 198
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
388-498 |
4.14e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 53.11 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKLVGVnADKRIEELLERLR------LTALT---KANpfSLSGGEKRRLsvatMLATApdI------VL--LD 450
Cdd:COG0178 442 FENLELTEREAEI-AERILKEIRSRLGflvdvgLDYLTldrSAG--TLSGGEAQRI----RLATQ--IgsglvgVLyvLD 512
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 451 EPTFG--Q---DRrtfteLLTLLRQLADDGRTVISITHDPLVVQAmGDYVVDM 498
Cdd:COG0178 513 EPSIGlhQrdnDR-----LIETLKRLRDLGNTVIVVEHDEDTIRA-ADYIIDI 559
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
32-242 |
4.50e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 32 KAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGddsdgEATGKLLIEG---RTPASARGA--VGLVLQD---P 103
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT-----PAHGHVWLDGehiQHYASKEVArrIGLLAQNattP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DSQTISARVGDDVAFGAENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTAN 183
Cdd:PRK10253 94 GDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 184 IDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVL 242
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-236 |
4.65e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGddsdgEATGKLLIEGRtPASARGAVGLVLQDPDSQTIS----AR 111
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVR-----LASGKISILGQ-PTRQALQKNLVAYVPQSEEVDwsfpVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 112 VGDDVAFGAEN----LGVAPAEIGNRVRASLDLVGLdlpLDHpTHR----LSGGQKQRLALAGVLAMGARVICLDEPTan 183
Cdd:PRK15056 97 VEDVVMMGRYGhmgwLRRAKKRDRQIVTAALARVDM---VEF-RHRqigeLSGGQKKRVFLARAIAQQGQVILLDEPF-- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 184 idpAGVPVLRDAAITAAER----TGAALIVVEHRVDAWVDVVDRIIVLgRGGVIADG 236
Cdd:PRK15056 171 ---TGVDVKTEARIISLLRelrdEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
413-498 |
6.52e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 413 LRLTALTKANP-FSLSGGEKRRLSVATMLATA---PDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVV 488
Cdd:PRK00635 796 LGLDYLPLGRPlSSLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV 875
|
90
....*....|
gi 1081004564 489 QaMGDYVVDM 498
Cdd:PRK00635 876 K-VADYVLEL 884
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
410-494 |
6.60e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 410 LERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVV 488
Cdd:PRK11831 128 LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEV 207
|
....*.
gi 1081004564 489 QAMGDY 494
Cdd:PRK11831 208 LSIADH 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
300-490 |
6.93e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.34 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 300 RGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGgllEPMAGTvQVAGSGSAPW-KWPSKKlatrigtvfqdp 378
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA---GALKGT-PVAGCVDVPDnQFGREA------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 ehqfvtgTVLEEL-QLGPKLVGVnadkrieELLERLRLT--ALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFG 455
Cdd:COG2401 101 -------SLIDAIgRKGDFKDAV-------ELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081004564 456 QDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQA 490
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDD 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-235 |
7.55e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKaaVLNDITLDIERGEkvlLLGASGM---GKSTLLAAIAGVLgddsDGEATGKLLIEG-----RTPASA--------- 92
Cdd:PRK13549 274 HIK--RVDDVSFSLRRGE---ILGIAGLvgaGRTELVQCLFGAY----PGRWEGEIFIDGkpvkiRNPQQAiaqgiamvp 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 93 --RGAVGLVLQDPDSQTISARVGDDVAFG-----AENLGVAPAEIGN-RVR-ASLDLvgldlpldhPTHRLSGGQKQRLA 163
Cdd:PRK13549 345 edRKRDGIVPVMGVGKNITLAALDRFTGGsriddAAELKTILESIQRlKVKtASPEL---------AIARLSGGNQQKAV 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 164 LAGVLAMGARVICLDEPTANID-PAGVPVLRdaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIAD 235
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDvGAKYEIYK--LINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-195 |
8.16e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 10 PSSSGNVPAVSARGFGYRHaGRKAAVlNDITLDIERGEKVLLLGASGMGKST-------LLAAiagvlgddSDGEAtgKL 82
Cdd:NF033858 258 PADDDDEPAIEARGLTMRF-GDFTAV-DHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPA--------SEGEA--WL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 83 LieGRTPasargavglvlqDPDSQTISARVG-DDVAFG-------AENL-------GVAPAEIGNRVRASLDLVGLDLPL 147
Cdd:NF033858 326 F--GQPV------------DAGDIATRRRVGyMSQAFSlygeltvRQNLelharlfHLPAAEIAARVAEMLERFDLADVA 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081004564 148 DHPTHRLSGGQKQRLALAgvLAM--GARVICLDEPTANIDpagvPVLRDA 195
Cdd:NF033858 392 DALPDSLPLGIRQRLSLA--VAVihKPELLILDEPTSGVD----PVARDM 435
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
426-485 |
8.45e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 8.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 426 LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDP 485
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1079
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-252 |
1.25e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 19 VSArGFGYRhagrkaAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgeatgklliegrtpASARGAVGL 98
Cdd:PRK10636 318 VSA-GYGDR------IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL-------------------APVSGEIGL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 99 vlqdpdSQTIsaRVGDDVAFGAENLG-----------VAPAEIGNRVRASLDLVGLD-LPLDHPTHRLSGGQKQRLALAG 166
Cdd:PRK10636 372 ------AKGI--KLGYFAQHQLEFLRadesplqhlarLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLAL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 167 VLAMGARVICLDEPTANIDPAgvpvLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIA-DGAphrvLEDY 245
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLD----MRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPfDGD----LEDY 515
|
....*..
gi 1081004564 246 GQALTDA 252
Cdd:PRK10636 516 QQWLSDV 522
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-244 |
1.27e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.99 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 17 PAVSARGFGYRHAGRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTpasargav 96
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLA--VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG-----GTILLRGQH-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 97 glvLQDPDSQTIsARVGDDVAFG----------AENLGVA----------------PA------EIGNRVRASLDLVGLD 144
Cdd:PRK11300 69 ---IEGLPGHQI-ARMGVVRTFQhvrlfremtvIENLLVAqhqqlktglfsgllktPAfrraesEALDRAATWLERVGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 145 LPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRI 224
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|
gi 1081004564 225 IVLGRGGVIADGAPHRVLED 244
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNN 244
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
278-483 |
1.35e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.87 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 278 SGDIAIEtrELDIGYGAKKswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSgs 357
Cdd:PRK10790 338 SGRIDID--NVSFAYRDDN----------LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 358 apwkwPSKKLATR-----IGTVFQDPehQFVTGTVLEELQLGPKLvgvnADKRIEELLERLRLTALTKANP--------- 423
Cdd:PRK10790 404 -----PLSSLSHSvlrqgVAMVQQDP--VVLADTFLANVTLGRDI----SEEQVWQALETVQLAELARSLPdglytplge 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 424 --FSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT---FTELLTLLRQLAddgrTVISITH 483
Cdd:PRK10790 473 qgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTeqaIQQALAAVREHT----TLVVIAH 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
294-498 |
1.72e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.09 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 294 AKKSWF-RGSETVEPIaRGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTV-----QVAGSGSAPWKwpskkl 367
Cdd:PRK15079 22 DGKQWFwQPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkDLLGMKDDEWR------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 368 ATR--IGTVFQDP----EHQFVTGTVLEE-LQL-GPKLVGVNADKRIEELLERLRLTA-LTKANPFSLSGGEKRRLSVAT 438
Cdd:PRK15079 95 AVRsdIQMIFQDPlaslNPRMTIGEIIAEpLRTyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIAR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 439 MLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
308-483 |
1.72e-06 |
|
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: 49.41 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGS--GSAPWKWpskkLATRIGTVFQdpEHQFVTG 385
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAW----LRRQVGVVLQ--ENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQL---GPKLVGVNADKRI---EELLERLRL--TALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD 457
Cdd:cd03252 91 SIRDNIALadpGMSMERVIEAAKLagaHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180
....*....|....*....|....*.
gi 1081004564 458 RRTFTELLTLLRQLAdDGRTVISITH 483
Cdd:cd03252 171 YESEHAIMRNMHDIC-AGRTVIIIAH 195
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-236 |
2.28e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 6 LTRGPSSSGNVPAVSARGFgYRHAGRKAAVlNDITLDIERGEKVLLLGASGMgkstllAAIAGVLGDDSDGEATGKLLIE 85
Cdd:NF000106 1 MTRKTISNGARNAVEVRGL-VKHFGEVKAV-DGVDLDVREGTVLGVLGP*GA------A**RGALPAHV*GPDAGRRPWR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 86 GRTPASARGAvglvLQDPDSQTISARVGDDVAF-GAENL-----GVAPAEIGNRVRAS--LDLVGLDLPLDHPTHRLSGG 157
Cdd:NF000106 73 F*TWCANRRA----LRRTIG*HRPVR*GRRESFsGRENLymigr*LDLSRKDARARADelLERFSLTEAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 158 QKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWD-EVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-227 |
2.29e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 79 TGKLLIEG-----RTPASARGAVGLVLQDPDSQTISarVGDDVAFGAENlgvAPAEIGNRVR--ASLDLVGLDLPLDHPT 151
Cdd:PTZ00265 1276 SGKILLDGvdicdYNLKDLRNLFSIVSQEPMLFNMS--IYENIKFGKED---ATREDVKRACkfAAIDEFIESLPNKYDT 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 152 H------RLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVdAWVDVVDRII 225
Cdd:PTZ00265 1351 NvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIV 1429
|
..
gi 1081004564 226 VL 227
Cdd:PTZ00265 1430 VF 1431
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-185 |
2.37e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlGDDSDGEATgklLIEGRTpasargaVGLVLQDP---DSQ 106
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKEFEGEAR---PAPGIK-------VGYLPQEPqldPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 T---------------------ISARVGDDVAFG---AENLGVAPAEIgnrvrASLDLVGLDL------------PLDHP 150
Cdd:PRK11819 86 TvrenveegvaevkaaldrfneIYAAYAEPDADFdalAAEQGELQEII-----DAADAWDLDSqleiamdalrcpPWDAK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1081004564 151 THRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
365-496 |
2.81e-06 |
|
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: 49.80 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 365 KKLATRIGTVFQDP----EHQFVTGTVLEEL-QLGPKlvGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATM 439
Cdd:TIGR03269 105 RRIRKRIAIMLQRTfalyGDDTVLDNVLEALeEIGYE--GKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQ 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 440 LATAPDIVLLDEPTFGQDRRTFTELLTLLRQLA-DDGRTVISITHDPLVVQAMGDYVV 496
Cdd:TIGR03269 183 LAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKAI 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
308-496 |
2.98e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.91 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQvagSGSAPWKwpSKKLATRIgtVFQDPEhQFVTGTV 387
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---AGTAPLA--EAREDTRL--MFQDAR-LLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGpkLVGvNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTL 467
Cdd:PRK11247 99 IDNVGLG--LKG-QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175
|
170 180 190
....*....|....*....|....*....|
gi 1081004564 468 LRQL-ADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:PRK11247 176 IESLwQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
406-518 |
3.11e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 406 IEELLERLRLTALTKANPF--SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTFTELLTLLRQLADdgRTVIS 480
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDsnsEKLIEKTIVDIKDKAD--KTIIT 1414
|
90 100 110
....*....|....*....|....*....|....*...
gi 1081004564 481 ITHDPLVVQaMGDYVVDMDafHPERSGRAAPGQRASEE 518
Cdd:PTZ00265 1415 IAHRIASIK-RSDKIVVFN--NPDRTGSFVQAHGTHEE 1449
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
310-496 |
3.19e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.54 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPwkwpskkLAtrIGTVFqDPEHqfvtgTVLE 389
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL-------LE--LGAGF-HPEL-----TGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVN---ADKRIEELLErlrltaltkanpFS------------LSGGEKRRLSVATMLATAPDIVLLDEPTF 454
Cdd:COG1134 108 NIYLNGRLLGLSrkeIDEKFDEIVE------------FAelgdfidqpvktYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081004564 455 GQDRRtFTE-LLTLLRQLADDGRTVISITHDPLVVQAMGDYVV 496
Cdd:COG1134 176 VGDAA-FQKkCLARIRELRESGRTVIFVSHSMGAVRRLCDRAI 217
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
306-502 |
3.21e-06 |
|
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: 47.35 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKStlaltlggllepmagtvqvagsgsapwkwpskklatrigtvfqdpehqfvtg 385
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKS---------------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 386 TVLEELQLgpkLVGVNADKRIEELLERLRLT-ALTKANP----FSLSGGEKRRLSVATMLATAP----DIVLLDEPTFGQ 456
Cdd:cd03227 36 TILDAIGL---ALGGAQSATRRRSGVKAGCIvAAVSAELiftrLQLSGGEKELSALALILALASlkprPLYILDEIDRGL 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081004564 457 DRRTFTELLTLLRQLADDGRTVISITHDPLVVqAMGDYVVDMDAFH 502
Cdd:cd03227 113 DPRDGQALAEAILEHLVKGAQVIVITHLPELA-ELADKLIHIKKVI 157
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
392-483 |
4.40e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 48.14 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 392 QLGPKLVGVNADKRIEELLERLRLTA--LTKA-NPfSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLL 468
Cdd:COG0396 105 RRGEELSAREFLKLLKEKMKELGLDEdfLDRYvNE-GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGV 183
|
90
....*....|....*
gi 1081004564 469 RQLADDGRTVISITH 483
Cdd:COG0396 184 NKLRSPDRGILIITH 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
310-485 |
5.11e-06 |
|
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: 47.53 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPwkwpskkLAtrIGTVFqDPEHqfvtgTVLE 389
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL-------LG--LGGGF-NPEL-----TGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 390 ELQLGPKLVGVNA---DKRIEELLErlrLTALTKA--NPFS-LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTE 463
Cdd:cd03220 104 NIYLNGRLLGLSRkeiDEKIDEIIE---FSELGDFidLPVKtYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180
....*....|....*....|..
gi 1081004564 464 LLTLLRQLADDGRTVISITHDP 485
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDP 202
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
426-498 |
5.14e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 49.25 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 426 LSGGEKRRLSVATMLA---TAPDIVLLDEPTFG---QD-RRtfteLLTLLRQLADDGRTVISITHDPLVV-QAmgDYVVD 497
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGlhfHDiRK----LLEVLHRLVDKGNTVVVIEHNLDVIkTA--DWIID 900
|
.
gi 1081004564 498 M 498
Cdd:COG0178 901 L 901
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-269 |
5.86e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 31 RKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEAT--GKLL--IEGRTPASARGAVGLVLQDP-DS 105
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLR-LVESQGGEIIfnGQRIdtLSPGKLQALRRDIQFIFQDPyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 QTISARVGDDVAFGAENLGVAPAEIG-NRVRASLDLVGL--DLPLDHPtHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGLLPGKAAaARVAWLLERVGLlpEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 183 NIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED----YGQALTDAgvwIPG 258
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENpqhpYTRKLMAA---VPV 569
|
250
....*....|.
gi 1081004564 259 APPALPDARSV 269
Cdd:PRK10261 570 ADPSRQRPQRV 580
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
307-483 |
6.14e-06 |
|
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: 47.47 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwpSKKLATRIGTVFQDPehQFVTGT 386
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE--HKYLHSKVSLVGQEP--VLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VLEELQLG----------PKLVGVNADKRIEELLERLRLTALTKANpfSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQ 456
Cdd:cd03248 104 LQDNIAYGlqscsfecvkEAAQKAHAHSFISELASGYDTEVGEKGS--QLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180
....*....|....*....|....*..
gi 1081004564 457 DRRTFTELLTLLRQLADDgRTVISITH 483
Cdd:cd03248 182 DAESEQQVQQALYDWPER-RTVLVIAH 207
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
303-500 |
6.88e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 303 ETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEP----MAGTVQVAGSGSAPWKWPSKKLATrigtVFQDP 378
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIAT----IMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 EHQF-----VTGTVLEELQLGPKLvgvNADKRIEELLERLRLT---ALTKANPFSLSGGEKRRLSVA-TMLATAPDIVlL 449
Cdd:PRK10418 89 RSAFnplhtMHTHARETCLALGKP---ADDATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIAlALLCEAPFII-A 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 450 DEPTFGQDRRTFTELLTLLRQL-ADDGRTVISITHDPLVVQAMGDYVVDMDA 500
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSH 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
324-483 |
7.90e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.42 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPehQFVTGTVLEELQLGpklvgvNAD 403
Cdd:PRK13657 366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR--TVTRASLRRNIAVVFQDA--GLFNRSIEDNIRVG------RPD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 404 KRIEELLERLRLTA-----LTKANPF---------SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRT---FTELLT 466
Cdd:PRK13657 436 ATDEEMRAAAERAQahdfiERKPDGYdtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETeakVKAALD 515
|
170
....*....|....*..
gi 1081004564 467 LLRQladdGRTVISITH 483
Cdd:PRK13657 516 ELMK----GRTTFIIAH 528
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
324-496 |
8.51e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.42 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQvagsgsapwkwpsKKLATRIGTVFQ----DPEHQFvtgTVLEELQLGPklvG 399
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPDEGVIK-------------RNGKLRIGYVPQklylDTTLPL---TVNRFLRLRP---G 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 400 VNaDKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD-GRTV 478
Cdd:PRK09544 96 TK-KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAV 174
|
170
....*....|....*...
gi 1081004564 479 ISITHDPLVVQAMGDYVV 496
Cdd:PRK09544 175 LMVSHDLHLVMAKTDEVL 192
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
38-192 |
1.01e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.72 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 38 DITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARGAVGLVLqdpdsqtisARVG---- 113
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDA-----GEVLWQGEPIRRQRDEYHQDL---------LYLGhqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 114 -DDVAFGAENL-------GVAPAEignRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:PRK13538 85 iKTELTALENLrfyqrlhGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
....*..
gi 1081004564 186 PAGVPVL 192
Cdd:PRK13538 162 KQGVARL 168
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
307-495 |
1.23e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLL--EPMAGTVQVAGSGSAPWKwPSKKLATRIGTVFQDP------ 378
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELS-PEDRAGEGIFMAFQYPveipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 379 EHQFVTGTVL---EELQLGPKLVGVNADKRIEELLERLRLTA--LTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPT 453
Cdd:PRK09580 94 SNQFFLQTALnavRSYRGQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081004564 454 FGQDRRTFTELLTLLRQLADDGRTVISITHdplvVQAMGDYV 495
Cdd:PRK09580 174 SGLDIDALKIVADGVNSLRDGKRSFIIVTH----YQRILDYI 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
425-495 |
1.32e-05 |
|
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: 46.06 E-value: 1.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 425 SLSGGEKRRLSVATMLATAP------DIVLLDEPTFGQDR-RTFTELLTLLR-QLADDGRTVISITHDPLVVQAMGDYV 495
Cdd:cd03240 115 RCSGGEKVLASLIIRLALAEtfgsncGILALDEPTTNLDEeNIEESLAEIIEeRKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-241 |
1.47e-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: 48.09 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 141 VGLD-LPLDHPTHRLSGGQKQRLALAGVL---AMGARVICLDEPTANIDPAGVPVLRDaAITAAERTGAALIVVEHRVDA 216
Cdd:TIGR00630 816 VGLGyIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLE-VLQRLVDKGNTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|.
gi 1081004564 217 wVDVVDRIIVLG-----RGG-VIADGAPHRV 241
Cdd:TIGR00630 895 -IKTADYIIDLGpeggdGGGtVVASGTPEEV 924
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
426-483 |
2.04e-05 |
|
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: 47.12 E-value: 2.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 426 LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITH 483
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH 551
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
110-332 |
2.49e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 110 ARVGDDVAFGAENLGVAPAEIGNRVRASLDLvGLD-LPLDHPTHRLSGGQKQRLALAGVLAMGAR---VICLDEPTANID 185
Cdd:PRK00635 766 ADILEMTAYEAEKFFLDEPSIHEKIHALCSL-GLDyLPLGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLH 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 186 PAGVPVLRDAAITAAERtGAALIVVEHRVDAwVDVVDRIIVLG-----RGG-VIADGAPHRVLEDYGQALTDAGVWIPGA 259
Cdd:PRK00635 845 THDIKALIYVLQSLTHQ-GHTVVIIEHNMHV-VKVADYVLELGpeggnLGGyLLASCSPEELIHLHTPTAKALRPYLSSP 922
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 260 P--PALPDARsvacdQDGHPSGDIAIEtreldigygakkswfrgsETVEPIARGVSVSIPSEASTCIVGHNGSGK 332
Cdd:PRK00635 923 QelPYLPDPS-----PKPPVPADITIK------------------NAYQHNLKHIDLSLPRNALTAVTGPSASGK 974
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
35-185 |
2.78e-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: 47.21 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLgDDSDgeatGKLLIEGRTPASARgavglvlqdpDSQTISARVGD 114
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGEL-EPSE----GKIKHSGRISFSPQ----------TSWIMPGTIKD 505
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081004564 115 DVAFGAENLGVAPAEIGNRVRASLDLVGL----DLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:TIGR01271 506 NIIFGLSYDEYRYTSVIKACQLEEDIALFpekdKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
307-495 |
2.98e-05 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 45.71 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKS--TLALTLGGLLEPMAGTVQVAGSGSAPWKwPSKKLATRIGTVFQDPEHqfVT 384
Cdd:TIGR01978 14 EILKGVNLTVKKGEIHAIMGPNGSGKStlSKTIAGHPSYEVTSGTILFKGQDLLELE-PDERARAGLFLAFQYPEE--IP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 385 G-TVLEELQlgpklVGVNA--DKRIEELLERLRLTALTKAN------PFSL---------SGGEKRRLSVATMLATAPDI 446
Cdd:TIGR01978 91 GvSNLEFLR-----SALNArrSARGEEPLDLLDFEKLLKEKlalldmDEEFlnrsvnegfSGGEKKRNEILQMALLEPKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081004564 447 VLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDplvvQAMGDYV 495
Cdd:TIGR01978 166 AILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY----QRLLNYI 210
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
426-498 |
3.24e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 3.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 426 LSGGEKRRLSVATML---ATAPDIVLLDEPTFG---QDRRtftELLTLLRQLADDGRTVISITHDpLVVQAMGDYVVDM 498
Cdd:PRK00349 831 LSGGEAQRVKLAKELskrSTGKTLYILDEPTTGlhfEDIR---KLLEVLHRLVDKGNTVVVIEHN-LDVIKTADWIIDL 905
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
324-513 |
4.79e-05 |
|
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: 45.09 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApWKwPSKKLATRIGTVFQ-----DPEH----QFVTgTVLEELQlg 394
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YK-PQYIKADYEGTVRDllssiTKDFythpYFKT-EIAKPLQ-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 395 pklvgvnadkrIEELLERLRLTaltkanpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADD 474
Cdd:cd03237 105 -----------IEQILDREVPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081004564 475 G-RTVISITHDPLVVQAMGDYVVDMDAfHPERSGRAAPGQ 513
Cdd:cd03237 165 NeKTAFVVEHDIIMIDYLADRLIVFEG-EPSVNGVANPPQ 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
50-225 |
4.95e-05 |
|
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: 44.52 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 50 LLLGASGMGKSTLLAAIagvlgddsdgeatgKLLIEGRTPASARGAVGlvlqDPD---SQTISARVgdDVAFGAENlgva 126
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL--------------KYALTGELPPNSKGGAH----DPKlirEGEVRAQV--KLAFENAN---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 127 paeiGNRVRASLDLV-----------GLDLPLDHPTHRLSGGQKQ------RLALAGVLAMGARVICLDEPTANIDPAGV 189
Cdd:cd03240 82 ----GKKYTITRSLAilenvifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081004564 190 -PVLRDaAITAAERTGA-ALIVVEHrVDAWVDVVDRII 225
Cdd:cd03240 158 eESLAE-IIEERKSQKNfQLIVITH-DEELVDAADHIY 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
272-499 |
5.17e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.99 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 272 DQDGHPSGDIAIETRELDIgygakKSwFRGSETVEPIargvSVSIPSEASTCIVGHNGSGKSTLALTLGGLLePMAGTVQ 351
Cdd:PRK11174 339 EKELASNDPVTIEAEDLEI-----LS-PDGKTLAGPL----NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLK 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 352 VAG---SGSAPWKWpSKKLATrigtVFQDPehQFVTGTVLEELQLGpklvGVNA-DKRIEELLERLRLTALTKANPF--- 424
Cdd:PRK11174 408 INGielRELDPESW-RKHLSW----VGQNP--QLPHGTLRDNVLLG----NPDAsDEQLQQALENAWVSEFLPLLPQgld 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 425 --------SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQlADDGRTVISITH--DPLvvQAMgDY 494
Cdd:PRK11174 477 tpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHqlEDL--AQW-DQ 552
|
....*
gi 1081004564 495 VVDMD 499
Cdd:PRK11174 553 IWVMQ 557
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-231 |
5.43e-05 |
|
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: 44.16 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 36 LNDITLDIERGEKVLLLGASGMGKSTLLAAIAgvlGDDSDGEATGKLLIEGR-TPASARGAVGLVLQdpdsqtisarvgD 114
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLA---GRKTAGVITGEILINGRpLDKNFQRSTGYVEQ------------Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 115 DVAFGaeNLGVAPAeignrVRASLDLVGldlpldhpthrLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAG----VP 190
Cdd:cd03232 88 DVHSP--NLTVREA-----LRFSALLRG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAayniVR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081004564 191 VLRDAAitaaeRTGAALIVVEHRVDAWV-DVVDRIIVLGRGG 231
Cdd:cd03232 150 FLKKLA-----DSGQAILCTIHQPSASIfEKFDRLLLLKRGG 186
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-230 |
5.61e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVlgddsDGEATGKLLIEGR--TPASARGAV----GLVlqdp 103
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-----DKRAGGEIRLNGKdiSPRSPLDAVkkgmAYI---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 dsqTISARvgDDVAFG----AENLGVAPAEIGNRVRASLDLVG--------------LDL---PLDHPTHRLSGGQKQRL 162
Cdd:PRK09700 344 ---TESRR--DNGFFPnfsiAQNMAISRSLKDGGYKGAMGLFHevdeqrtaenqrelLALkchSVNQNITELSGGNQQKV 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081004564 163 ALAGVLAMGARVICLDEPTANIDpagvpVLRDAAITAAERT----GAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGID-----VGAKAEIYKVMRQladdGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
310-483 |
5.83e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 310 RGVSVSIPSEASTCIVGHNGSGKStlaltlggllepmagT-------VQVAGSGS-----APWKWPSKKLATR--IGTVF 375
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKS---------------TlmkilsgVYQPDSGEilldgEPVRFRSPRDAQAagIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 376 QDPeHQFVTGTVLEELQLG--PKLVGVNADKRI----EELLERL----RLTALTKanpfSLSGGEKRRLSVATMLATAPD 445
Cdd:COG1129 86 QEL-NLVPNLSVAENIFLGrePRRGGLIDWRAMrrraRELLARLgldiDPDTPVG----DLSVAQQQLVEIARALSRDAR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081004564 446 IVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITH 483
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
388-498 |
6.83e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 388 LEELQLGPKlvgvnaDKRI-----EELLERLR------LTALT---KANpfSLSGGEKRRLSVATmlatapDI------V 447
Cdd:PRK00349 446 FENLKLSEQ------EAKIaepilKEIRERLKflvdvgLDYLTlsrSAG--TLSGGEAQRIRLAT------QIgsgltgV 511
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 448 L--LDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAmGDYVVDM 498
Cdd:PRK00349 512 LyvLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRA-ADYIVDI 563
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-482 |
7.88e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 30 GRKAavLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGR------TPASARGAVGLVLQDP 103
Cdd:PRK10982 10 GVKA--LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS-----GSILFQGKeidfksSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DsQTISARVGDDVAFG---AENLGVAPAEIGNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEP 180
Cdd:PRK10982 83 N-LVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 181 TANIDPAGVPVLRdAAITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED------YGQALTDAgv 254
Cdd:PRK10982 162 TSSLTEKEVNHLF-TIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDkiiammVGRSLTQR-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 255 wipgappaLPDARSVAcdqdghpsGDIAIETRELdigygakkswfrgSETVEPIARGVSVSIPSEASTCIVGHNGSGKST 334
Cdd:PRK10982 239 --------FPDKENKP--------GEVILEVRNL-------------TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 335 LALTLGGLLEPMAGTVQVAGsgsapwkwpsKKLATRigTVFQDPEHQFvtGTVLEE---------LQLGPKLVGVNADKR 405
Cdd:PRK10982 290 IVETLFGIREKSAGTITLHG----------KKINNH--NANEAINHGF--ALVTEErrstgiyayLDIGFNSLISNIRNY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 406 IEE--LLERLRLTALT--------------KANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLR 469
Cdd:PRK10982 356 KNKvgLLDNSRMKSDTqwvidsmrvktpghRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIA 435
|
490
....*....|...
gi 1081004564 470 QLADDGRTVISIT 482
Cdd:PRK10982 436 ELAKKDKGIIIIS 448
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
425-481 |
1.33e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 1.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 425 SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISI 481
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
425-498 |
1.35e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 425 SLSGGEKRRLSVATMLATAPD---IVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAmGDYVVDM 498
Cdd:PRK00635 1699 SLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEM 1774
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
33-185 |
1.36e-04 |
|
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: 44.08 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 33 AAVLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRTPASARgavglvlqdpDSQTISARV 112
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE-----GKIKHSGRISFSSQ----------FSWIMPGTI 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 113 GDDVAFGAENLGVAPAEIGNRVRASLDLVGL----DLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACQLEEDITKFpekdNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
45-182 |
1.62e-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: 41.98 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 45 RGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatgklliegrtpasargaVGLVLQDPDsqtisarvgddvafgaenlg 124
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG---------------------GGVIYIDGE-------------------- 39
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 125 vapaeignRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTA 182
Cdd:smart00382 40 --------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITS 89
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
414-513 |
1.67e-04 |
|
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: 42.56 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 414 RLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDG-RTVISITHDPLVVQAMG 492
Cdd:cd03222 60 GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLS 139
|
90 100
....*....|....*....|.
gi 1081004564 493 DYVVDMDAfHPERSGRAAPGQ 513
Cdd:cd03222 140 DRIHVFEG-EPGVYGIASQPK 159
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
37-213 |
1.74e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 37 NDITLDieRGEKVLLLGASGMGKSTLLAAIAGVLGddsdgeatgkllieGRTPASARGAVGLvlqdpdSQTISARVgddv 116
Cdd:cd03227 14 NDVTFG--EGSLTIITGPNGSGKSTILDAIGLALG--------------GAQSATRRRSGVK------AGCIVAAV---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 117 afgaenlgvapaeignrvraSLDLVGLDlpldhptHRLSGGQKQRLALAGVLAMGAR----VICLDEPTANIDPagvpvl 192
Cdd:cd03227 68 --------------------SAELIFTR-------LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDP------ 114
|
170 180
....*....|....*....|....*.
gi 1081004564 193 RDAAITAA---ERT--GAALIVVEHR 213
Cdd:cd03227 115 RDGQALAEailEHLvkGAQVIVITHL 140
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
426-498 |
1.96e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 1.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 426 LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGRTVISITHDPLVVQAMGDYVVDM 498
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
403-498 |
1.97e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 403 DKRIEELLERL--RLTALTKAN-PF--------SLSGGEKRRLSVATMLATAPDIV--LLDEPTFGQDRRTFTELLTLLR 469
Cdd:PRK00635 443 SLSIEEVLQGLksRLSILIDLGlPYltperalaTLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIK 522
|
90 100
....*....|....*....|....*....
gi 1081004564 470 QLADDGRTVISITHDPLVVqAMGDYVVDM 498
Cdd:PRK00635 523 KLRDQGNTVLLVEHDEQMI-SLADRIIDI 550
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
35-217 |
2.05e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.97 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIA-------GVLGDDSDGeatgKLLIEGRTPASARGAvglvLQD----P 103
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvygGRLTKPAKG----KLFYVPQRPYMTLGT----LRDqiiyP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 DSQTISARVGddvaFGAENLgvapaeignrvRASLDLVgldlPLDHPTHR-------------LSGGQKQRLALAGVLAM 170
Cdd:TIGR00954 539 DSSEDMKRRG----LSDKDL-----------EQILDNV----QLTHILEReggwsavqdwmdvLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081004564 171 GARVICLDEPTANIDPAgvpvLRDAAITAAERTGAALIVVEHRVDAW 217
Cdd:TIGR00954 600 KPQFAILDECTSAVSVD----VEGYMYRLCREFGITLFSVSHRKSLW 642
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
324-484 |
2.16e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.78 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 324 IVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPehQFVTGTVLEELQLGPKLVGVNAD 403
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS--TLKPEIYRQQVSYCAQTP--TLFGDTVYDNLIFPWQIRNQQPD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 404 -KRIEELLERLRL--TALTKaNPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTFTELLTllRQLADDGRT 477
Cdd:PRK10247 114 pAIFLDDLERFALpdTILTK-NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnKHNVNEIIH--RYVREQNIA 190
|
....*..
gi 1081004564 478 VISITHD 484
Cdd:PRK10247 191 VLWVTHD 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
307-460 |
2.28e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPehQFVTGT 386
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFGLMDLRKVLGIIPQAP--VLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VleELQLGPklVGVNADKRIEELLERLRLTALTKANPFSL-----------SGGEKRRLSVATMLATAPDIVLLDEPTFG 455
Cdd:PLN03130 1329 V--RFNLDP--FNEHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
....*
gi 1081004564 456 QDRRT 460
Cdd:PLN03130 1405 VDVRT 1409
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-186 |
2.60e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGvlgDDSDGEATgKLLIEGRTPASA------RGAVGLVlqdpDSQ-- 106
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG---DHPQGYSN-DLTLFGRRRGSGetiwdiKKHIGYV----SSSlh 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 107 ---TISARVGDDVAFGA-ENLGVAPAeIGNRVRAS----LDLVGLDLPL-DHPTHRLSGGQkQRLAL-AGVLAMGARVIC 176
Cdd:PRK10938 347 ldyRVSTSVRNVILSGFfDSIGIYQA-VSDRQQKLaqqwLDILGIDKRTaDAPFHSLSWGQ-QRLALiVRALVKHPTLLI 424
|
170
....*....|
gi 1081004564 177 LDEPTANIDP 186
Cdd:PRK10938 425 LDEPLQGLDP 434
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-185 |
2.67e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatgkllieGRTPASARGAVGLVLQDP----------- 103
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS-----------GTVKWSENANIGYYAQDHaydfendltlf 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 104 -----------DSQTISARVGdDVAFGAEnlgvapaEIGNRVRAsldlvgldlpldhpthrLSGGQKQRLaLAGVLAMG- 171
Cdd:PRK15064 403 dwmsqwrqegdDEQAVRGTLG-RLLFSQD-------DIKKSVKV-----------------LSGGEKGRM-LFGKLMMQk 456
|
170
....*....|....
gi 1081004564 172 ARVICLDEPTANID 185
Cdd:PRK15064 457 PNVLVMDEPTNHMD 470
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
306-453 |
2.77e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 306 EPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVqvagsgsapwKWPSKklaTRIGTVFQDPEHQFVTG 385
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSEN---ANIGYYAQDHAYDFEND 398
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 386 TVLEELQLGPKLVGVNaDKRIEELLERLRLTA-LTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPT 453
Cdd:PRK15064 399 LTLFDWMSQWRQEGDD-EQAVRGTLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
394-491 |
3.51e-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: 41.20 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 394 GPKLVGVNADKRIEELLERLRLTaLTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELL------TL 467
Cdd:smart00382 30 GGGVIYIDGEDILEEVLDQLLLI-IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLL 108
|
90 100
....*....|....*....|....
gi 1081004564 468 LRQLADDGRTVISITHDPLVVQAM 491
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
312-483 |
4.85e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwkwpskkLATRIGTVFQdpehqfVTGtvLEEL 391
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL--------IAISSGLNGQ------LTG--IENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 392 QLGPKLVGVNADKRIE---ELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDrRTFT-ELLTL 467
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEiipEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD-QTFTkKCLDK 185
|
170
....*....|....*.
gi 1081004564 468 LRQLADDGRTVISITH 483
Cdd:PRK13545 186 MNEFKEQGKTIFFISH 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-212 |
5.09e-04 |
|
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: 41.97 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 46 GEKVLLLGASGMGKSTLLAAIAGV----LGDDSDGEATGKLLIEGRtpasargavGLVLQDPDSQTISARVgdDVAFGAE 121
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKlkpnLGKFDDPPDWDEILDEFR---------GSELQNYFTKLLEGDV--KVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 122 NLGVAPAEIGNRV---------RASLDLVGLDLPLDHPTHR----LSGGQKQRLALAGVLAMGARVICLDEPTANIDpag 188
Cdd:cd03236 95 YVDLIPKAVKGKVgellkkkdeRGKLDELVDQLELRHVLDRnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLD--- 171
|
170 180
....*....|....*....|....*.
gi 1081004564 189 VPVLRDAAITAAE--RTGAALIVVEH 212
Cdd:cd03236 172 IKQRLNAARLIRElaEDDNYVLVVEH 197
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
406-483 |
7.35e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.11 E-value: 7.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081004564 406 IEELLERLrltaltkanPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLADDGR-TVISITH 483
Cdd:PRK10771 119 IEDLLARL---------PGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQlTLLMVSH 188
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
394-499 |
9.35e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 41.63 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 394 GPKLVGVNAD---KRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD---RRTFTELLTL 467
Cdd:PRK11432 102 GLKMLGVPKEerkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDanlRRSMREKIRE 181
|
90 100 110
....*....|....*....|....*....|..
gi 1081004564 468 LRQLAddGRTVISITHDPLVVQAMGDYVVDMD 499
Cdd:PRK11432 182 LQQQF--NITSLYVTHDQSEAFAVSDTVIVMN 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
426-483 |
9.42e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.01 E-value: 9.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081004564 426 LSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLAdDGRTVISITH 483
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAH 508
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
300-483 |
9.55e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.05 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 300 RGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPe 379
Cdd:cd03288 28 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLRSRLSIILQDP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 380 hQFVTGTVleELQLGPKLVGvnADKRIEELLERLRLTALTKANPFSL-----------SGGEKRRLSVATMLATAPDIVL 448
Cdd:cd03288 105 -ILFSGSI--RFNLDPECKC--TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1081004564 449 LDEPTFGQDRRTfTELLTLLRQLADDGRTVISITH 483
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVVMTAFADRTVVTIAH 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-185 |
9.69e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 23 GFGYRhagrkaaVL-NDITLDIERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIeGRTPAsargaVGLVLQ 101
Cdd:PRK11819 333 SFGDR-------LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDS-----GTIKI-GETVK-----LAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 102 DPDSQTISARVGDDVAFGAENLGVAPAEIGNRVRASL------D---LVGLdlpldhpthrLSGGQKQRLALAGVLAMGA 172
Cdd:PRK11819 395 SRDALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGRfnfkggDqqkKVGV----------LSGGERNRLHLAKTLKQGG 464
|
170
....*....|...
gi 1081004564 173 RVICLDEPTANID 185
Cdd:PRK11819 465 NVLLLDEPTNDLD 477
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
313-485 |
1.02e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.04 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 313 SVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVagsgsapwkwPSKklatriGTVFQDPEHQFVTGTVLEELQ 392
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK----------PAK------GKLFYVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 393 LGP------KLVGVnADKRIEELLERLRLTALTKAN-PFS--------LSGGEKRRLSVATMLATAPDIVLLDEPTFG-- 455
Cdd:TIGR00954 536 IYPdssedmKRRGL-SDKDLEQILDNVQLTHILEREgGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAvs 614
|
170 180 190
....*....|....*....|....*....|...
gi 1081004564 456 ---QDRrtftelltLLRQLADDGRTVISITHDP 485
Cdd:TIGR00954 615 vdvEGY--------MYRLCREFGITLFSVSHRK 639
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
51-236 |
1.09e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.40 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 51 LLGASGMGKSTLLAAIAGVLGDDSdgeatGKLLIEGRT----------PASARGaVGLVLQDpdsqtisARVgddvaF-- 118
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQK-----GRIVLNGRVlfdaekgiclPPEKRR-IGYVFQD-------ARL-----Fph 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 119 ----GAENLGVAPAEIG--NRVrasLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID-PAG--- 188
Cdd:PRK11144 91 ykvrGNLRYGMAKSMVAqfDKI---VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKrel 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081004564 189 VPVLRdaaiTAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADG 236
Cdd:PRK11144 168 LPYLE----RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
307-500 |
1.16e-03 |
|
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: 41.63 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKWPSkkLATRIGTVFQDPeHQFvTGT 386
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS--LRRQVALVSQDV-VLF-NDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VLEELQLGpKLVGVNaDKRIEELLERLRLTALTKANPFS-----------LSGGEKRRLSVA-TMLATAPdIVLLDEPTF 454
Cdd:TIGR02203 422 IANNIAYG-RTEQAD-RAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIArALLKDAP-ILILDEATS 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081004564 455 GQDRRTFTELLTLLRQLAdDGRTVISITHDPLVVQAmGDYVVDMDA 500
Cdd:TIGR02203 499 ALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDD 542
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
41-333 |
1.54e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 41 LDIERGEKVLLLGASGMGKSTLLAAIAGVLgddsdgeatgkLLIEGRTPASARGAVGLV---LQDPDSQTISARVGDDVA 117
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGEL-----------PLLSGERQSQFSHITRLSfeqLQKLVSDEWQRNNTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 118 FGAENLGVAPAEI-------GNRVRASLDLVGLDLPLDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVP 190
Cdd:PRK10938 93 PGEDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 191 VLRDAaITAAERTGAALIVVEHRVDAWVDVVDRIIVLGRGGVIADGAPHRVLED-------YGQALTDAGVWIPGAPPAL 263
Cdd:PRK10938 173 QLAEL-LASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQalvaqlaHSEQLEGVQLPEPDEPSAR 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 264 PDArsvacdqdghPSGDIAIETRELDIGYGAKkswfrgsetvePIARGVSVSIPSEASTCIVGHNGSGKS 333
Cdd:PRK10938 252 HAL----------PANEPRIVLNNGVVSYNDR-----------PILHNLSWQVNPGEHWQIVGPNGAGKS 300
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
262-535 |
1.66e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 262 ALPDARSVACDQDGHPSGDIAIETRELDIGYGAKKSWFRGSETVEPIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGG 341
Cdd:PTZ00243 629 GSPSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 342 LLEPMAGTVQVAGSGSAPWKWPSKKLAT-RIGTVFQDPE-----HQFVTGTVLE----------ELQLGPKlvGVNadkr 405
Cdd:PTZ00243 709 QFEISEGRVWAERSIAYVPQQAWIMNATvRGNILFFDEEdaarlADAVRVSQLEadlaqlggglETEIGEK--GVN---- 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 406 ieellerlrltaltkanpfsLSGGEKRRLSVATMLATAPDIVLLDEPTFGQD----RRTFTELltLLRQLAddGRTVISI 481
Cdd:PTZ00243 783 --------------------LSGGQKARVSLARAVYANRDVYLLDDPLSALDahvgERVVEEC--FLGALA--GKTRVLA 838
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1081004564 482 THDPLVVqAMGDYVVDMDAFHPERSGRAAPGQRASEEQAGPSSSKGSRGQGEAG 535
Cdd:PTZ00243 839 THQVHVV-PRADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKENKDSKEGD 891
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-453 |
2.20e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 35 VLNDITLDIERGEKVLLLGASGMGKSTLLAAIA------------------GVLGDD---------SDGEATGKLLIEGR 87
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqEVVGDDttalqcvlnTDIERTQLLEEEAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 88 TPASARGAvglvlqDPDSQTISARVGDDVAFGAENLGVAPAEIGNRV----------RASLDLVGLDLPLD---HPTHRL 154
Cdd:PLN03073 272 LVAQQREL------EFETETGKGKGANKDGVDKDAVSQRLEEIYKRLelidaytaeaRAASILAGLSFTPEmqvKATKTF 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 155 SGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLrDAAITAAERTgaaLIVVEHRVDAWVDVVDRIIVLGRGGVIA 234
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKWPKT---FIVVSHAREFLNTVVTDILHLHGQKLVT 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 235 DGAPHRVLE---------------------DYGQALTDAGVWiPGAPPALPDARSVACDQDGH----------------- 276
Cdd:PLN03073 422 YKGDYDTFErtreeqlknqqkafesnersrSHMQAFIDKFRY-NAKRASLVQSRIKALDRLGHvdavvndpdykfefptp 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 277 ---PSGDIaIETRELDIGYGAKKSWFrgsetvepiaRGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVqva 353
Cdd:PLN03073 501 ddrPGPPI-ISFSDASFGYPGGPLLF----------KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--- 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 354 gsgsapWKWPSKKLAtrigtVFQdpEHQfVTGTvleELQLGPKLV------GVnADKRIEELLERLRLTALTKANP-FSL 426
Cdd:PLN03073 567 ------FRSAKVRMA-----VFS--QHH-VDGL---DLSSNPLLYmmrcfpGV-PEQKLRAHLGSFGVTGNLALQPmYTL 628
|
490 500
....*....|....*....|....*..
gi 1081004564 427 SGGEKRRLSVATMLATAPDIVLLDEPT 453
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPS 655
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
38-230 |
3.02e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 38 DITLDIERGEKVLLLGASGMGKSTLLAAIAGvLGDDSDGEAT-GKLLIEGRTPASA-----------RGAVGLVLQDPDS 105
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYG-LRPARGGRIMlNGKEINALSTAQRlarglvylpedRQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 106 QTISARVGDDVAFGAEnlGVAPAEIGNRVRASLDLVGLDLplDHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANID 185
Cdd:PRK15439 360 WNVCALTHNRRGFWIK--PARENAVLERYRRALNIKFNHA--EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081004564 186 PAG----VPVLRDAAitaaeRTGAALIVVEHRVDAWVDVVDRIIVLGRG 230
Cdd:PRK15439 436 VSArndiYQLIRSIA-----AQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
423-510 |
3.58e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 423 PFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQLAD-DGRTVISITHDPLVVQAMGDYVVDMDAF 501
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAG 230
|
....*....
gi 1081004564 502 HPERSGRAA 510
Cdd:PRK11022 231 QVVETGKAH 239
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
418-483 |
3.60e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 3.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081004564 418 LTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLLRQL-ADDGRTVISITH 483
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAH 638
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-232 |
3.90e-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: 38.32 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 154 LSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVLRDAAITAAERTGAALIVVEHRVDAWVDVVDRIIVL-GRGGV 232
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFeGEPGV 151
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
307-522 |
4.09e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.65 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWKwPSKKLATRIGTVFQDPeHQFVTGT 386
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIYLVPQEP-LLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VLEELQLG-PKlvGVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTF----GQDRRTF 461
Cdd:PRK15439 103 VKENILFGlPK--RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAsltpAETERLF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 462 TELLTLL----------------RQLAD------DGRTVISITHDPL----VVQAMGDYVVDMDAFHPERSGRAAPGQRA 515
Cdd:PRK15439 181 SRIRELLaqgvgivfishklpeiRQLADrisvmrDGTIALSGKTADLstddIIQAITPAAREKSLSASQKLWLELPGNRR 260
|
....*..
gi 1081004564 516 SEEQAGP 522
Cdd:PRK15439 261 QQAAGAP 267
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
43-192 |
4.23e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 43 IERGEKVLLLGASGMGKSTLLAAIAGVLGDDSdgeatgkllieGRTPASARGAVGLVLQDP-DSQTISArvgDDVAFGAE 121
Cdd:PLN03073 532 IDLDSRIAMVGPNGIGKSTILKLISGELQPSS-----------GTVFRSAKVRMAVFSQHHvDGLDLSS---NPLLYMMR 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081004564 122 NLGVAPAEignRVRASLDLVGL--DLPLdHPTHRLSGGQKQRLALAGVLAMGARVICLDEPTANIDPAGVPVL 192
Cdd:PLN03073 598 CFPGVPEQ---KLRAHLGSFGVtgNLAL-QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
425-519 |
4.78e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 425 SLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDrrtFTELLTLLRQLADDGRTVISITH-----DPLV-------VQAMG 492
Cdd:PRK10636 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHdrdflDPIVdkiihieQQSLF 225
|
90 100
....*....|....*....|....*..
gi 1081004564 493 DYVVDMDAFHPERSGRAAPGQRASEEQ 519
Cdd:PRK10636 226 EYTGNYSSFEVQRATRLAQQQAMYESQ 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
307-460 |
5.45e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 307 PIARGVSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSApwKWPSKKLATRIGTVFQDPehQFVTGT 386
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFGLTDLRRVLSIIPQSP--VLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 387 VleELQLGPklVGVNADKRIEELLERLRLTALTKANPFSL-----------SGGEKRRLSVATMLATAPDIVLLDEPTFG 455
Cdd:PLN03232 1326 V--RFNIDP--FSEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
....*
gi 1081004564 456 QDRRT 460
Cdd:PLN03232 1402 VDVRT 1406
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
299-484 |
5.85e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 299 FRGSETVEpIARGVsvsipseasTCIVGHNGSGKStlaltlggllepmagTVQVA------GSGSAPWKWPS-----KKL 367
Cdd:COG0419 13 YRDTETID-FDDGL---------NLIVGPNGAGKS---------------TILEAiryalyGKARSRSKLRSdlinvGSE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 368 ATRIGTVFQDPEHQFVT----GTVLEELQLGPK--------LVGVNADKRIEELLERL--------------------RL 415
Cdd:COG0419 68 EASVELEFEHGGKRYRIerrqGEFAEFLEAKPSerkealkrLLGLEIYEELKERLKELeealesaleelaelqklkqeIL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081004564 416 TALTKANPF-SLSGGEKRRLSVATMLAtapdiVLLDeptFG-QDRRTFTELLTLLRQLAddgrtvIsITHD 484
Cdd:COG0419 148 AQLSGLDPIeTLSGGERLRLALADLLS-----LILD---FGsLDEERLERLLDALEELA------I-ITHV 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
308-485 |
7.23e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.65 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 308 IARGVSVSIPSEASTCIVGHNGSGKSTLALT------LGGLLEPMAGTVQVAGSGSAPWKWPSKKLATRIGTVFQDPEHQ 381
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdltGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 382 FVTgTVLEELQLG--PKLVGVNADKR-----IEELLERLRLTALTKANPFSLSGGEKRRLSVATMLA---------TAPD 445
Cdd:PRK13547 96 FAF-SAREIVLLGryPHARRAGALTHrdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081004564 446 IVLLDEPTFGQDRRTFTELLTLLRQLADDGRT-VISITHDP 485
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDP 215
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
312-485 |
7.53e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 312 VSVSIPSEASTCIVGHNGSGKSTLALTLGGLLEPMAGTVQVAGSGSAPWkwpSKKLATRIGtvfqdpeHQF---VTGTVL 388
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI---AKPYCTYIG-------HNLglkLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081004564 389 EELQLGPKLvgVNADKRIEELLERLRLTALTKANPFSLSGGEKRRLSVATMLATAPDIVLLDEPTFGQDRRTFTELLTLL 468
Cdd:PRK13541 89 ENLKFWSEI--YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
170
....*....|....*..
gi 1081004564 469 RQLADDGRTVISITHDP 485
Cdd:PRK13541 167 VMKANSGGIVLLSSHLE 183
|
|
| |
