|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-661 |
0e+00 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 644.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:PRK10535 3 ALLELKDIRRSYP-SGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:PRK10535 82 QLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSanderPAHPSAGVerh 248
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNP-----PAQEKVNV--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 249 lqaddlsQRLAEGSSEPSGAWR---AELLEAVRAAWRVMWINRFRTALTLLGIIIGVASVVVMLAVGEGSKRQVMAQMGA 325
Cdd:PRK10535 234 -------AGGTEPVVNTASGWRqfvSGFREALTMAWRAMAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 326 FGSNII--Y----LSGYSPNPRAPMGIvssDDVAAIATLPQVKKVMPVNGGELVVRYGNIDYHAYVGGNNTDFPEILNWP 399
Cdd:PRK10535 307 IGTNTIdiYpgkdFGDDDPQYQQALKY---DDLIAIQKQPWVASATPAVSQSLRLRYGNIDVAASANGVSGDYFNVYGMT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 400 VAEGSYFTERDEDAATTVAVIGYKVRKKLF-GSANPIGRYILIENVPFQVIGVLAEKGSSSGDKDAdNRIAIPYSAASIR 478
Cdd:PRK10535 384 FSEGNTFNQEQLNGRAQVVVLDSNTRRQLFpHKADVVGEVILVGNMPATVIGVAEEKQSMFGSSKV-LRVWLPYSTMSGR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 479 LFGTRNPEYVIIAAADAQRVHQAERAIDQLmLRLHRGQRDYELTNNAAMIQAEAKTQNTLSLMLGSIAAISLLVGGIGVM 558
Cdd:PRK10535 463 VMGQSWLNSITVRVKEGYDSAEAEQQLTRL-LTLRHGKKDFFTWNMDSVLKTAEKTTRTLQLFLTLVAVISLVVGGIGVM 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 559 NIMLMTVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALALCIGGV--LLLGQVAVAFSLSAIVGAFSCA 636
Cdd:PRK10535 542 NIMLVSVTERTREIGIRMAVGARASDVLQQFLIEAVLVCLVGGALGITLSLLIAFTlqLFLPGWEIGFSPLALLSAFLCS 621
|
650 660
....*....|....*....|....*
gi 15597586 637 LVTGLVFGFMPARKAAQLDPVAALA 661
Cdd:PRK10535 622 TVTGILFGWLPARNAARLDPVDALA 646
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-233 |
9.08e-125 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 368.60 E-value: 9.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:COG1136 3 PLLELRNLTKSYG-TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELA-SQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSA 233
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-228 |
2.04e-109 |
|
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: 329.07 E-value: 2.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWL 90
Cdd:cd03255 1 IELKNLSKTYGGGGE-KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| SalY |
COG0577 |
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms]; |
275-663 |
7.15e-92 |
|
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
Pssm-ID: 440342 [Multi-domain] Cd Length: 339 Bit Score: 288.34 E-value: 7.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 275 EAVRAAWRVMWINRFRTALTLLGIIIGVASVVVMLAVGEGSKRQVMAQMGAFGSNIIYLSGYSPNPRAPMgivSSDDV-A 353
Cdd:COG0577 1 EYLRLALRSLRRNKLRSLLTVLGIAIGIALVIAILALGRGLRRSLLRDLDSLGFDLLTVSRTPGGSRATL---SYEDLrE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 354 AIATLPQVKKVMPVNGGELVVRY-GNIDYHAYVGGNNTDFPEILNWPVAEGSYFTERDEDAATTVAVIGYKVRKKLFGSA 432
Cdd:COG0577 78 ALRALPGVESVAPSSSGSATVRYgGGEPPSVRVLGVDPDYFRVLGIPLLAGRFFTAADDLGAPPVVVIGEALARRLFGGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 433 NPIGRYILIENVPFQVIGVLaekgsssgdkdadnriaipysaasirlfgtrnpeyviiaaadaqrvhqaERAIDQLMLRL 512
Cdd:COG0577 158 DPVGKTIRLNGRPFTVVGVV-------------------------------------------------EAELRALLRRR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 513 HRGQrDYELTNNAAMIQAEAKTQNTLSLMLGSIAAISLLVGGIGVMNIMLMTVRERTREIGIRMATGARQGDILRQFLTE 592
Cdd:COG0577 189 DPGD-DFEVQTLDEILAALYGVLRTLTLLLGAIAGLALLVACIGIMNLMLASVTERTREIGIRKALGASRRDILRQFLTE 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 593 AAMLSVVGGLAGIALALCIGGVL-LLGQVAVAFSLSAIVGAFSCALVTGLVFGFMPARKAAQLDPVAALASQ 663
Cdd:COG0577 268 ALLLALLGGLLGLLLALLLLRLLaALLGLPVSLDPWVLLLALALSLLVGLLAGLYPARRAARLDPVEALRSE 339
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-237 |
3.67e-85 |
|
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: 266.99 E-value: 3.67e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 1 MENATQPVplIELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVA 80
Cdd:COG4181 1 MSSSSAPI--IELRGLTKTVGTGAGE-LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELDSDEQAWLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGipASERHTRARALLERLGLAERTANRPHQLSGGQQQRV 160
Cdd:COG4181 78 ALDEDARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 161 SIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDER 237
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATAA 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-234 |
7.96e-78 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 247.27 E-value: 7.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWL 90
Cdd:COG2884 2 IRFENVSKRYPGG----REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIVSDSAN 234
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElVDRMPKRVLELEDGRLVRDEAR 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-231 |
2.61e-68 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 223.40 E-value: 2.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:COG3638 1 PMLELRNLSKRYPGG----TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAfGFVFQGYHLIPSASAQENV------EMPAIYAGI---PASERHtRARALLERLGLAERTANRPHQLSGGQQQR 159
Cdd:COG3638 77 RLRRRI-GMIFQQFNLVPRLSVLTNVlagrlgRTSTWRSLLglfPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILIT-HDRDVAAR-AKRIIEVRDGEIVSD 231
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNlHQVDLARRyADRIIGLRDGRVVFD 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-282 |
4.25e-67 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 220.35 E-value: 4.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 5 TQPVPLIELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDS 84
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGG-VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 85 DeqawlrreaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIAR 164
Cdd:COG1116 81 D---------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAAR-AKRII--EVRDGEIVSDSAND-ERPa 239
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKtVLFVTHDVDEAVFlADRVVvlSARPGRIVEEIDVDlPRP- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15597586 240 hpsagveRHLQADDlSQRLAEgssepsgaWRAELLEAVRAAWR 282
Cdd:COG1116 231 -------RDRELRT-SPEFAA--------LRAEILDLLREEAE 257
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-241 |
8.04e-66 |
|
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: 225.17 E-value: 8.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 4 ATQPVPLIELRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELD 83
Cdd:COG1123 254 AAAAEPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 84 SDEQAWLRREAfGFVFQG-YH-LIPSASAQENVEMPA-IYAGIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQR 159
Cdd:COG1123 334 RRSLRELRRRV-QMVFQDpYSsLNPRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDE- 236
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEv 492
|
....*..
gi 15597586 237 --RPAHP 241
Cdd:COG1123 493 faNPQHP 499
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-241 |
4.14e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 211.78 E-value: 4.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAw 89
Cdd:COG1126 1 MIEIENLHKSFGDL-----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREaFGFVFQGYHLIPSASAQENVEMPAIYA-GIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:COG1126 75 LRRK-VGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD----RDVaarAKRIIEVRDGEIVSDSANDE---RPAHP 241
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEmgfaREV---ADRVVFMDGGRIVEEGPPEEffeNPQHE 230
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-223 |
6.61e-64 |
|
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: 210.16 E-value: 6.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 13 LRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRR 92
Cdd:TIGR03608 1 LKNISKKFGDK-----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 93 EAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHI 172
Cdd:TIGR03608 76 EKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15597586 173 ILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEV 223
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-221 |
7.53e-64 |
|
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: 210.41 E-value: 7.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeqawl 90
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rreaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03293 75 ----RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15597586 171 HIILADEPTGALDSHSgAEVM--ALLDELASQGHVVILITHDRDVAAR-AKRII 221
Cdd:cd03293 151 DVLLLDEPFSALDALT-REQLqeELLDIWRETGKTVLLVTHDIDEAVFlADRVV 203
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-227 |
1.42e-61 |
|
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: 204.40 E-value: 1.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAW 89
Cdd:TIGR02673 1 MIEFHNVSKAYPGG----VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:TIGR02673 77 LRRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGE 227
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRvAHRVIILDDGR 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-228 |
3.09e-61 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 204.28 E-value: 3.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:PRK11629 4 ILLQCDNLCKRYQ-EGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-229 |
6.57e-61 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 206.85 E-value: 6.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawL 90
Cdd:COG1135 2 IELENLSKTFPTKGGP-VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 R--REAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:COG1135 78 RaaRRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVaarAKRI------IEvrDGEIV 229
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDV---VRRIcdrvavLE--NGRIV 220
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
25-228 |
7.34e-61 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 202.64 E-value: 7.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 25 TPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRREAFGFVFQGYHL 104
Cdd:NF038007 15 TIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQSFNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 105 IPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDS 184
Cdd:NF038007 95 IPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15597586 185 HSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:NF038007 175 KNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-229 |
3.77e-59 |
|
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: 198.57 E-value: 3.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGTpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAW 89
Cdd:cd03258 1 MIELKNVSKVFGDTGG-KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:cd03258 80 ARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-229 |
2.14e-58 |
|
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: 196.19 E-value: 2.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAW 89
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREaFGFVFQGYH--LIPSASAQENVEMPAIYAGIP--ASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVSIAR 164
Cdd:cd03257 80 RRKE-IQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-231 |
2.68e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 193.74 E-value: 2.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEldsDEQAWL 90
Cdd:COG1131 1 IEVRGLTKRYGD-----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR---DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RReaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:COG1131 73 RR--IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIVSD 231
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIVAD 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-228 |
1.70e-56 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 191.15 E-value: 1.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 18 KRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRREAFGF 97
Cdd:PRK10584 13 KKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 98 VFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADE 177
Cdd:PRK10584 93 VFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597586 178 PTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-236 |
2.71e-56 |
|
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: 191.24 E-value: 2.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWL 90
Cdd:cd03256 1 IEVENLSKTYPNG----KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPSASAQENV------EMP---AIYAGIPASERHtRARALLERLGLAERTANRPHQLSGGQQQRVS 161
Cdd:cd03256 77 RRQ-IGMIFQQFNLIERLSVLENVlsgrlgRRStwrSLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDE 236
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAE 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-231 |
6.75e-56 |
|
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: 189.47 E-value: 6.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawL 90
Cdd:COG1122 1 IELENLSFSYPG----GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE---L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAfGFVFQ--GYHLIpSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERtANR-PHQLSGGQQQRVSIARALM 167
Cdd:COG1122 74 RRKV-GLVFQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHL-ADRpPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSD 231
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVAD 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-229 |
3.47e-55 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 188.26 E-value: 3.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:COG1127 4 PMIEVRNLTKSFGDR-----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREaFGFVFQGYHLIPSASAQENVEMPAI-YAGIPASERHTRARALLERLGLAErTANR-PHQLSGGQQQRVSIARAL 166
Cdd:COG1127 79 ELRRR-IGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPG-AADKmPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 167 MNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLtSVVVTHDLDSAFAiADRVAVLADGKII 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-228 |
5.97e-55 |
|
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: 186.58 E-value: 5.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaelDSDEQAW- 89
Cdd:cd03262 1 IEIKNLHKSFGDF-----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL---TDDKKNIn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 -LRREAfGFVFQGYHLIPSASAQENVEMPAIYA-GIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALM 167
Cdd:cd03262 73 eLRQKV-GMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD----RDVaarAKRIIEVRDGEI 228
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEmgfaREV---ADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-227 |
7.19e-54 |
|
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: 183.44 E-value: 7.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 12 ELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawlR 91
Cdd:cd03225 1 ELKNLSFSYPDGARP---ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 REAFGFVFQgyhlipSASAQ-------ENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIAR 164
Cdd:cd03225 74 RRKVGLVFQ------NPDDQffgptveEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGE 227
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-229 |
2.04e-53 |
|
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: 182.33 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeqawL 90
Cdd:cd03259 1 LELKGLSKTYGS-----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03259 70 ERRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALAlADRIAVMNEGRIV 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-251 |
3.45e-53 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 183.08 E-value: 3.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGgNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSdeqAW 89
Cdd:COG1124 1 MLEVRNLSVSYG-QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR---KA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRReAFGFVFQGYH--LIPSASAQENVEMPAIYAGIPASERhtRARALLERLGLAERTANR-PHQLSGGQQQRVSIARAL 166
Cdd:COG1124 77 FRR-RVQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 167 MNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHPSAG 244
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
....*..
gi 15597586 245 VERHLQA 251
Cdd:COG1124 234 YTRELLA 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-228 |
2.78e-52 |
|
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: 179.53 E-value: 2.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWL 90
Cdd:cd03292 1 IEFINVTKTYPNG----TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03292 77 RRK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEI 228
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKElVDTTRHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-241 |
4.69e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 183.38 E-value: 4.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELdsdeQA 88
Cdd:COG3842 4 PALELENVSKRYGD-----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL----PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRReaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:COG3842 75 EKRN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 169 GGHIILADEPTGALDSHS----GAEVMALLDELasqGHVVILITHDRDVA-ARAKRIIEVRDGEIV-SDSAND--ERPAH 240
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLreemREELRRLQREL---GITFIYVTHDQEEAlALADRIAVMNDGRIEqVGTPEEiyERPAT 229
|
.
gi 15597586 241 P 241
Cdd:COG3842 230 R 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-265 |
6.64e-52 |
|
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: 187.42 E-value: 6.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTL-MNILGCLDRPS--SGSYHFAGHDVAELDsd 85
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVP---AVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGGriSGEVLLDGRDLLELS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 eqAWLRREAFGFVFQ--GYHLIPSASAQENVEMPAIyAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIA 163
Cdd:COG1123 78 --EALRGRRIGMVFQdpMTQLNPVTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 164 RALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHP 241
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAP 234
|
250 260
....*....|....*....|....*
gi 15597586 242 SA-GVERHLQADDLSQRLAEGSSEP 265
Cdd:COG1123 235 QAlAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-236 |
3.09e-51 |
|
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: 177.49 E-value: 3.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAW 89
Cdd:TIGR02315 1 MLEVENLSKVYPNG----KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREaFGFVFQGYHLIPSASAQENVEMPAIYA--------GIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVS 161
Cdd:TIGR02315 77 LRRR-IGMIFQHYNLIERLTVLENVLHGRLGYkptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILIT-HDRDVAAR-AKRIIEVRDGEIVSDSANDE 236
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINlHQVDLAKKyADRIVGLKAGEIVFDGAPSE 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-260 |
6.22e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 174.13 E-value: 6.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAw 89
Cdd:PRK09493 1 MIEFKNVSKHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREAfGFVFQGYHLIPSASAQENVEM-PAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:PRK09493 75 IRQEA-GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHPSagver 247
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPP----- 228
|
250
....*....|...
gi 15597586 248 hlqaddlSQRLAE 260
Cdd:PRK09493 229 -------SQRLQE 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-216 |
1.75e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 173.45 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 4 ATQPVPLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVA--- 80
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDL-----EVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ----ELDSDEQAWLR--REAFGFVFQGYHLIPSASAQENV-EMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLS 153
Cdd:COG4598 77 drdgELVPADRRQLQriRTRLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 154 GGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD----RDVAAR 216
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEmgfaRDVSSH 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-241 |
2.18e-49 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 175.24 E-value: 2.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDRP--SSGSYHFAGHDVAELDSDE 86
Cdd:COG0444 1 LLEVRNLKVYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 QAWLRREAFGFVFQ------------GYHLIpsasaqenvEMPAIYAGIPASERHTRARALLERLGL--AERTANR-PHQ 151
Cdd:COG0444 80 LRKIRGREIQMIFQdpmtslnpvmtvGDQIA---------EPLRIHGGLSKAEARERAIELLERVGLpdPERRLDRyPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAAR---------AKRII 221
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLaILFITHDLGVVAEiadrvavmyAGRIV 230
|
250 260
....*....|....*....|.
gi 15597586 222 EVRD-GEIVsdsandERPAHP 241
Cdd:COG0444 231 EEGPvEELF------ENPRHP 245
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-227 |
2.40e-49 |
|
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: 170.06 E-value: 2.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwl 90
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIPSASAQENVEMPaiyagipaserhtrarallerlglaertanrphqLSGGQQQRVSIARALMNGG 170
Cdd:cd03229 74 LRRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGE 227
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-228 |
1.55e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.23 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawL 90
Cdd:COG4619 1 LELEGLSFRVGGK-----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---W 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPsASAQENVEMPAIYAGIPASErhTRARALLERLGLAERTANRP-HQLSGGQQQRVSIARALMNG 169
Cdd:COG4619 73 RRQ-VAYVPQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAAR-AKRIIEVRDGEI 228
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRaVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-229 |
3.51e-48 |
|
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: 168.90 E-value: 3.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLmniLGCLDR--------PSSGSYHFAGHDVAEL 82
Cdd:cd03260 1 IELRDLNVYYG-----DKHALKDISLDIPKGEITALIGPSGCGKSTL---LRLLNRlndlipgaPDEGEVLLDGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 83 DSDEqAWLRREaFGFVFQGYHLIPsASAQENVEMPAIYAGI-PASERHTRARALLERLGLAERTANRPH--QLSGGQQQR 159
Cdd:cd03260 73 DVDV-LELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQgHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARvADRTAFLLNGRLV 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-260 |
4.10e-48 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 172.29 E-value: 4.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGnGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWL 90
Cdd:PRK11153 2 IELKNISKVFPQ-GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERtANR-PHQLSGGQQQRVSIARALMNG 169
Cdd:PRK11153 81 RRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDK-ADRyPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHPSAGVER 247
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
250
....*....|...
gi 15597586 248 HLQADDLSQRLAE 260
Cdd:PRK11153 239 EFIQSTLHLDLPE 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-235 |
2.34e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 167.19 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGcLDRPSSGSYHFAGHDVAEldsdeq 87
Cdd:COG1121 5 PAIELENLTVSYGGR-----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG-LLPPTSGTVRLFGKPPRR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 88 awlRREAFGFVFQgYHLIPS---ASAQENVEMPAIYA----GIPASERHTRARALLERLGLAERtANRP-HQLSGGQQQR 159
Cdd:COG1121 73 ---ARRRIGYVPQ-RAEVDWdfpITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDL-ADRPiGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIVSDSAND 235
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLLNRGLVAHGPPEE 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-229 |
2.76e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 166.73 E-value: 2.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGH--DVAELDSDEQA 88
Cdd:COG4161 3 IQLKNINCFYGSH-----QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGYHLIPSASAQEN-VEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALM 167
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-229 |
7.45e-47 |
|
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: 165.37 E-value: 7.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWL 90
Cdd:cd03261 1 IELRGLTKSFGGR-----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPSASAQENVEMPAIYAGI-PASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:cd03261 76 RRR-MGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIV 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-229 |
9.23e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 165.57 E-value: 9.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGH--DVAELDSDEQA 88
Cdd:PRK11124 3 IQLNGINCFYGAH-----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGYHLIPSASAQEN-VEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALM 167
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-231 |
1.50e-46 |
|
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: 165.22 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAw 89
Cdd:COG1120 1 MLEAENLSVGYGGR-----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lRReaFGFVFQGYHLIPSASAQENVEM---PAIYA-GIPASERHTRARALLERLGLAERtANRP-HQLSGGQQQRVSIAR 164
Cdd:COG1120 75 -RR--IAYVPQEPPAPFGLTVRELVALgryPHLGLfGRPSAEDREAVEEALERTGLEHL-ADRPvDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELA-SQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSD 231
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQ 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-243 |
3.83e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 167.25 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDV-AELDSDEqaw 89
Cdd:COG1118 3 IEVRNISKRFGS-----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lRReaFGFVFQGYHLIPSASAQENVE--MPAiyAGIPASERHTRARALLERL---GLAERtanRPHQLSGGQQQRVSIAR 164
Cdd:COG1118 75 -RR--VGFVFQHYALFPHMTVAENIAfgLRV--RPPSKAEIRARVEELLELVqleGLADR---YPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV-SDSAND--ERPA 239
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALElADRVVVMNQGRIEqVGTPDEvyDRPA 226
|
....
gi 15597586 240 HPSA 243
Cdd:COG1118 227 TPFV 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-241 |
4.88e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 163.77 E-value: 4.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGH--DVAELDSDEQA 88
Cdd:PRK11264 4 IEVKNLVKKFHGQ-----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLR--REAFGFVFQGYHLIPSASAQENV-EMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARA 165
Cdd:PRK11264 79 LIRqlRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD----RDVAARAkriIEVRDGEIVSDSANDERPAHP 241
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEmsfaRDVADRA---IFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-242 |
1.09e-45 |
|
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: 163.20 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGN----------GTPEVEVLKG---------VSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGS 71
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakGKSKEEILKKtgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 72 YHFAGHDVAELDSDEQAWLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQ 151
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRlGDRIAIMKDGRLV 240
|
250
....*....|...
gi 15597586 230 SDSANDERPAHPS 242
Cdd:cd03294 241 QVGTPEEILTNPA 253
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-227 |
1.13e-45 |
|
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: 159.86 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeQAWL 90
Cdd:cd03228 1 IEFKNVSFSYPGRPKP---VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RReAFGFVFQGYHLIpSASAQENVempaiyagipaserhtrarallerlglaertanrphqLSGGQQQRVSIARALMNGG 170
Cdd:cd03228 75 RK-NIAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGE 227
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-226 |
1.17e-45 |
|
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: 161.83 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKR---YGGNGTpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNilgCLDR---PSSGS--YHFAGH--D 78
Cdd:COG4778 3 TLLEVENLSKTftlHLQGGK-RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLK---CIYGnylPDSGSilVRHDGGwvD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 79 VAELDSDEQAWLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERT-ANRPHQLSGGQQ 157
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 158 QRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDG 226
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-229 |
3.70e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 164.48 E-value: 3.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawl 90
Cdd:COG3839 4 LELENVSKSYGG-----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RReaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:COG3839 75 RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVA-ARAKRIIEVRDGEIV 229
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAmTLADRIAVMNDGRIQ 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-241 |
7.89e-45 |
|
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: 160.16 E-value: 7.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGnGTPEVevlKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawL 90
Cdd:cd03295 1 IEFENVTKRYGG-GKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERT-ANR-PHQLSGGQQQRVSIARALMN 168
Cdd:cd03295 74 RRK-IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfADRyPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHP 241
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-241 |
9.77e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 162.59 E-value: 9.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 4 ATQPVPLIELRDIRKRY---GGNGTPEVEVLK---GVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGH 77
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrGGLFGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 78 DVAELDSDEQAWLRREAfGFVFQGyhliPSAS------AQENVEMPAIYAGI-PASERHTRARALLERLGLAERTANR-P 149
Cdd:COG4608 81 DITGLSGRELRPLRRRM-QMVFQD----PYASlnprmtVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRyP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 150 HQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHD----RDVAAR-----AKR 219
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDlsvvRHISDRvavmyLGK 235
|
250 260
....*....|....*....|..
gi 15597586 220 IIEVRDGEIVSdsandERPAHP 241
Cdd:COG4608 236 IVEIAPRDELY-----ARPLHP 252
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-280 |
1.09e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 160.41 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqa 88
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQP-QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlrreafGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:COG4525 79 -------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAA-RAKRIIevrdgeIVSdsanderpAHPSAGVE 246
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALfLATRLV------VMS--------PGPGRIVE 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15597586 247 RHlqADDLSQRLAEGS------SEPS-GAWRAELLEAVRAA 280
Cdd:COG4525 218 RL--ELDFSRRFLAGEdaraikSDPAfIALREELLDIIFAQ 256
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-241 |
1.98e-44 |
|
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: 166.78 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNGTpEVEVLKGVSLSIHAGEFVAIVGASGSGKS-TLMNILGCLDRPS---SGSYHFAGHDVAELDS 84
Cdd:COG4172 5 PLLSVEDLSVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 85 DEQAWLRREAFGFVFQGyhliPSAS-------AQENVEMPAIYAGIPASERHTRARALLERLGL--AERTANR-PHQLSG 154
Cdd:COG4172 84 RELRRIRGNRIAMIFQE----PMTSlnplhtiGKQIAEVLRLHRGLSGAAARARALELLERVGIpdPERRLDAyPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 155 GQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDS 232
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQG 239
|
250
....*....|..
gi 15597586 233 ANDE---RPAHP 241
Cdd:COG4172 240 PTAElfaAPQHP 251
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-229 |
8.34e-44 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 156.57 E-value: 8.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAW 89
Cdd:PRK10908 1 MIRFEHVSKAYLGGR----QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:PRK10908 77 LRRQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIV 229
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHLH 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-229 |
1.07e-43 |
|
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: 156.63 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwl 90
Cdd:cd03300 1 IELENVSKFYGG-----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rreaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03300 74 ----VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 171 HIILADEPTGALD----SHSGAEVMALLDELasqGHVVILITHDRDVA-ARAKRIIEVRDGEIV 229
Cdd:cd03300 150 KVLLLDEPLGALDlklrKDMQLELKRLQKEL---GITFVFVTHDQEEAlTMSDRIAVMNKGKIQ 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-220 |
5.28e-43 |
|
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: 153.79 E-value: 5.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeqa 88
Cdd:COG4133 1 MMLEAENLSCRRGER-----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERhtRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:COG4133 73 --YRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRI 220
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-236 |
5.67e-43 |
|
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: 165.39 E-value: 5.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeQAWL 90
Cdd:COG2274 474 IELENVSFRYPGDSPP---VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RReAFGFVFQGYHLIpSASAQENVEMPAIYAGIpaserhTRARALLERLGLAERTANRPH-----------QLSGGQQQR 159
Cdd:COG2274 548 RR-QIGVVLQDVFLF-SGTIRENITLGDPDATD------EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELAsQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEE 695
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-229 |
1.04e-42 |
|
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: 162.62 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeqA 88
Cdd:COG4988 335 PSIELEDVSFSYPG----GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA--S 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WlrREAFGFVFQGYHLiPSASAQENVEMpaiyAGIPASErhTRARALLERLGLAERTANRPH-----------QLSGGQQ 157
Cdd:COG4988 409 W--RRQIAWVPQNPYL-FAGTIRENLRL----GRPDASD--EELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 158 QRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELAsQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-231 |
1.47e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 154.51 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAeldSDEQAWL 90
Cdd:TIGR04520 1 IEVENVSFSYPESEKP---ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL---DEENLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGyhliP-----SASAQENVempaiyA------GIPASERHTRARALLERLGLAERTANRPHQLSGGQQQR 159
Cdd:TIGR04520 75 IRKKVGMVFQN----PdnqfvGATVEDDV------AfglenlGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 160 VSIARAL-MNGGHIILaDEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAARAKRIIEVRDGEIVSD 231
Cdd:TIGR04520 145 VAIAGVLaMRPDIIIL-DEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-236 |
1.72e-41 |
|
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: 159.16 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 4 ATQPVPLIELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELD 83
Cdd:COG4987 327 PAPGGPSLELEDVSFRYPGAGRP---VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 84 SDEqawlRREAFGFVFQGYHLIpSASAQENVEMpaiyAGIPASERhtRARALLERLGLAERTANRPH-----------QL 152
Cdd:COG4987 404 EDD----LRRRIAVVPQRPHLF-DTTLRENLRL----ARPDATDE--ELWAALERVGLGDWLAALPDgldtwlgeggrRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 153 SGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELAsQGHVVILITHDRDVAARAKRIIEVRDGEIVSDS 232
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
....
gi 15597586 233 ANDE 236
Cdd:COG4987 552 THEE 555
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-228 |
2.63e-41 |
|
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: 147.93 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEldsdEQAWL 90
Cdd:cd03230 1 IEVRNLSKRYGKK-----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPSASAQENVEmpaiyagipaserhtrarallerlglaertanrphqLSGGQQQRVSIARALMNGG 170
Cdd:cd03230 72 KRR-IGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEI 228
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-243 |
3.63e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 150.50 E-value: 3.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 15 DIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEL-DSD-------- 85
Cdd:PRK10619 10 DLHKRYG-----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrDKDgqlkvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 EQAWLRREAFGFVFQGYHLIPSASAQENV-EMPAIYAGIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVSIA 163
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 164 RALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHPS 242
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
.
gi 15597586 243 A 243
Cdd:PRK10619 245 S 245
|
|
| MacB_PCD |
pfam12704 |
MacB-like periplasmic core domain; This family represents the periplasmic core domain found in ... |
291-508 |
4.68e-41 |
|
MacB-like periplasmic core domain; This family represents the periplasmic core domain found in a variety of ABC transporters. The structure of this family has been solved for the MacB protein. Some structural similarity was found to the periplasmic domain of the AcrB multidrug efflux transporter.
Pssm-ID: 463676 [Multi-domain] Cd Length: 211 Bit Score: 148.83 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 291 TALTLLGIIIGVASVVVMLAVGEGSKRQVMAQMgAFGSNIIYLSGYSPNPRAPMGIVSSDDVAAIATLPQVKKVMPVNGg 370
Cdd:pfam12704 1 TALTVLGIAIGVAAVIAILSLGDGLLSAVPEQI-SDSDNLVVVQPGAAGGGGTRPPLSDPDAEALRRAVPVEAVAPVVS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 371 elVVRYGNIDY--HAYVGGNNTDFPEILNWPVAEGSYFTERDEDAATTVAVIGYKVRKKLFGSANPIGRYILIENVPFQV 448
Cdd:pfam12704 79 --TVRYGNSTTerLVTVVGVDPDFFKVFGLPLAEGRFFTEADVLGGPNVVVLGESLAEKLFGGDDPVGKTIRLNGQPFTV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 449 IGVLAEKGSSSGDkdaDNRIAIPYSAASIRLFGTRNpeYVIIAAADAQRVHQAERAIDQL 508
Cdd:pfam12704 157 VGVLPDFPGSDGG---GDLVYVPLTTLQRRLGDSVS--TILVRLKDGADLAAAAAELRAL 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-236 |
4.81e-41 |
|
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: 149.62 E-value: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeqaw 89
Cdd:COG4555 1 MIEVENLSKKYGK-----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:COG4555 72 -ARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHImQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-227 |
4.88e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 146.62 E-value: 4.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 12 ELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawlR 91
Cdd:cd00267 1 EIENLSFRYGGR-----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 REAFGFVFQgyhlipsasaqenvempaiyagipaserhtrarallerlglaertanrphqLSGGQQQRVSIARALMNGGH 171
Cdd:cd00267 72 RRRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 172 IILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAK-RIIEVRDGE 227
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-221 |
1.18e-40 |
|
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: 148.35 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwl 90
Cdd:cd03219 1 LEVRGLTKRFGG-----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIPSASAQENVEMPA--------IYAGIPASERHTRARA--LLERLGLAERTANRPHQLSGGQQQRV 160
Cdd:cd03219 74 -RLGIGRTFQIPRLFPELTVLENVMVAAqartgsglLLARARREEREARERAeeLLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 161 SIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRII 221
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVT 214
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-278 |
1.32e-40 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 151.73 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 7 PVPLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDe 86
Cdd:TIGR03265 1 SSPYLSIDNIRKRFG-----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 qawlRREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARAL 166
Cdd:TIGR03265 75 ----KRD-YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 167 MNGGHIILADEPTGALDS----HSGAEVMALLDELasqGHVVILITHDRDVA-ARAKRIIEVRDGEIVSDSANDE---RP 238
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDArvreHLRTEIRQLQRRL---GVTTIMVTHDQEEAlSMADRIVVMNHGVIEQVGTPQEiyrHP 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15597586 239 AHP--------------SAGVERHLQADDLSQRLAEGSSEPSGAWRAelleAVR 278
Cdd:TIGR03265 227 ATPfvadfvgevnwlpgTRGGGSRARVGGLTLACAPGLAQPGASVRL----AVR 276
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-231 |
1.58e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 146.04 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 12 ELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLR 91
Cdd:cd03214 1 EVENLSVGYGGR-----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 reafGFVFQgyhlipsasaqenvempaiyagipaserhtraraLLERLGLAErTANRP-HQLSGGQQQRVSIARALMNGG 170
Cdd:cd03214 76 ----AYVPQ----------------------------------ALELLGLAH-LADRPfNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELA-SQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSD 231
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-229 |
7.23e-40 |
|
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: 145.09 E-value: 7.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 12 ELRDIRKRYGGNGtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAeldsdeqAWLR 91
Cdd:cd03226 1 RIENISFSYKKGT----EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 REAFGFVFQ--GYHLIPSASAQEnvempaIYAGIP-ASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:cd03226 70 RKSIGYVMQdvDYQLFTDSVREE------LLLGLKeLDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
46-242 |
1.07e-39 |
|
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: 148.41 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 46 IVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELdsdeQAWLRreAFGFVFQGYHLIPSASAQENVEMPAIYAGIPA 125
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV----PPHLR--HINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 126 SERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALD----SHSGAEVMALLDELasqG 201
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---G 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15597586 202 HVVILITHDRDVA-ARAKRIIEVRDGEIVSDSANDERPAHPS 242
Cdd:TIGR01187 152 ITFVFVTHDQEEAmTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-228 |
1.88e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 149.33 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 1 MENATQPVPLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVA 80
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGK-----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELDSDeqawlRREAfGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRV 160
Cdd:PRK09452 80 HVPAE-----NRHV-NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 161 SIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVA-ARAKRIIEVRDGEI 228
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-242 |
3.83e-39 |
|
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: 144.40 E-value: 3.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeqawL 90
Cdd:cd03296 3 IEVRNVSKRFGD-----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIPSASAQENV----EMPAIYAGIPASERHTRARALLERLGLaERTANR-PHQLSGGQQQRVSIARA 165
Cdd:cd03296 72 QERNVGFVFQHYALFRHMTVFDNVafglRVKPRSERPPEAEIRAKVHELLKLVQL-DWLADRyPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVV-ILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHPS 242
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTtVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-266 |
4.85e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 144.44 E-value: 4.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 5 TQPVPLIeLRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYhFAGHdvAELDS 84
Cdd:PRK11247 8 NQGTPLL-LNAVSKRYGER-----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--APLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 85 deqawlRREAFGFVFQGYHLIPSASAQENVEMpaiyaGIPASERhTRARALLERLGLAERTANRPHQLSGGQQQRVSIAR 164
Cdd:PRK11247 79 ------AREDTRLMFQDARLLPWKKVIDNVGL-----GLKGQWR-DAALQALAAVGLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVA-ARAKRIIEVRDGEIVSDSAND-ERPAHP 241
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAvAMADRVLLIEEGKIGLDLTVDlPRPRRR 226
|
250 260
....*....|....*....|....*
gi 15597586 242 SAGVERHLQADDLSQRLAEGSSEPS 266
Cdd:PRK11247 227 GSARLAELEAEVLQRVMSRGESEPT 251
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
31-179 |
1.04e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.09 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDvaeLDSDEQAWLRREaFGFVFQGYHLIPSASA 110
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 111 QENVEMPAIYAGIPASERHTRARALLERLGL----AERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPT 179
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-230 |
1.73e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.62 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaeldSDEQA 88
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY---ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL----SEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGyhliPS-----ASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIA 163
Cdd:PRK13635 77 WDVRRQVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 164 RALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAARAKRIIEVRDGEIVS 230
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-231 |
1.81e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.01 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 7 PVPLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaELDSDE 86
Cdd:COG1129 1 AEPLLEMRGISKSFGG-----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 QAwlRREAFGFVFQGYHLIPSASAQENV---EMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIA 163
Cdd:COG1129 75 DA--QAAGIAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 164 RALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIVSD 231
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDeVFEIADRVTVLRDGRLVGT 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-229 |
2.08e-38 |
|
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: 139.49 E-value: 2.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAeldsdeqawl 90
Cdd:cd03216 1 LELRGITKRFGG-----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rreafgfvfqgyhlipSASAQEnvempAIYAGIpaserhtrarallerlglaeRTAnrpHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03216 66 ----------------FASPRD-----ARRAGI--------------------AMV---YQLSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIV 229
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-241 |
2.19e-38 |
|
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: 149.45 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNG------TPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTL-MNILGCLdrPSSGSYHFAGHDVAE 81
Cdd:COG4172 274 PLLEARDLKVWFPIKRglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 82 LDSDEQAWLRREaFGFVFQ---GyHLIPSASAQENVEMP-AIYA-GIPASERHTRARALLERLGLAERTANR-PHQLSGG 155
Cdd:COG4172 352 LSRRALRPLRRR-MQVVFQdpfG-SLSPRMTVGQIIAEGlRVHGpGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 156 QQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHD-RDVAARAKRIIEVRDGEIV-SDS 232
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDlAVVRALAHRVMVMKDGKVVeQGP 509
|
250
....*....|.
gi 15597586 233 AND--ERPAHP 241
Cdd:COG4172 510 TEQvfDAPQHP 520
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-221 |
3.96e-38 |
|
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: 142.10 E-value: 3.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:COG0411 3 PLLEVRGLTKRFGG-----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlRReafGFV--FQGYHLIPSASAQENVEMPAIYA-------------GIPASERHTRARA--LLERLGLAERTANRPHQ 151
Cdd:COG0411 78 --RL---GIArtFQNPRLFPELTVLENVLVAAHARlgrgllaallrlpRARREEREARERAeeLLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRII 221
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGlADRIV 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-229 |
5.79e-38 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 140.08 E-value: 5.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwl 90
Cdd:cd03301 1 VELENVTKRFG-----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rreaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03301 74 ----IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVA-ARAKRIIEVRDGEIV 229
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQIQ 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-249 |
2.01e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 139.12 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQawl 90
Cdd:COG3840 2 LRLDDLTYRYGD-------FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rreAFGFVFQGYHLIPSASAQENvempaIYAGI-----PASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARA 165
Cdd:COG3840 72 ---PVSMLFQENNLFPHLTVAQN-----IGLGLrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEVMALLDELA-SQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPA-HPS 242
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDgEPP 223
|
....*..
gi 15597586 243 AGVERHL 249
Cdd:COG3840 224 PALAAYL 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-231 |
9.39e-37 |
|
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: 137.91 E-value: 9.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGS------YHFAGHDVAEL 82
Cdd:COG1119 2 PLLELRNVTVRRGGK-----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 83 dsdeqawlrREAFGFV---FQGYHLiPSASAqENVEMPAIYAGI-----PASERHTRARALLERLGLAERtANRP-HQLS 153
Cdd:COG1119 77 ---------RKRIGLVspaLQLRFP-RDETV-LDVVLSGFFDSIglyrePTDEQRERARELLELLGLAHL-ADRPfGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 154 GGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDR-DVAARAKRIIEVRDGEIVSD 231
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHVeEIPPGITHVLLLKDGRVVAA 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-221 |
1.04e-36 |
|
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: 136.51 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 12 ELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLdRPSSGSYHFAGHDVAEldsdeqawl 90
Cdd:cd03235 1 EVEDLTVSYGGH-----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFGKPLEK--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIPS--ASAQENVEMPAIY-----AGIPASERHtRARALLERLGLAErTANRP-HQLSGGQQQRVSI 162
Cdd:cd03235 66 ERKRIGYVPQRRSIDRDfpISVRDVVLMGLYGhkglfRRLSKADKA-KVDEALERVGLSE-LADRQiGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 163 ARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRII 221
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVL 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-229 |
1.39e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.92 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 1 MENATQPVPL------IELRDIRKRYGGngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHF 74
Cdd:COG1132 324 IPDPPGAVPLppvrgeIEFENVSFSYPG----DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 75 AGHDVAELDsdeQAWLRReAFGFVFQGYHLIpSASAQENVempaIYAGIPASE-------RHTRARALLERL--GLAERT 145
Cdd:COG1132 400 DGVDIRDLT---LESLRR-QIGVVPQDTFLF-SGTIRENI----RYGRPDATDeeveeaaKAAQAHEFIEALpdGYDTVV 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 146 ANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRD 225
Cdd:COG1132 471 GERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDD 549
|
....
gi 15597586 226 GEIV 229
Cdd:COG1132 550 GRIV 553
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-213 |
3.11e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 138.94 E-value: 3.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 6 QPVPLIELRDIRKRY---GGNGTPE--VEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVA 80
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkRGLFKPErlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELDSDEQAwLRREAFGFVFQGYH--LIPSASAQENVEMP-AIYAGIPASERHTRARALLERLGLAERTANR-PHQLSGGQ 156
Cdd:PRK11308 81 KADPEAQK-LLRQKIQIVFQNPYgsLNPRKKVGQILEEPlLINTSLSAAERREKALAMMAKVGLRPEHYDRyPHMFSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 157 QQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDV 213
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSV 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-236 |
5.17e-36 |
|
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: 134.80 E-value: 5.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAElDSDEQawl 90
Cdd:cd03265 1 IEVENLVKKYGDF-----EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREV--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03265 72 -RRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVA-ARAKRIIEVRDGEIVSDSANDE 236
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-251 |
5.36e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 136.36 E-value: 5.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNG----TPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDS 84
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGlsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 85 DEQAWLRREAfGFVFQGYhliPSA-SAQENVEmpAIYA-------GIPASERHTRARALLERLGLAERTANR-PHQLSGG 155
Cdd:PRK10419 82 AQRKAFRRDI-QMVFQDS---ISAvNPRKTVR--EIIReplrhllSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 156 QQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHD-RDVAARAKRIIEVRDGEIVSDSA 233
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDlRLVERFCQRVMVMDNGQIVETQP 235
|
250 260
....*....|....*....|
gi 15597586 234 --NDERPAHPSAgveRHLQA 251
Cdd:PRK10419 236 vgDKLTFSSPAG---RVLQN 252
|
|
| LolE |
COG4591 |
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ... |
413-662 |
6.82e-36 |
|
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443648 [Multi-domain] Cd Length: 283 Bit Score: 136.59 E-value: 6.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 413 AATTVAVIGYKVRKKLfgsANPIGRYILI-------ENVPFQVIGVLaekgsSSGDKDADNRIA-IPYSAASiRLFGTRN 484
Cdd:COG4591 31 KASDEVVLGEGLAKKL---GLKVGDTITLispdgspKTRRFTVVGIF-----ESGGYELDGSLVyVPLETAQ-ELLGLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 485 -PEYVIIAAADAQRVHQAERAIDQLMlrlhrgqRDYELTNNAAMIQAEAKTQNTLSLMLGSIAAISLLVGGIGVMNIMLM 563
Cdd:COG4591 102 qVSGILVKLKDGADAEAVAAALEAAL-------PGLEVKTWRELNAALFSALKTEKLILLLILLLILLVAAFNIVNTLLM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 564 TVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALALCIGGVL---------LLGQVAVAFSLSAIVGAFS 634
Cdd:COG4591 175 SVLERTREIGILKALGASRRQIRRIFLLEGLLLGLIGGLLGLLLGLLLALLLnallgillpFIFALPVSLSPSDVLLALL 254
|
250 260
....*....|....*....|....*...
gi 15597586 635 CALVTGLVFGFMPARKAAQLDPVAALAS 662
Cdd:COG4591 255 LALLISLLASLYPARRAARLDPVEALRG 282
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-231 |
9.32e-36 |
|
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: 134.25 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawl 90
Cdd:cd03245 3 IEFRNVSFSYPNQ---EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIpSASAQENVEMPAIYAgipASERHTRAralLERLGLAERTANRPH-----------QLSGGQQQR 159
Cdd:cd03245 76 LRRNIGYVPQDVTLF-YGTLRDNITLGAPLA---DDERILRA---AELAGVTDFVNKHPNgldlqigergrGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASqGHVVILITHDRDVAARAKRIIEVRDGEIVSD 231
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
31-226 |
1.27e-35 |
|
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: 134.13 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwlrreafgfVFQGYHLIPSASA 110
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 111 QENVEMP--AIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGA 188
Cdd:TIGR01184 72 RENIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15597586 189 EVMALLDELASQGHV-VILITHDRDVAA-RAKRIIEVRDG 226
Cdd:TIGR01184 152 NLQEELMQIWEEHRVtVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-231 |
3.45e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 135.21 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgNGTP-EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFA-GHDVAELDSDEQA 88
Cdd:PRK13651 3 IKVKNIVKIFN-KKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 W--------------------LRREAfGFVFQ--GYHLIpSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTA 146
Cdd:PRK13651 82 KvleklviqktrfkkikkikeIRRRV-GVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 147 NR-PHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVR 224
Cdd:PRK13651 160 QRsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDnVLEWTKRTIFFK 239
|
....*..
gi 15597586 225 DGEIVSD 231
Cdd:PRK13651 240 DGKIIKD 246
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-229 |
4.85e-35 |
|
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: 132.17 E-value: 4.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGcLDRPSSGSYHFAGHDVAELDSDEQAw 89
Cdd:cd03224 1 LEVENLNAGYG-----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMG-LLPPRSGSIRFDGRDITGLPPHERA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lrREAFGFVFQGYHLIPSASAQENVEMpAIYAGIPASERHTRAR--ALLERlgLAERTANRPHQLSGGQQQRVSIARALM 167
Cdd:cd03224 74 --RAGIGYVPEGRRIFPELTVEENLLL-GAYARRRAKRKARLERvyELFPR--LKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-229 |
5.76e-35 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 131.55 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFvAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAElDSDEQawl 90
Cdd:cd03264 1 LQLENLTKRYGKK-----RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKL--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03264 71 -RRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASqGHVVILITHD-RDVAARAKRIIEVRDGEIV 229
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-231 |
1.74e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 131.78 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNIL-GCLdRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:COG4559 1 MLEAENLSVRLGGR-----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLR-------REAFGFvfqgyhlipsaSAQENVEMPAIYAGIPASERHTRARALLERLGLAERtANRP-HQLSGGQQQRV 160
Cdd:COG4559 75 RRRavlpqhsSLAFPF-----------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHL-AGRSyQTLSGGEQQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 161 SIARAL-------MNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSD 231
Cdd:COG4559 143 QLARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQ 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-229 |
2.53e-34 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 130.53 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEvLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeqawl 90
Cdd:cd03299 1 LKVENLSKDWK-----EFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03299 70 -KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHD-RDVAARAKRIIEVRDGEIV 229
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVtVLHVTHDfEEAWALADKVAIMLNGKLI 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-229 |
4.58e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 136.31 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaELDSDEQA 88
Cdd:COG3845 4 PALELRGITKRFGG-----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlRREAFGFVFQGYHLIPSASAQENVEM---PAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARA 165
Cdd:COG3845 78 --IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIV 229
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKlREVMAIADRVTVLRRGKVV 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-210 |
5.47e-34 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 130.20 E-value: 5.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqaw 89
Cdd:PRK11248 1 MLQISHLYADYGGK-----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lrreafGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:PRK11248 73 ------GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHD 210
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHD 188
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-229 |
5.98e-34 |
|
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: 129.16 E-value: 5.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAeldsdEQAWL 90
Cdd:cd03263 1 LQIRNLTKTYKKGTKP---AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-----TDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLaERTANRP-HQLSGGQQQRVSIARALMNG 169
Cdd:cd03263 73 ARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL-TDKANKRaRTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-236 |
7.89e-34 |
|
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: 129.20 E-value: 7.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeqaWL 90
Cdd:cd03249 1 IEFKNVSFRYPSR--PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR---WL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIpSASAQENVEMPAIYAGIPASERHTRARALLERL-----GLAERTANRPHQLSGGQQQRVSIARA 165
Cdd:cd03249 76 RSQ-IGLVSQEPVLF-DGTIAENIRYGKPDATDEEVEEAAKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEVMALLDElASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDR-AMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-231 |
1.06e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 129.51 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNIL-GCLdRPSSGSYHFAGHDVAELDSDEQ 87
Cdd:PRK13548 1 AMLEARNLSVRLGGR-----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 88 AwlRREA-------FGFVFqgyhlipsaSAQENVEMpaiyAGIPASERHTRARAL----LERLGLAErTANRP-HQLSGG 155
Cdd:PRK13548 75 A--RRRAvlpqhssLSFPF---------TVEEVVAM----GRAPHGLSRAEDDALvaaaLAQVDLAH-LAGRDyPQLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 156 QQQRVSIARALM------NGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAAR-AKRIIEVRDGE 227
Cdd:PRK13548 139 EQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLaVIVVLHDLNLAARyADRIVLLHQGR 218
|
....
gi 15597586 228 IVSD 231
Cdd:PRK13548 219 LVAD 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
41-232 |
1.19e-33 |
|
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: 128.18 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 41 GEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFagHDVAELDSDEQAWL--RREAFGFVFQGYHLIPSASAQENVEMpa 118
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL--NGTVLFDSRKKINLppQQRKIGLVFQQYALFPHLNVRENLAF-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 119 IYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELA 198
Cdd:cd03297 99 GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 15597586 199 SQGH-VVILITHDRDVAAR-AKRIIEVRDGEIVSDS 232
Cdd:cd03297 179 KNLNiPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-236 |
1.81e-33 |
|
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: 128.12 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawL 90
Cdd:cd03251 1 VEFKNVTFRYPGDGPP---VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIpSASAQENVEmpaiYAGIPASERHTRARA-------LLERL--GLAERTANRPHQLSGGQQQRVS 161
Cdd:cd03251 75 RRQ-IGLVSQDVFLF-NDTVAENIA----YGRPGATREEVEEAAraanaheFIMELpeGYDTVIGERGVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEE 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-241 |
2.42e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 128.51 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 7 PVPLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAG-----HDVAE 81
Cdd:PRK11701 3 DQPLLSVRGLTKLYGP-----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 82 LDSDEQAWLRREAFGFVFQ----GyhLIPSASAQENVEMPAIYAGipasERH---TRARAL--LERLGL-AERTANRPHQ 151
Cdd:PRK11701 78 LSEAERRRLLRTEWGFVHQhprdG--LRMQVSAGGNIGERLMAVG----ARHygdIRATAGdwLERVEIdAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVaAR--AKRIIEVRDGEI 228
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAV-ARllAHRLLVMKQGRV 230
|
250
....*....|....*.
gi 15597586 229 VSDSAND---ERPAHP 241
Cdd:PRK11701 231 VESGLTDqvlDDPQHP 246
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
10-240 |
2.72e-33 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 128.18 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLmniLGCLDR-----PS---SGSYHFAGHDVAE 81
Cdd:TIGR00972 1 AIEIENLNLFYGEK-----EALKNINLDIPKNQVTALIGPSGCGKSTL---LRSLNRmndlvPGvriEGKVLFDGQDIYD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 82 LDSDEQAwLRREaFGFVFQGYHLIPsASAQENVEM-PAIYAGIPASERHTRARALLERLGLAERTANRPHQ----LSGGQ 156
Cdd:TIGR00972 73 KKIDVVE-LRRR-VGMVFQKPNPFP-MSIYDNIAYgPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDsalgLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 157 QQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQgHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSAND 235
Cdd:TIGR00972 150 QQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARiSDRTAFFYDGELVEYGPTE 228
|
....*...
gi 15597586 236 ---ERPAH 240
Cdd:TIGR00972 229 qifTNPKE 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-207 |
4.79e-33 |
|
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: 127.02 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGcLDRPSSGSYHFAGHDVAELDSDEQ 87
Cdd:COG0410 2 PMLEVENLHAGYG-----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 88 AwlrREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRAR--ALLERLglAERTANRPHQLSGGQQQRVSIARA 165
Cdd:COG0410 76 A---RLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERvyELFPRL--KERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15597586 166 LMNGGHIILADEPTGALdshsgA-----EVMALLDELASQGHVVILI 207
Cdd:COG0410 151 LMSRPKLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLV 192
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-228 |
6.86e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.82 E-value: 6.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSdeqawl 90
Cdd:PRK10851 3 IEIANIKKSFG-----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIPSASAQENVEMpaiyaGIPASERHTRARA---------LLERLGLAeRTANR-PHQLSGGQQQRV 160
Cdd:PRK10851 72 RDRKVGFVFQHYALFRHMTVFDNIAF-----GLTVLPRRERPNAaaikakvtqLLEMVQLA-HLADRyPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 161 SIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEI 228
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-229 |
8.28e-33 |
|
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: 126.58 E-value: 8.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeQAWL 90
Cdd:cd03253 1 IEFENVTFAYD----PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RReAFGFVFQG--------YHLI----PSASaQENVEMPAIYAGIpaserHTRARALLErlGLAERTANRPHQLSGGQQQ 158
Cdd:cd03253 74 RR-AIGVVPQDtvlfndtiGYNIrygrPDAT-DEEVIEAAKAAQI-----HDKIMRFPD--GYDTIVGERGLKLSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 159 RVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-223 |
1.23e-32 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 132.41 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 7 PVPLIELRDIRKRYGGNGtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDe 86
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRR----PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 qAWLRReaFGFVFQGYHLIPsASAQENVEMPAIYAGIPASERHTRARALLE-----RLGLAERTANRPHQLSGGQQQRVS 161
Cdd:TIGR02857 393 -SWRDQ--IAWVPQHPFLFA-GTIAENIRLARPDASDAEIREALERAGLDEfvaalPQGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELAsQGHVVILITHDRDVAARAKRIIEV 223
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-231 |
1.49e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 127.13 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNG-TPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELdsdEQA 88
Cdd:PRK13633 4 MIKCKNVSYKYESNEeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE---ENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGY-HLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALM 167
Cdd:PRK13633 81 WDIRNKAGMVFQNPdNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAARAKRIIEVRDGEIVSD 231
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGItIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-229 |
2.11e-32 |
|
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: 128.68 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 34 VSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaeLDSDEQAWL---RReAFGFVFQGYHLIPSASA 110
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLpphRR-RIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 111 QENVEmpaiYA--GIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGA 188
Cdd:COG4148 95 RGNLL----YGrkRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15597586 189 EVMALLDELASQGHV-VILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:COG4148 171 EILPYLERLRDELDIpILYVSHSLDEVARlADHVVLLEQGRVV 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-230 |
2.77e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 131.34 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 13 LRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFA-GHDVAELDSDEQAWLR 91
Cdd:COG0488 1 LENLSKSFGGR-----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 REAFGFVFQG----------YHLIPSASAQENVEMPAI------YAGIPASERHTRARALLERLGLAERTANRP-HQLSG 154
Cdd:COG0488 76 LTVLDTVLDGdaelraleaeLEELEAKLAEPDEDLERLaelqeeFEALGGWEAEARAEEILSGLGFPEEDLDRPvSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 155 GQQQRVSIARALMNGGHIILADEPTGALDSHSgaeVMALLDELASQGHVVILITHDRD----VaarAKRIIEVRDGEIVS 230
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPGTVLVVSHDRYfldrV---ATRILELDRGKLTL 229
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
399-660 |
4.24e-32 |
|
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.
Pssm-ID: 274576 [Multi-domain] Cd Length: 803 Bit Score: 133.02 E-value: 4.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 399 PVAEGSYFTERDEDAATTVAVIGYKVRKKLFGSANPIGRYILIEN---VPFQVIGVLAEKGSSSGDKDADNRIAIPYSAA 475
Cdd:TIGR03434 543 PLLRGRDFTERDTAGSPPVAIVNEAFARRYFPGEDPIGKRIRLGGddgPWFEIVGVVGDVRYAGLDEPPRPEVYLPYAQS 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 476 sirlfGTRNPEYVIIAAAD----AQRVHQAERAIDqlmlrlhRGQRDYELTNNAAMIQAEAKTQNTLSLMLGSIAAISLL 551
Cdd:TIGR03434 623 -----PDRGMTLVVRTAGDpaalAAAVRRAVRAID-------PNLPVYDVRTMEEQVDRSLAQERFLALLLGLFAALALL 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 552 VGGIGVMNIMLMTVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALALCIGGVL--LLGQVAvAFSLSAI 629
Cdd:TIGR03434 691 LAAIGLYGVLAYSVAQRTREIGIRMALGAQRGDVLRLVLRQGLRLAAAGLAIGLAAALALARLLasLLFGVS-PTDPLTF 769
|
250 260 270
....*....|....*....|....*....|.
gi 15597586 630 VGAFSCALVTGLVFGFMPARKAAQLDPVAAL 660
Cdd:TIGR03434 770 AAVAALLLAVALLACYLPARRAARVDPMIAL 800
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-264 |
6.31e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 124.81 E-value: 6.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgNGTP-EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELdSDEqaw 89
Cdd:COG1101 2 LELKNLSKTFN-PGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEY--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lRREAF-GFVFQ----GyhLIPSASAQENVEMPA-------IYAGIPASERHtRARALLERL--GLAERTANRPHQLSGG 155
Cdd:COG1101 77 -KRAKYiGRVFQdpmmG--TAPSMTIEENLALAYrrgkrrgLRRGLTKKRRE-LFRELLATLglGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 156 QQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHD-RDVAARAKRIIEVRDGEIVSDSA 233
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLtTLMVTHNmEQALDYGNRLIMMHEGRIILDVS 232
|
250 260 270
....*....|....*....|....*....|.
gi 15597586 234 NDERpahpsagveRHLQADDLSQRLAEGSSE 264
Cdd:COG1101 233 GEEK---------KKLTVEDLLELFEEIRGE 254
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-236 |
1.17e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.42 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGgNGTpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGhdvAELDSDEQAW 89
Cdd:PRK13639 1 ILETRDLKYSYP-DGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG---EPIKYDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LR-REAFGFVFQGY-HLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALM 167
Cdd:PRK13639 74 LEvRKTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIVSDSANDE 236
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDlVPVYADKVYVMSDGKIIKEGTPKE 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-242 |
2.70e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 125.72 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYggNGTPEVEvlkGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSdeqa 88
Cdd:PRK11607 18 PLLEIRNLTKSF--DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:PRK11607 89 --YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 169 GGHIILADEPTGALDSHSgAEVMAL--LDELASQGHVVILITHDRDVA-ARAKRIIEVRDGEIVSDSANDERPAHPS 242
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKL-RDRMQLevVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-231 |
7.52e-31 |
|
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: 119.91 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwl 90
Cdd:cd03298 1 VRLDKIRFSYG-------EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rreaFGFVFQGYHLIPSASAQENVEMpAIYAGIPASERHTRA-RALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:cd03298 72 ----VSMLFQENNLFAHLTVEQNVGL-GLSPGLKLTAEDRQAiEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSD 231
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQ 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-222 |
8.72e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.89 E-value: 8.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 12 ELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDRP--SSGSYHFAGHDVAELdsdeQA 88
Cdd:COG4136 3 SLENLTITLGG-----RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTAL----PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRReaFGFVFQGYHLIPSASAQENVEMpAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:COG4136 74 EQRR--IGILFQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMAL-LDELASQGHVVILITHDRDVAARAKRIIE 222
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAPAAGRVLD 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-259 |
1.03e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 121.86 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 24 GTP-EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAG-HDVAELDSDEQAWLRREAfGFVFQg 101
Cdd:PRK13641 15 GTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyHITPETGNKNLKKLRKKV-SLVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 102 yhlIPSASAQENVEMPAIYAG---IPASERHTRARAL--LERLGLAERTANR-PHQLSGGQQQRVSIARALMNGGHIILA 175
Cdd:PRK13641 93 ---FPEAQLFENTVLKDVEFGpknFGFSEDEAKEKALkwLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 176 DEPTGALDSHSGAEVMALLDELASQGHVVILITHDR-DVAARAKRIIEVRDGEIVSDSANDERPAHPSaGVERHLQADDL 254
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIKHASPKEIFSDKE-WLKKHYLDEPA 248
|
....*
gi 15597586 255 SQRLA 259
Cdd:PRK13641 249 TSRFA 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-221 |
1.78e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 19 RYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHdvaeldsdeqawlRREAFgfV 98
Cdd:NF040873 1 GYGGR-----PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-------------ARVAY--V 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 99 FQGYHLIPS--ASAQENVEMpAIYAGIPASERHTRA-RAL----LERLGLAERTANRPHQLSGGQQQRVSIARALMNGGH 171
Cdd:NF040873 61 PQRSEVPDSlpLTVRDLVAM-GRWARRGLWRRLTRDdRAAvddaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15597586 172 IILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRII 221
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-236 |
2.03e-30 |
|
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: 119.51 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSdeqAWL 90
Cdd:cd03252 1 ITFEHVRFRYKPDGP---VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP---AWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREaFGFVFQGYHLIPS------ASAQENVEMPAIYAGIPASERHTRARALleRLGLAERTANRPHQLSGGQQQRVSIAR 164
Cdd:cd03252 75 RRQ-VGVVLQENVLFNRsirdniALADPGMSMERVIEAAKLAGAHDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDE 222
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-236 |
2.22e-30 |
|
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: 127.29 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawl 90
Cdd:TIGR03375 464 IEFRNVSFAYPGQETP---ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD---- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIpSASAQENVEMpaiyaGIPASERHTRARALlERLGLAERTANRPH-----------QLSGGQQQR 159
Cdd:TIGR03375 537 LRRNIGYVPQDPRLF-YGTLRDNIAL-----GAPYADDEEILRAA-ELAGVTEFVRRHPDgldmqigergrSLSGGQRQA 609
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQ 685
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
2.23e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.61 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 1 MENAtqpvplIELRDIRKRYGgNGTpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVA 80
Cdd:PRK13647 1 MDNI------IEVEDLHFRYK-DGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 EldsDEQAWLRREAfGFVFQGYH-LIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQR 159
Cdd:PRK13647 71 A---ENEKWVRSKV-GLVFQDPDdQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSAN 234
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-229 |
3.22e-30 |
|
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: 118.15 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeqawl 90
Cdd:cd03269 1 LEVENVTKRFG-----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03269 69 -RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
29-247 |
3.33e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 119.73 E-value: 3.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 29 EVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCL---DRPSSGSYHFAGHDV---AELDSDEQAwlRREAFGFVFQGY 102
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVqreGRLARDIRK--SRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 103 HLIPSASAQENVEMPAIyAGIP---------ASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHII 173
Cdd:PRK09984 96 NLVNRLSVLENVLIGAL-GSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 174 LADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSA----NDERPAHPSAGVER 247
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSsqqfDNERFDHLYRSINR 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-229 |
6.97e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.57 E-value: 6.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGgNGTpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHdvaELDSDEQAW 89
Cdd:PRK13636 5 ILKVEELNYNYS-DGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK---PIDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LR-REAFGFVFQGY-HLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALM 167
Cdd:PRK13636 78 MKlRESVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILI-THDRD-VAARAKRIIEVRDGEIV 229
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIaTHDIDiVPLYCDNVFVMKEGRVI 221
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
11-281 |
9.02e-30 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 121.25 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPS--SGSYHFAGHDVAELDSdeqa 88
Cdd:TIGR03258 6 IRIDHLRVAYGAN-----TVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAPP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:TIGR03258 77 --HKRGLALLFQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 169 GGHIILADEPTGALDSHSGA----EVMALLDELASQghVVILITHDRDVA-ARAKRIIEVRDGEIVSDSANDERPAHPSA 243
Cdd:TIGR03258 155 EPDVLLLDEPLSALDANIRAnmreEIAALHEELPEL--TILCVTHDQDDAlTLADKAGIMKDGRLAAHGEPQALYDAPAD 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 15597586 244 G-VERHLQADDLSQRLAEGSSEPSGAWRAELLEAVRAAW 281
Cdd:TIGR03258 233 GfAAEFLGAANILPAIALGITEAPGLVDVSCGGAVIFAF 271
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-228 |
1.34e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 115.01 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawl 90
Cdd:cd03246 1 LEVENVSFRYPGAEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIpSASAQENVempaiyagipaserhtrarallerlglaertanrphqLSGGQQQRVSIARALMNGG 170
Cdd:cd03246 74 LGDHVGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-231 |
1.47e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 116.70 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAeldSDEQAW 89
Cdd:cd03266 1 MITADALTKRFRDVKKT-VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRReaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:cd03266 77 RRR--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIVSD 231
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYE 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-216 |
1.72e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.45 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLmniLGCLDR-----PS---SGSYHFAGHDVA 80
Cdd:COG1117 10 PKIEVRNLNVYYGDK-----QALKDINLDIPENKVTALIGPSGCGKSTL---LRCLNRmndliPGarvEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELDSDeQAWLRREaFGFVFQGYHLIPSaSAQENVEMPAIYAGI-PASERHTRARALLERLGLAERTANRPHQ----LSGG 155
Cdd:COG1117 82 DPDVD-VVELRRR-VGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDEVKDRLKKsalgLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 156 QQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQgHVVILITHDRDVAAR 216
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAAR 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-229 |
2.95e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 122.08 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 2 ENATQPVPLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAE 81
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSG-----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 82 LdSDEQAwlrrEAFG--FVFQGYHLIPSASAQENvempaIYAGIPASERHT-RARALLERLGLAERTANRPHQLSGGQQQ 158
Cdd:PRK15439 78 L-TPAKA----HQLGiyLVPQEPLLFPNLSVKEN-----ILFGLPKRQASMqKMKQLLAALGCQLDLDSSAGSLEVADRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 159 RVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIV 229
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTIA 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-256 |
4.02e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 120.14 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRREAFGFVFQGYHLIPSASA 110
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 111 QENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEV 190
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 191 MALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHPSAG-VERHLQADDLSQ 256
Cdd:PRK10070 204 QDELVKLqAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDyVRTFFRGVDISQ 272
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-209 |
5.52e-29 |
|
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: 114.19 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRK-RYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNIL-GCLDRPS-SGSYHFAGHdvaelDSDEQ 87
Cdd:cd03213 4 LSFRNLTVtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGR-----PLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 88 AWlrREAFGFVFQGYHLIPSASAQENVEMPAiyagipaserHTRarallerlglaertanrphQLSGGQQQRVSIARALM 167
Cdd:cd03213 79 SF--RKIIGYVPQDDILHPTLTVRETLMFAA----------KLR-------------------GLSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITH 209
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
9-270 |
7.91e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 115.70 E-value: 7.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGN----GTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDS 84
Cdd:COG4167 3 ALLEVRNLSKTFKYRtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 85 DEQAWLRReafgFVFQ--GYHLIPSASAQENVEMPAIYA-GIPASERHTRARALLERLGLAERTAN-RPHQLSGGQQQRV 160
Cdd:COG4167 83 KYRCKHIR----MIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLPEHANfYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 161 SIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERP 238
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELqEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
|
250 260 270
....*....|....*....|....*....|....*
gi 15597586 239 AHPSagverhlqaDDLSQRLAE---GSSEPSGAWR 270
Cdd:COG4167 239 ANPQ---------HEVTKRLIEshfGEALTADAWR 264
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-232 |
8.33e-29 |
|
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: 115.12 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRY-------GGNGTP---------EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHF 74
Cdd:cd03267 1 IEVSNLSKSYrvyskepGLIGSLkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 75 AGHDvaeldsdeqAWLRREAF----GFVF-QGYHLIPSASAQENVEM-PAIYaGIPASERHTRARALLERLGLAERTANR 148
Cdd:cd03267 81 AGLV---------PWKRRKKFlrriGVVFgQKTQLWWDLPVIDSFYLlAAIY-DLPPARFKKRLDELSELLDLEELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 149 PHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHD-RDVAARAKRIIEVRDG 226
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYmKDIEALARRVLVIDKG 230
|
....*.
gi 15597586 227 EIVSDS 232
Cdd:cd03267 231 RLLYDG 236
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
27-214 |
1.82e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 112.52 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGhdvAELDSDEQAWL-RREAFGFVFQGY-HL 104
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG---EPLDYSRKGLLeRRQRVGLVFQDPdDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 105 IPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDS 184
Cdd:TIGR01166 81 LFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 15597586 185 HSGAEVMALLDELASQGHVVILITHDRDVA 214
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-240 |
2.05e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.24 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCL-----DRPSSGSYHFAGHDVAELDSD 85
Cdd:PRK14247 4 IEIRDLKVSFG-----QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 EqawLRREAfGFVFQGYHLIPSASAQENVEMPAIYAGIPASER--HTRARALLERLGLAERTANR----PHQLSGGQQQR 159
Cdd:PRK14247 79 E---LRRRV-QMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQgHVVILITHDRDVAARAKRIIE-VRDGEIVSDSANDE-- 236
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAfLYKGQIVEWGPTREvf 233
|
....*
gi 15597586 237 -RPAH 240
Cdd:PRK14247 234 tNPRH 238
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-229 |
2.46e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 119.95 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 25 TPEVEVLKG-VSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLdrPSSGSYHFAGHDVAELDsdEQAWlrREAFGFVFQGY 102
Cdd:PRK11174 359 SPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELD--PESW--RKHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 103 HLiPSASAQENVEMpaiyAGIPASErhTRARALLERLGLAERTANRPH-----------QLSGGQQQRVSIARALMNGGH 171
Cdd:PRK11174 433 QL-PHGTLRDNVLL----GNPDASD--EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 172 IILADEPTGALDSHSGAEVMALLDElASQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-232 |
4.71e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.11 E-value: 4.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 24 GTP-EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRREAFGFVFQgy 102
Cdd:PRK13646 15 GTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 103 hlIPSASA-QENVEMPAIYA----GIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVSIARALMNGGHIILAD 176
Cdd:PRK13646 93 --FPESQLfEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 177 EPTGALDSHSGAEVMALLDELA-SQGHVVILITHD-RDVAARAKRIIEVRDGEIVSDS 232
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-229 |
1.13e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 110.77 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeqawL 90
Cdd:cd03268 1 LKTNDLTKTYGKK-----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RR-----EAFGFVfqgyhliPSASAQENVEMPAIYAGIpaseRHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARA 165
Cdd:cd03268 72 RRigaliEAPGFY-------PNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIV 229
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-231 |
3.00e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.87 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRY-------GGNGTP---------EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNIL-GCLdRPSSGSYH 73
Cdd:COG4586 2 IEVENLSKTYrvyekepGLKGALkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 74 FAGHDvaeldsdeqAWLRREAF----GFVF-QGYHLIPSASAQENVEM-PAIYaGIPASERHTRARALLERLGLAErTAN 147
Cdd:COG4586 81 VLGYV---------PFKRRKEFarriGVVFgQRSQLWWDLPAIDSFRLlKAIY-RIPDAEYKKRLDELVELLDLGE-LLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 148 RP-HQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHD-RDVAARAKRIIEVR 224
Cdd:COG4586 150 TPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDmDDIEALCDRVIVID 229
|
....*..
gi 15597586 225 DGEIVSD 231
Cdd:COG4586 230 HGRIIYD 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
3.10e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.38 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 1 MENATqpvPLIELRDIRKRYGGNgtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVA 80
Cdd:PRK13648 1 MEDKN---SIIVFKNVSFQYQSD---ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELDSDEQawlrREAFGFVFQGyhlipsasaQENVEMPAIYA----------GIPASERHTRARALLERLGLAERTANRPH 150
Cdd:PRK13648 75 DDNFEKL----RKHIGIVFQN---------PDNQFVGSIVKydvafglenhAVPYDEMHRRVSEALKQVDMLERADYEPN 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 151 QLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVIL-ITHDRDVAARAKRIIEVRDGEI 228
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAMEADHVIVMNKGTV 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
15-283 |
3.10e-27 |
|
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: 113.67 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 15 DIRKRYGGNgtpeveVLKgVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRREA 94
Cdd:TIGR02142 4 RFSKRLGDF------SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 95 FGFVFQGYHLIPSASAQENVEMPaiYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIIL 174
Cdd:TIGR02142 77 IGYVFQEARLFPHLSVRGNLRYG--MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 175 ADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAAR-AKRIIEVRDGEIVSDSANDE---RPAHP-------- 241
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEvwaSPDLPwlaredqg 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15597586 242 ---SAGVERHLQADDLSQ-RLAEGSsepsgAWRAELLEAVRAAWRV 283
Cdd:TIGR02142 235 sliEGVVAEHDQHYGLTAlRLGGGH-----LWVPENLGPTGARLRL 275
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-237 |
4.18e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 4.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQa 88
Cdd:PRK10247 6 PLLQLQNVGYLAGDA-----KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlrREAFGFVFQGYHLIpSASAQENVEMPAIYAGIPASERHTRARalLERLGLAERTANRP-HQLSGGQQQRVSIARALM 167
Cdd:PRK10247 80 ---RQQVSYCAQTPTLF-GDTVYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTILTKNiAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVIL-ITHDRDVAARAKRIIEVRDGEIVSDSANDER 237
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHDKDEINHADKVITLQPHAGEMQEARYEL 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-229 |
4.49e-27 |
|
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: 115.97 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqaw 89
Cdd:TIGR02203 330 DVEFRNVTFRYPGRD---RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREaFGFVFQGYHLIPSASAqENVEMPAIY----AGIPASERHTRARALLERL--GLAERTANRPHQLSGGQQQRVSIA 163
Cdd:TIGR02203 404 LRRQ-VALVSQDVVLFNDTIA-NNIAYGRTEqadrAEIERALAAAYAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597586 164 RALMNGGHIILADEPTGALDSHSGAEVMALLDELAsQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-236 |
5.16e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.95 E-value: 5.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGhdvaELDSDEQAWLRREAFGFVFQGY-HLI 105
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG----ELLTAENVWNLRRKIGMVFQNPdNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 106 PSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSH 185
Cdd:PRK13642 95 VGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597586 186 SGAEVMALLDELASQGHVVIL-ITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSE 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
3-209 |
6.78e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 115.91 E-value: 6.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 3 NATQPVPLIELRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPS---SGSYHFAGHDV 79
Cdd:TIGR00955 13 RVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 80 aelDSDEQawlrREAFGFVFQGYHLIPSASAQEN------VEMPAIYagiPASERHTRARALLERLGLAE------RTAN 147
Cdd:TIGR00955 93 ---DAKEM----RAISAYVQQDDLFIPTLTVREHlmfqahLRMPRRV---TKKEKRERVDEVLQALGLRKcantriGVPG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 148 RPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITH 209
Cdd:TIGR00955 163 RVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-236 |
7.61e-27 |
|
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: 109.24 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeQAWL 90
Cdd:cd03254 3 IEFENVNFSYD-EKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIpSASAQENVEMPAIYAG---IPASERHTRARALLERL--GLAERTANRPHQLSGGQQQRVSIARA 165
Cdd:cd03254 76 -RSMIGVVLQDTFLF-SGTIMENIRLGRPNATdeeVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-229 |
7.64e-27 |
|
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: 107.40 E-value: 7.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDrPSSGSYHFAGHDVAELDSdeqaw 89
Cdd:cd03247 1 LSINNVSFSYPEQEQQ---VLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLK-PQQGEITLDGVPVSDLEK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREAFGFVFQGYHLIpsasaqenvempaiyagipaserhtrARALLERLGLaertanrphQLSGGQQQRVSIARALMNG 169
Cdd:cd03247 72 ALSSLISVLNQRPYLF--------------------------DTTLRNNLGR---------RFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELAsQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-229 |
1.17e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.92 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 2 ENATQPVPLIELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAE 81
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDQPQP---VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 82 LDsdEQAWlrREAFGFVFQGYHLIpSASAQENVEMpaiyagipASERHTRAR--ALLERLGLAERTANRP---------- 149
Cdd:PRK11160 407 YS--EAAL--RQAISVVSQRVHLF-SATLRDNLLL--------AAPNASDEAliEVLQQVGLEKLLEDDKglnawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 150 HQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELAsQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
11-241 |
1.20e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgTP-EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAW 89
Cdd:PRK13634 3 ITFQKVEHRYQYK-TPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREAFGFVFQgyhlIPSASA-QENVEMPAIYA----GIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVSIA 163
Cdd:PRK13634 82 PLRKKVGIVFQ----FPEHQLfEETVEKDICFGpmnfGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 164 RALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHD-RDVAARAKRIIEVRDGEIVSDSANDERPAHP 241
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSmEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-267 |
1.24e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.42 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 4 ATQPVPLIELRDIRKRYGGNgtpEVEVLKGVSLSIHAGEFVAIVGASGSGKS-TLMNILGCLDRPS----SGSYHFAGHD 78
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQT---VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 79 VaeLDSDEQAW--LRREAFGFVFQG--YHLIPSASAQENV-EMPAIYAGIpaseRHTRARA----LLERLGL---AERTA 146
Cdd:PRK15134 78 L--LHASEQTLrgVRGNKIAMIFQEpmVSLNPLHTLEKQLyEVLSLHRGM----RREAARGeilnCLDRVGIrqaAKRLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 147 NRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVIL-ITHDRDVAAR-AKRIIEVR 224
Cdd:PRK15134 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLfITHNLSIVRKlADRVAVMQ 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15597586 225 DGEIVSDSANDE---RPAHPsagverhlqaddLSQRLAegSSEPSG 267
Cdd:PRK15134 232 NGRCVEQNRAATlfsAPTHP------------YTQKLL--NSEPSG 263
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-243 |
1.25e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 111.74 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAElDSDEQawl 90
Cdd:PRK11432 7 VVLKNITKRFGSN-----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTR---ARALLERLGLAERTANrphQLSGGQQQRVSIARALM 167
Cdd:PRK11432 78 -RD-ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRvkeALELVDLAGFEDRYVD---QISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVIL-ITHDRDVA-ARAKRIIEVRDGEIVSDSANDERPAHPSA 243
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLyVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-229 |
1.42e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.20 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLM-NILGCLDrPSSGSYHFAGHDVAELDsdeqaw 89
Cdd:COG4152 2 LELKGLTKRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGILA-PDSGEVLWDGEPLDPED------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lrREAFGFvfqgyhlipsasaqenveMP--------------AIY----AGIPASERHTRARALLERLGLAERTANRPHQ 151
Cdd:COG4152 70 --RRRIGY------------------LPeerglypkmkvgeqLVYlarlKGLSKAEAKRRADEWLERLGLGDRANKKVEE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARALMnggH----IILaDEPTGALDSHSgAEVMA-LLDELASQGHVVILITHDRDVAAR-AKRIIEVRD 225
Cdd:COG4152 130 LSKGNQQKVQLIAALL---HdpelLIL-DEPFSGLDPVN-VELLKdVIRELAAKGTTVIFSSHQMELVEElCDRIVIINK 204
|
....
gi 15597586 226 GEIV 229
Cdd:COG4152 205 GRKV 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-241 |
1.53e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 110.97 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 1 MENATQPVPLIELRDIRKRYGgngTPE--VEVLKGVSLSIHAGEFVAIVGASGSGKS-TLMNILGCLDRPS--SGSYHFA 75
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFS---TPDgdVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 76 GHDVAELDSDEQAWLRREAFGFVFQG--YHLIPSASAQENV-EMPAIYAGIPASERHTRARALLERLGLAE---RTANRP 149
Cdd:PRK09473 80 GREILNLPEKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 150 HQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAA---------RAKR 219
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAgicdkvlvmYAGR 239
|
250 260
....*....|....*....|....
gi 15597586 220 IIEVrdgeivsDSAND--ERPAHP 241
Cdd:PRK09473 240 TMEY-------GNARDvfYQPSHP 256
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-229 |
2.54e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 24 GTP-EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAeldsDEQAWLR--REAFGFVFQ 100
Cdd:PRK13637 15 GTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT----DKKVKLSdiRKKVGLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 101 --GYHLIpsasaQENVEMPAIYA----GIPASERHTRARALLERLGLA-ERTANR-PHQLSGGQQQRVSIARALMNGGHI 172
Cdd:PRK13637 91 ypEYQLF-----EETIEKDIAFGpinlGLSEEEIENRVKRAMNIVGLDyEDYKDKsPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 173 ILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHD-RDVAARAKRIIEVRDGEIV 229
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
35-228 |
3.69e-26 |
|
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: 106.87 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 35 SLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwlrreaFGFVFQGYHLIPSASAQENV 114
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 115 EMpAIYAGIP-ASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMAL 193
Cdd:TIGR01277 92 GL-GLHPGLKlNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 15597586 194 LDELASQGHV-VILITHD-RDVAARAKRIIEVRDGEI 228
Cdd:TIGR01277 171 VKQLCSERQRtLLMVTHHlSDARAIASQIAVVSQGKI 207
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-241 |
3.93e-26 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 107.99 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELD----- 83
Cdd:TIGR02323 2 PLLQVSGLSKSYGG-----GKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 84 SDEQAWLRREAFGFVFQ----GYHLIPSASAQENVEMPAIYAGIPASERHTrARALLERLGL-AERTANRPHQLSGGQQQ 158
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQnprdGLRMRVSAGANIGERLMAIGARHYGNIRAT-AQDWLEEVEIdPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 159 RVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAA-RAKRIIEVRDGEIVSDSAND- 235
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLaVIIVTHDLGVARlLAQRLLVMQQGRVVESGLTDq 235
|
....*...
gi 15597586 236 --ERPAHP 241
Cdd:TIGR02323 236 vlDDPQHP 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-229 |
6.51e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 111.93 E-value: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 8 VPLIELRDIRKRYggngtPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSdeq 87
Cdd:PRK11288 2 SPYLSFDGIGKTF-----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 88 awlrREAFG----FVFQGYHLIPSASAQENV---EMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRV 160
Cdd:PRK11288 74 ----TAALAagvaIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 161 SIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIV 229
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEeIFALCDAITVFKDGRYV 219
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
383-660 |
7.15e-26 |
|
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.
Pssm-ID: 274576 [Multi-domain] Cd Length: 803 Bit Score: 113.38 E-value: 7.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 383 AYVGGNntdFPEILNWPVAEGSYFTERDEDA-ATTVAVIGYKVRKKLFGSA-NPIGRYILIENVPFQVIGVLAEkGSSSG 460
Cdd:TIGR03434 113 AFVSAN---FFPVLGVQPALGRLFTPEDDRPgAPPVVVLSYALWQRRFGGDpAVVGRTIRLNGRPYTVVGVMPP-GFTFP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 461 DKDADNRIAIPYSAASIRLFGTRNPEYVIIAaadaqR------VHQAERAIDQLMLRLHR------GQRDYELTNNAAMI 528
Cdd:TIGR03434 189 GRDPDVWVPLAMDPALAGSANRGSRWLRVIG-----RlkpgvtLAQAQAELDAIAARLAAaypdtnAGRGLAVTPLRESL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 529 QAEAKTqntLSLMLGSIAAISLLVGGIGVMNIMLMTVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALA 608
Cdd:TIGR03434 264 VGDVRP---PLLVLLGAVGLVLLIACANVANLLLARAAARQREIAVRLALGAGRGRLVRQLLTESLLLALAGGALGLLLA 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 609 LciGGVLLL---------GQVAVAFSLSAIVGAFSCALVTGLVFGFMPARKAAQLDPVAAL 660
Cdd:TIGR03434 341 Y--WGLRLLlallpaslpRLLEISLDGRVLLFALALSLLTGLLFGLAPALQATRSDLAEAL 399
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-233 |
9.27e-26 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 111.63 E-value: 9.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYggngtPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVA---ELDSD 85
Cdd:PRK10762 3 ALLQLKGIDKAF-----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 EQAwlrreaFGFVFQGYHLIPSASAQENV----EMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVS 161
Cdd:PRK10762 78 EAG------IGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHdrdvaaRAKRIIEV-------RDGEIVSDSA 233
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH------RLKEIFEIcddvtvfRDGQFIAERE 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-229 |
9.51e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 9.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaeldSDEQA 88
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN---ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGyhliPS-----ASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIA 163
Cdd:PRK13632 79 KEIRKKIGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 164 RALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGH-VVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-227 |
9.60e-26 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 103.30 E-value: 9.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHfaghdvaeldsdeqaWL 90
Cdd:cd03221 1 IELENLSKTYGGK-----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------WG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVfqgyhlipsasaqenvempaiyagipaserhtrarallerlglaertanrpHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03221 61 STVKIGYF---------------------------------------------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 171 HIILADEPTGALDSHSgaeVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGE 227
Cdd:cd03221 90 NLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-229 |
9.63e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 9.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFaGHDV--------- 79
Cdd:COG0488 314 KVLELEGLSKSYGDK-----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVkigyfdqhq 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 80 AELDSDEQA--WLRREAFGfvfqgyhlipsasaqenvempaiyagipASERHtrARALLERLGLAERTANRP-HQLSGGQ 156
Cdd:COG0488 388 EELDPDKTVldELRDGAPG----------------------------GTEQE--VRGYLGRFLFSGDDAFKPvGVLSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 157 QQRVSIARALMNGGHIILADEPTGALDSHSgaeVMALLDELAS-QGhVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIET---LEALEEALDDfPG-TVLLVSHDRYFLDRvATRILEFEDGGVR 508
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-243 |
1.12e-25 |
|
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: 105.70 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwl 90
Cdd:cd03218 1 LRAENLSKRYGKR-----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:cd03218 74 -RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGhVVILIT-HD-RDVAARAKRIIEVRDGEIVSDSANDERPAHPSA 243
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRG-IGVLITdHNvRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-228 |
1.26e-25 |
|
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: 104.05 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawLRREAFGFVfqgyhlipsas 109
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIRAGIAYV----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 aqenvempaiyagipASERHTRAraLLERLGLAERTANrPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAE 189
Cdd:cd03215 81 ---------------PEDRKREG--LVLDLSVAENIAL-SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15597586 190 VMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEI 228
Cdd:cd03215 143 IYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-183 |
1.33e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 108.78 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawl 90
Cdd:PRK11650 4 LKLQAVRKSYDGK----TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAfgFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTR---ARALLERLGLAERtanRPHQLSGGQQQRVSIARALM 167
Cdd:PRK11650 76 RDIA--MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERvaeAARILELEPLLDR---KPRELSGGQRQRVAMGRAIV 150
|
170
....*....|....*.
gi 15597586 168 NGGHIILADEPTGALD 183
Cdd:PRK11650 151 REPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-236 |
2.83e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEldsdEQAW 89
Cdd:PRK13650 4 IIEVKNLTFKYKED--QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE----ENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREAFGFVFQGyhliPS-----ASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIAR 164
Cdd:PRK13650 78 DIRHKIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-236 |
3.27e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwlRREAFgfvFQGYHLIPSA- 108
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA--RRLAL---LPQHHLTPEGi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 109 SAQENVEmpaiYAGIP--------ASERHTRARALLERLGLAErTANRP-HQLSGGQQQRVSIARALMNGGHIILADEPT 179
Cdd:PRK11231 92 TVRELVA----YGRSPwlslwgrlSAEDNARVNQAMEQTRINH-LADRRlTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 180 GALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDE 236
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEE 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-210 |
3.95e-25 |
|
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: 109.76 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 8 VPLIELRDIRKRYGGNGtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTL-MNILGCLDrPSSGSYHFAGHDVAELDSDE 86
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAP----PVLDGVSLDLPPGERVAILGPSGSGKSTLlATLAGLLD-PLQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 QawlrREAFGFVFQGYHLIpSASAQENVEMPAiyAGIPASErhtrARALLERLGLAERTANRPH-----------QLSGG 155
Cdd:TIGR02868 407 V----RRRVSVCAQDAHLF-DTTVRENLRLAR--PDATDEE----LWAALERVGLADWLRALPDgldtvlgeggaRLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 156 QQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDElASQGHVVILITHD 210
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-236 |
7.24e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.51 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 35 SLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeqawlrREAFGFVFQGYHLIPSASAQENV 114
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 115 EMpAIYAGIP--ASERHTRaRALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMA 192
Cdd:PRK10771 93 GL-GLNPGLKlnAAQREKL-HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15597586 193 LLDELASQGHVVIL-ITHDRDVAAR-AKRIIEVRDGEIVSDSANDE 236
Cdd:PRK10771 171 LVSQVCQERQLTLLmVSHSLEDAARiAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-236 |
7.60e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 108.72 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:PRK09700 4 PYISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLrreAFGFVFQGYHLIPSASAQENVEMPAI----YAGIPA---SERHTRARALLERLGLAERTANRPHQLSGGQQQRVS 161
Cdd:PRK09700 79 QL---GIGIIYQELSVIDELTVLENLYIGRHltkkVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGE-----IVSDSAND 235
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSsvcsgMVSDVSND 235
|
.
gi 15597586 236 E 236
Cdd:PRK09700 236 D 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-240 |
7.92e-25 |
|
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: 109.52 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 26 PEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeQAWLRReAFGFVFQ----- 100
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLRA-AIGIVPQdtvlf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 101 ----GYHLI---PSASaQENVEMPAiyagipaseRHTRARALLERL--GLAERTANRPHQLSGGQQQRVSIARALMNGGH 171
Cdd:COG5265 445 ndtiAYNIAygrPDAS-EEEVEAAA---------RAAQIHDFIESLpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 172 IILADEPTGALDSHSGAEVMALLDElASQGHVVILITHDRDVAARAKRIIEVRDGEIVsdsandERPAH 240
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAHRLSTIVDADEILVLEAGRIV------ERGTH 576
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-241 |
9.85e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 105.59 E-value: 9.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 20 YGGNGTPEVEVLKgVSLSIHAGEFVAIVGASGSGKS-TLMNILGCLDRP---SSGSYHFAGHDVAELDSDEQAWLRREAF 95
Cdd:PRK11022 13 FGDESAPFRAVDR-ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 96 GFVFQG--YHLIPSASAQENVeMPAI--YAGIPASERHTRARALLERLGL---AERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:PRK11022 92 AMIFQDpmTSLNPCYTVGFQI-MEAIkvHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRD-VAARAKRIIEVRDGEIVSDSANDE---RPAHP 241
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMaLVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHDifrAPRHP 248
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-213 |
1.54e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 105.17 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 32 KGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGcLDRPSSGSYHFAGHDVAELdSDEQAWLRREAFGFVFQGyhliPSASA 110
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGEVAWLGKDLLGM-KDDEWRAVRSDIQMIFQD----PLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 111 QENVEMPAI--------YAGIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVSIARALMNGGHIILADEPTGA 181
Cdd:PRK15079 112 NPRMTIGEIiaeplrtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190
....*....|....*....|....*....|...
gi 15597586 182 LDSHSGAEVMALLDELASQ-GHVVILITHDRDV 213
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAV 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-230 |
2.42e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 107.18 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILgcldrpsSGSY---------HFAGhDVA 80
Cdd:NF040905 1 ILEMRGITKTFPG-----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGVYphgsyegeiLFDG-EVC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 EL----DSdeqawlrrEAFGFVF--QGYHLIPSASAQENVEM---PAIYAGIPASERHTRARALLERLGLAERTANRPHQ 151
Cdd:NF040905 68 RFkdirDS--------EALGIVIihQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIVS 230
Cdd:NF040905 140 IGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIRRVADSITVLRDGRTIE 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-210 |
3.67e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 13 LRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwlrr 92
Cdd:PRK11000 6 LRNVTKAYG-----DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 93 eaFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHI 172
Cdd:PRK11000 77 --VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 15597586 173 ILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHD 210
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHD 193
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-249 |
4.31e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 101.06 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 12 ELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwlr 91
Cdd:TIGR03410 2 EVSNLNVYYGQS-----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 REAFGFVFQGYHLIPSASAQENVEMPAiyAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGH 171
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGL--AALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 172 IILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVA-ARAKRIIEVRDGEIVSDSANDERPAhpsAGVERHL 249
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMaILLVEQYLDFArELADRYYVMERGRVVASGAGDELDE---DKVRRYL 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-216 |
5.63e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.96 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 7 PVPLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEldsde 86
Cdd:PRK13537 4 SVAPIDFRNVEKRYG-----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 QAWLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARAL 166
Cdd:PRK13537 74 RARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15597586 167 MNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR 216
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAER 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-216 |
6.99e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 6.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:PRK09536 2 PMIDVSDLSVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlRREAFgfVFQGYHLIPSASAQENVEM---PAIYAGIPASERHTRA-RALLERLGLAeRTANRP-HQLSGGQQQRVSIA 163
Cdd:PRK09536 77 --RRVAS--VPQDTSLSFEFDVRQVVEMgrtPHRSRFDTWTETDRAAvERAMERTGVA-QFADRPvTSLSGGERQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15597586 164 RALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR 216
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAAR 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-208 |
1.40e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGcLDRPSSGSYHFAGHDVAELDSDEQ 87
Cdd:COG1137 2 MTLEAENLVKSYGKR-----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYmIVG-LVKPDSGRIFLDGEDITHLPMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 88 AwlrREAFGF------VFQGyhLipsaSAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVS 161
Cdd:COG1137 76 A---RLGIGYlpqeasIFRK--L----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGhVVILIT 208
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG-IGVLIT 192
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
9-229 |
1.60e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.95 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSdeqA 88
Cdd:PRK11614 4 VMLSFDKVSAHYG-----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPA-SERHTRARALLERlgLAERTANRPHQLSGGQQQRVSIARALM 167
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV 229
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-209 |
1.68e-23 |
|
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: 98.58 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEldsdeQAWLRREAFGFVFQGYHLIP 106
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-----QRDEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 107 SASAQENVEMpaiYAGIPASERHTrARALLERLGLAERtANRP-HQLSGGQQQRVSIARALMNGGHIILADEPTGALDSH 185
Cdd:TIGR01189 87 ELSALENLHF---WAAIHGGAQRT-IEDALAAVGLTGF-EDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....
gi 15597586 186 SGAEVMALLDELASQGHVVILITH 209
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
27-231 |
1.69e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYH----FAGHDVAELDSDEQAWLR--------REA 94
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELITNPYSKkiknfkelRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 95 FGFVFQ--GYHLIPSaSAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVSIARALMNGGH 171
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERsPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 172 IILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDvaarakRIIEVRDGEIVSD 231
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME------HVLEVADEVIVMD 250
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-210 |
3.07e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQA 88
Cdd:PRK11300 4 PLLSVSGLMMRFGG-----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlrREAFGFVFQGYHLIPSASAQENVEMP-------AIYAGI---PA---SERHTRARAL--LERLGLAErTANRPH-QL 152
Cdd:PRK11300 79 ---RMGVVRTFQHVRLFREMTVIENLLVAqhqqlktGLFSGLlktPAfrrAESEALDRAAtwLERVGLLE-HANRQAgNL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 153 SGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHD 210
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVtVLLIEHD 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-216 |
3.79e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.06 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEldsdeQAWL 90
Cdd:PRK13536 42 IDLAGVSKSYGDK-----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-----RARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGG 170
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR 216
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAER 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-229 |
3.82e-23 |
|
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: 98.33 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeqawL 90
Cdd:cd03244 3 IEFKNVSLRYRPNLPP---VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG------L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 R--REAFGFVFQGYHLIpSASAQENVEmpaiyagiPASErHTRAR--ALLERLGLAERTANRPHQL-----------SGG 155
Cdd:cd03244 74 HdlRSRISIIPQDPVLF-SGTIRSNLD--------PFGE-YSDEElwQALERVGLKEFVESLPGGLdtvveeggenlSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 156 QQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDElASQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-232 |
4.27e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDeQAWLRREAFGFVFQGyhliP 106
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAK-TVWDIREKVGIVFQN----P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 107 S-----ASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGA 181
Cdd:PRK13640 94 DnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597586 182 LDSHSGAEVMALLDELASQGHV-VILITHDRDVAARAKRIIEVRDGEIVSDS 232
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLtVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-251 |
4.51e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 103.63 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 4 ATQPVPLIELRD------IRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKST----LMNILgcldrPSSGSYH 73
Cdd:PRK15134 269 PEPASPLLDVEQlqvafpIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 74 FAGHDVAELDSDEQAWLRREaFGFVFQGYH--LIPSASAQENVE--MPAIYAGIPASERHTRARALLERLGLAERTANR- 148
Cdd:PRK15134 344 FDGQPLHNLNRRQLLPVRHR-IQVVFQDPNssLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRy 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 149 PHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVV-ILITHD-RDVAARAKRIIEVRDG 226
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAyLFISHDlHVVRALCHQVIVLRQG 502
|
250 260
....*....|....*....|....*
gi 15597586 227 EIVSDSANDERPAHPSAGVERHLQA 251
Cdd:PRK15134 503 EVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-241 |
5.45e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 100.37 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 25 TPE--VEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLD---RPSSGSYHFAGHDVAELDSDEQ-AWLRREaFGF 97
Cdd:COG4170 15 TPQgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPRERrKIIGRE-IAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 98 VFQ--GYHLIPSASAQENVEmpaiyAGIPASE-----------RHTRARALLERLGLAERTA---NRPHQLSGGQQQRVS 161
Cdd:COG4170 94 IFQepSSCLDPSAKIGDQLI-----EAIPSWTfkgkwwqrfkwRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELA-SQGHVVILITHD-RDVAARAKRIIEVRDGEIVsDSANDE--- 236
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDlESISQWADTITVLYCGQTV-ESGPTEqil 247
|
....*.
gi 15597586 237 -RPAHP 241
Cdd:COG4170 248 kSPHHP 253
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-227 |
5.81e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 97.15 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDRpSSGSYHFAGHD--VAEldsdeQ 87
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGSIayVSQ-----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 88 AWLRreafgfvfqgyhlipSASAQENvempaIYAGIPASERhtRARALLERLGLAERTANRPHQ-----------LSGGQ 156
Cdd:cd03250 75 PWIQ---------------NGTIREN-----ILFGKPFDEE--RYEKVIKACALEPDLEILPDGdlteigekginLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 157 QQRVSIARALMNGGHIILADEPTGALDSHSGAEVM--ALLDELAsQGHVVILITHDRDVAARAKRIIEVRDGE 227
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLLL-NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-216 |
6.47e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.38 E-value: 6.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCL-----DRPSSGSYHFAGHDVAELDSD 85
Cdd:PRK14267 5 IETVNLRVYYGSN-----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 EQAwLRREAfGFVFQGYHLIPSASAQENVEMPAIYAGI--PASERHTRARALLERLGLAERTANR----PHQLSGGQQQR 159
Cdd:PRK14267 80 PIE-VRREV-GMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQgHVVILITHDRDVAAR 216
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAAR 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-229 |
6.49e-23 |
|
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: 102.96 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHF-AGH---DVAELDS 84
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDewvDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 85 DEQAWLRReAFGFVFQGYHLIPSASAQENVeMPAIYAGIPASERHTRARALLERLGLAERTANR-----PHQLSGGQQQR 159
Cdd:TIGR03269 358 DGRGRAKR-YIGILHQEYDLYPHRTVLDNL-TEAIGLELPDELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVM-ALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIV 229
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGKIV 507
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-229 |
7.76e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 7.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGnGTP-EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAW 89
Cdd:PRK13649 3 INLQNVSYTYQA-GTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREAFGFVFQgyhLIPSASAQENVEMPAIYA----GIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVSIAR 164
Cdd:PRK13649 82 QIRKKVGLVFQ---FPESQLFEETVLKDVAFGpqnfGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITH--DrDVAARAKRIIEVRDGEIV 229
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlmD-DVANYADFVYVLEKGKLV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-216 |
1.15e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.54 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLmniLGCLDRPS--------SGSYHFAGHDVA 80
Cdd:PRK14239 4 PILQVSDLSVYYN-----KKKALNSVSLDFYPNEITALIGPSGSGKSTL---LRSINRMNdlnpevtiTGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELDSDeQAWLRREaFGFVFQGYHLIPsASAQENVEMPAIYAGIpaSERHTRARALLERLGLA---ERTANRPHQ----LS 153
Cdd:PRK14239 76 SPRTD-TVDLRKE-IGMVFQQPNPFP-MSIYENVVYGLRLKGI--KDKQVLDEAVEKSLKGAsiwDEVKDRLHDsalgLS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 154 GGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQgHVVILITHDRDVAAR 216
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASR 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-224 |
1.55e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 33 GVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSD---EQAWLrreafgfvfqGYH--LIPS 107
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqDLLYL----------GHQpgIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 108 ASAQENVempAIYAGIPASERHTRARALLERLGLAERtANRP-HQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHS 186
Cdd:PRK13538 89 LTALENL---RFYQRLHGPGDDEALWEALAQVGLAGF-EDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 15597586 187 GAEVMALLDELASQGHVVILITHdRDVAARAKRIIEVR 224
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTTH-QDLPVASDKVRKLR 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-228 |
4.01e-22 |
|
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: 95.62 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 26 PEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeQAWLRREAfGFVFQGYHLI 105
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE---HKYLHSKV-SLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 106 pSASAQEN-------VEMPAIYAGIPASERHTRARALleRLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEP 178
Cdd:cd03248 101 -ARSLQDNiayglqsCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15597586 179 TGALDSHSGAEVMALLDElASQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:cd03248 178 TSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-230 |
4.48e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.00 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILgCLDRPS---SGSYHFAGHDVaeldsd 85
Cdd:PRK13549 4 YLLEMKNITKTFGG-----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPHgtyEGEIIFEGEEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 eQAWLRR--EAFGFV--FQGYHLIPSASAQENVEM---PAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQ 158
Cdd:PRK13549 72 -QASNIRdtERAGIAiiHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 159 RVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIVS 230
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNeVKAISDTICVIRDGRHIG 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-209 |
5.48e-22 |
|
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: 95.03 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRpssGSYHFAGH-DVAELDSDEQAWLRReaFGFVFQGYHLI 105
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE---GGGTTSGQiLFNGQPRKPDQFQKC--VAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 106 PSASAQENVEmpaiYAGIPASERHTRARA--------LLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADE 177
Cdd:cd03234 94 PGLTVRETLT----YTAILRLPRKSSDAIrkkrvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 15597586 178 PTGALDSHSGAEVMALLDELASQGHVVILITH 209
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-236 |
6.86e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRyggngtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaELDSDEQA 88
Cdd:COG1129 255 VVLEVEGLSVG---------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wLRReafGFVF-------QGyhLIPSASAQENVEMPAI--YAG---IPASERHTRARALLERLGLaeRTANrPHQ----L 152
Cdd:COG1129 325 -IRA---GIAYvpedrkgEG--LVLDLSIRENITLASLdrLSRgglLDRRRERALAEEYIKRLRI--KTPS-PEQpvgnL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 153 SGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIVSD 231
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSElPELLGLSDRILVMREGRIVGE 475
|
....*
gi 15597586 232 SANDE 236
Cdd:COG1129 476 LDREE 480
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-240 |
7.75e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.09 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAE--LDSdeqa 88
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP---ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLAS---- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 wlRREAFGFVFQGYHLIPSASAQeNVEmpaiYAgipASERHTR------ARA-----LLERL--GLAERTANRPHQLSGG 155
Cdd:PRK11176 415 --LRNQVALVSQNVHLFNDTIAN-NIA----YA---RTEQYSReqieeaARMayamdFINKMdnGLDTVIGENGVLLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 156 QQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGEIVsdsand 235
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEILVVEDGEIV------ 557
|
....*
gi 15597586 236 ERPAH 240
Cdd:PRK11176 558 ERGTH 562
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-249 |
9.90e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.18 E-value: 9.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeQAW 89
Cdd:TIGR00958 478 LIEFQDVSFSYPNR--PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD---HHY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRREAfGFVFQGYHLIpSASAQENV-------EMPAIYAGIPASERHTRARALLErlGLAERTANRPHQLSGGQQQRVSI 162
Cdd:TIGR00958 553 LHRQV-ALVGQEPVLF-SGSVRENIaygltdtPDEEIMAAAKAANAHDFIMEFPN--GYDTEVGEKGSQLSGGQKQRIAI 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 163 ARALMNGGHIILADEPTGALDshsgAEVMALLDELAS-QGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDERPAHP 241
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALD----AECEQLLQESRSrASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
....*...
gi 15597586 242 saGVERHL 249
Cdd:TIGR00958 705 --GCYKHL 710
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-236 |
1.11e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 99.11 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLD--RPSSGS--YH------------- 73
Cdd:TIGR03269 1 IEVKNLTKKFDG-----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRiiYHvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 74 -FAGH--------------DVAELDSDEQAWLRREaFGFVFQ-GYHLIPSASAQENVEMPAIYAGIPASERHTRARALLE 137
Cdd:TIGR03269 76 sKVGEpcpvcggtlepeevDFWNLSDKLRRRIRKR-IAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 138 RLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILIT-HDRDVAAR 216
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIED 234
|
250 260
....*....|....*....|.
gi 15597586 217 -AKRIIEVRDGEIVSDSANDE 236
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDE 255
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
10-230 |
1.43e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.57 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAghDVAELDSDEQAW 89
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LR--REAFGFVFQgyhlIPSASAQENVEMPAIYAG-----IPASERHTRARALLERLGLA-ERTANRPHQLSGGQQQRVS 161
Cdd:PRK13643 79 IKpvRKKVGVVFQ----FPESQLFEETVLKDVAFGpqnfgIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITH-DRDVAARAKRIIEVRDGEIVS 230
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIIS 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-236 |
2.29e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 28 VEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawlRREAfGFVF-----QGY 102
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE----RRRL-GVAYipedrLGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 103 HLIPSASAQENVEMPAIYAG-------IPASERHTRARALLERLGLaeRTANrPHQ----LSGGQQQRVSIARALMNGGH 171
Cdd:COG3845 346 GLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDV--RTPG-PDTparsLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597586 172 IILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIVSDSANDE 236
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDeILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
30-228 |
2.87e-21 |
|
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: 97.80 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeqawlrREAFG----FVFQGYHLI 105
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD--------RETFGkhigYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 106 PSASAQ------ENVEMPAIYAGIPASERHTraraLLERL------GLAERTANrphqLSGGQQQRVSIARALMNGGHII 173
Cdd:TIGR01842 405 PGTVAEniarfgENADPEKIIEAAKLAGVHE----LILRLpdgydtVIGPGGAT----LSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 174 LADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-209 |
3.91e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwlrreafgfVFQGYH--L 104
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC---------HYLGHRnaM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 105 IPSASAQENVEMPAIYAGipasERHTRARALLERLGLAeRTANRPHQ-LSGGQQQRVSIARALMNGGHIILADEPTGALD 183
Cdd:PRK13539 85 KPALTVAENLEFWAAFLG----GEELDIAAALEAVGLA-PLAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*.
gi 15597586 184 SHSGAEVMALLDELASQGHVVILITH 209
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
36-236 |
4.05e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 92.61 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 36 LSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEldsdeqawlRREAFGFVFQGYHL---IPSASAQE 112
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK---------GWRHIGYVPQRHEFawdFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 113 NVEMPAIYAGI---PASERHTRARALLERLGLAErTANRP-HQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGA 188
Cdd:TIGR03771 72 VMSGRTGHIGWlrrPCVADFAAVRDALRRVGLTE-LADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15597586 189 EVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:TIGR03771 151 LLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQ 198
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-229 |
8.33e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGgNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAw 89
Cdd:PRK13644 1 MIRLENVSYSYP-DGTP---ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lrREAFGFVFQGYHL-IPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:PRK13644 76 --RKLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-236 |
9.69e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 9.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeQAW 89
Cdd:PRK13657 334 AVEFDDVSFSYDNSR----QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRReAFGFVFQGYHLI------------PSASAQENVEmpaiyagipASERhTRARALLER--LGLAERTANRPHQLSGG 155
Cdd:PRK13657 407 LRR-NIAVVFQDAGLFnrsiednirvgrPDATDEEMRA---------AAER-AQAHDFIERkpDGYDTVVGERGRQLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 156 QQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSAND 235
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFD 554
|
.
gi 15597586 236 E 236
Cdd:PRK13657 555 E 555
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-230 |
1.19e-20 |
|
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: 95.66 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGngtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILgCLDRPS---SGSYHFAGhdvAELDSDE 86
Cdd:TIGR02633 1 LLEMKGIVKTFGG-----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYPHgtwDGEIYWSG---SPLKASN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 QAWLRREAFGFVFQGYHLIPSASAQENVEM------PAIYAGIPASERhtRARALLERLGLAERTANRP-HQLSGGQQQR 159
Cdd:TIGR02633 72 IRDTERAGIVIIHQELTLVPELSVAENIFLgneitlPGGRMAYNAMYL--RAKNLLRELQLDADNVTRPvGDYGGGQQQL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 160 VSIARALMNGGHIILADEPTGALdshSGAEVMALLD---ELASQGHVVILITHDRD-VAARAKRIIEVRDGEIVS 230
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSL---TEKETEILLDiirDLKAHGVACVYISHKLNeVKAVCDTICVIRDGQHVA 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-230 |
1.34e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.44 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLdRPSSGSYHFAGHDVAELDSDEQAwlRREAF-------GFVFQGYH 103
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELA--RHRAYlsqqqspPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 104 LIpsASAQEnvempaiyAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN-------GGHIILAD 176
Cdd:COG4138 89 YL--ALHQP--------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 177 EPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVS 230
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRhADRVWLLKQGKLVA 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-241 |
1.78e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.69 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNG------TPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEL 82
Cdd:PRK10261 312 PILQVRNLVTRFPLRSgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 83 DSDEQAWLRREaFGFVFQGYH--LIPSASAQENVEMPAIYAGI-PASERHTRARALLERLGLAERTANR-PHQLSGGQQQ 158
Cdd:PRK10261 392 SPGKLQALRRD-IQFIFQDPYasLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 159 RVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEIVS---DSA 233
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEigpRRA 550
|
....*...
gi 15597586 234 NDERPAHP 241
Cdd:PRK10261 551 VFENPQHP 558
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-216 |
2.34e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.38 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 1 MENATQPVPLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTlmnILGCLDR-----PS---SGSY 72
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSF-----LAVKNVWLDIPKNQITAFIGPSGCGKST---ILRCFNRlndliPGfrvEGKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 73 HFAGHDVAELDSDEQAWLRReaFGFVFQGYHLIPSaSAQENVEMPAIYAGIPAS-----ERHTRARAL-------LERLG 140
Cdd:PRK14243 73 TFHGKNLYAPDVDPVEVRRR--IGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmdelvERSLRQAALwdevkdkLKQSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597586 141 LAertanrphqLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQgHVVILITHDRDVAAR 216
Cdd:PRK14243 150 LS---------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAAR 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-236 |
2.64e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDR------PSSGSYHFAGHDVAELDSDEqawLRREAfGFVFQGYH 103
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIK---LRKEV-GMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 104 LIPSASAQENVEMPAIYAGIPASERHTR-ARALLERLGLAERTANR----PHQLSGGQQQRVSIARALMNGGHIILADEP 178
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 179 TGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-239 |
2.67e-20 |
|
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: 94.86 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaelDSDEQAWL 90
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIPSasaqenvempaiYAGIPASERHTRARALLERLGLAERTA-------NRphQLSGGQQQRVSIA 163
Cdd:COG4615 405 -RQLFSAVFSDFHLFDR------------LLGLDGEADPARARELLERLELDHKVSvedgrfsTT--DLSQGQRKRLALL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 164 RALMNGGHIILADEptgaldshsgaevMA--------------LLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:COG4615 470 VALLEDRPILVFDE-------------WAadqdpefrrvfyteLLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
250
....*....|
gi 15597586 230 SDSANDERPA 239
Cdd:COG4615 537 ELTGPAALAA 546
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-236 |
5.13e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 94.04 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNIL-GCLdRPSSGSYHFAGHDVAELDSDEqawlRREAFGFVFQGYHLIPSA 108
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREE----LGRHIGYLPQDVELFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 109 SAQ----------ENVEMPAIYAGIpaserHtrarALLERL--GLAERTANRPHQLSGGQQQRVSIARALMNGGHIILAD 176
Cdd:COG4618 422 IAEniarfgdadpEKVVAAAKLAGV-----H----EMILRLpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 177 EPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
27-209 |
6.37e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.36 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILgcLDRPS----SGSYHFAGHDVAELDSDEQAwlrREAFGFVFQ-- 100
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGHPKyevtSGSILLDGEDILELSPDERA---RAGIFLAFQyp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 101 --------GYHLIPSASAQENVEMPAIyagipasERHTRARALLERLGLAERTANRP--HQLSGGQQQRVSIARALMNGG 170
Cdd:COG0396 87 veipgvsvSNFLRTALNARRGEELSAR-------EFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15597586 171 HIILADEPtgalDShsGAEVMAL------LDELASQGHVVILITH 209
Cdd:COG0396 160 KLAILDET----DS--GLDIDALrivaegVNKLRSPDRGILIITH 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-236 |
1.59e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNgtpeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQaw 89
Cdd:PRK13652 3 LIETRDLCYSYSGS----KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lrREAFGFVFQGYH-LIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:PRK13652 77 --RKFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAARAKRIIEVRD-GEIVSDSANDE 236
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDkGRIVAYGTVEE 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
30-236 |
2.12e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAwlRReaFGFVFQGYHLIPSAS 109
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENVEMpaiyAGIPASERHTRAR--------ALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGA 181
Cdd:PRK10253 98 VQELVAR----GRYPHQPLFTRWRkedeeavtKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 182 LDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDE 236
Cdd:PRK10253 174 LDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKE 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-230 |
3.02e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 25 TP-EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDV-AELDS-DEQAWLRREaFGFVFQ- 100
Cdd:PRK13645 20 TPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRKE-IGLVFQf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 101 -GYHLIpSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVSIARALMNGGHIILADEP 178
Cdd:PRK13645 99 pEYQLF-QETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15597586 179 TGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVS 230
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVIS 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-231 |
5.59e-19 |
|
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: 86.05 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 13 LRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGsyhfaghdvaELDSDEQ-AWLR 91
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG----------TVTVRGRvSSLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 REAFGFVfqgyhliPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERtANRP-HQLSGGQQQRVSIARALMNGG 170
Cdd:cd03220 90 GLGGGFN-------PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDF-IDLPvKTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 171 HIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIVSD 231
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDpSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-247 |
1.21e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 89.65 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPevevLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAelDSDEQAWl 90
Cdd:PRK10522 323 LELRNVTFAYQDNGFS----VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT--AEQPEDY- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAFGFVFQGYHLIPSASAQENVEMPAiyagipaserhTRARALLERLGLAERTANRPH-----QLSGGQQQRVSIARA 165
Cdd:PRK10522 396 -RKLFSAVFTDFHLFDQLLGPEGKPANP-----------ALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEV-MALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIvSDSANDERPAHPSAG 244
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL-SELTGEERDAASRDA 542
|
...
gi 15597586 245 VER 247
Cdd:PRK10522 543 VAR 545
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-236 |
1.22e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 29 EVLKGVSLSIHAGEFVAIVGASGSGKSTL-MNILGCLdRPSSGSYHFAGHdvaELDSDEQAWLR-REAFGFVFQG-YHLI 105
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGK---PLDYSKRGLLAlRQQVATVFQDpEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 106 PSASAQENVEMPAIYAGIPASERhtrARALLERLGL--AERTANRPHQ-LSGGQQQRVSIARALMNGGHIILADEPTGAL 182
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEI---TRRVDEALTLvdAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 183 DSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEV-RDGEIVSDSANDE 236
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVlRQGQILTHGAPGE 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-243 |
1.23e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.91 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKryggngTPEVEVLKGVSLSIHAGEFVAIVGASGSGKS-TLMNILGCLD---RPSSGSYHFAGHDVAEldsde 86
Cdd:PRK10418 5 IELRNIAL------QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 qAWLRREAFGFVFQGyhlipSASAQENVEMPAIYA-------GIPASERhtRARALLERLGLAE--RTANR-PHQLSGGQ 156
Cdd:PRK10418 74 -CALRGRKIATIMQN-----PRSAFNPLHTMHTHAretclalGKPADDA--TLTAALEAVGLENaaRVLKLyPFEMSGGM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 157 QQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAAR-AKRIIEVRDGEIV-SDSA 233
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVeQGDV 225
|
250
....*....|..
gi 15597586 234 ND--ERPAHPSA 243
Cdd:PRK10418 226 ETlfNAPKHAVT 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-241 |
8.09e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 26 PEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAG-------HDVAELDSDEQAWLRR---EAF 95
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQSAAQMRHvrgADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 96 GFVFQG--YHLIPSASAQENV-EMPAIYAGIPASERHTRARALLERLGLAERTA---NRPHQLSGGQQQRVSIARALMNG 169
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAAR-AKRIIEVRDGEIVSDSANDE---RPAHP 241
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQifhAPQHP 263
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-212 |
8.92e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 8.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 34 VSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaeLDSDEQAWL----RReaFGFVFQGYHLIPSAS 109
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKGICLppekRR--IGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENV------EMPAIYA------GIpaserhtraRALLERLglaertanrPHQLSGGQQQRVSIARALMNGGHIILADE 177
Cdd:PRK11144 93 VRGNLrygmakSMVAQFDkivallGI---------EPLLDRY---------PGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 15597586 178 PTGALDSHSGAEVMALLDELASQGHVVIL-ITHDRD 212
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILyVSHSLD 190
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-273 |
1.07e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRK----RYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHdvaELDSD 85
Cdd:PRK15112 4 LLEVRNLSKtfryRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 EQAWlRREAFGFVFQ--GYHLIPSASAQENVEMPAIY-AGIPASERHTRARALLERLGLAERTANR-PHQLSGGQQQRVS 161
Cdd:PRK15112 81 DYSY-RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILIT-HDRDVAARAKRIIEVRDGEIVSDSANDERPA 239
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTqHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250 260 270
....*....|....*....|....*....|....
gi 15597586 240 HPSAGVERHLQADDLSQRLAegssepSGAWRAEL 273
Cdd:PRK15112 240 SPLHELTKRLIAGHFGEALT------ADAWRKDR 267
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-230 |
1.09e-17 |
|
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: 82.07 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawL 90
Cdd:cd03369 7 IEVENLSVRYAPDLPP---VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREafgfvfqgYHLIPsasaQEnvemPAIYAGIPAS----ERHTRARALLERLGLAERTANrphqLSGGQQQRVSIARAL 166
Cdd:cd03369 81 RSS--------LTIIP----QD----PTLFSGTIRSnldpFDEYSDEEIYGALRVSEGGLN----LSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 167 MNGGHIILADEPTGALDSHSGAEVMALLDELASqGHVVILITHDRDVAARAKRIIEVRDGEIVS 230
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
27-229 |
1.35e-17 |
|
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: 81.42 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLD-RPSSGSYHFAGHDVAELDSDEQAwlrREAFGFVFQgyhl 104
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 105 ipsasaqenveMPAIYAGIpaserhtraralleRLGLAERTANrpHQLSGGQQQRVSIARALMNGGHIILADEPTGALDS 184
Cdd:cd03217 85 -----------YPPEIPGV--------------KNADFLRYVN--EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15597586 185 HSGAEVMALLDELASQGHVVILITHDRDVAA--RAKRIIEVRDGEIV 229
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-226 |
2.61e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.63 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 25 TPEVEVL-KGVSLSIHAGEFVAIVGASGSGKSTLMNIL--------GCLDRPssgsyhfAGHDVAeldsdeqawlrreaf 95
Cdd:COG4178 372 TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsGRIARP-------AGARVL--------------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 96 gFVFQ-GYhlIPSASAQENVempaIYAGIPASERHTRARALLERLGLA------ERTANRPHQLSGGQQQRVSIARALMN 168
Cdd:COG4178 430 -FLPQrPY--LPLGTLREAL----LYPATAEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALL-DELAsqGHVVILITHDRDVAARAKRIIEVRDG 226
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLrEELP--GTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-231 |
2.89e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 13 LRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeqawlrr 92
Cdd:COG1134 24 LKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 93 eaFGFVFQgyhliPSASAQENVEMPAIYAGIPASERHTRARALLERLGLaERTANRP-HQLSGGQQQRVSIARALMNGGH 171
Cdd:COG1134 95 --LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAEL-GDFIDQPvKTYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 172 IILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSD 231
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMD 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-236 |
4.92e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.13 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 34 VSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLdrPSSGSYHFAGHDVAELDSDEQAWLR-------REAFGF-VFQGYHL 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArMAGLL--PGSGSIQFAGQPLEAWSAAELARHRaylsqqqTPPFAMpVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 105 IPSASAQENVEMPAIYagipaserhtrarALLERLGLAERTANRPHQLSGGQQQRVSIA-------RALMNGGHIILADE 177
Cdd:PRK03695 93 HQPDKTRTEAVASALN-------------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 178 PTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDE 236
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRDE 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-236 |
5.35e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 1 MENATQPVPLIELRDIRKRyggngTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVA 80
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFR-----VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELDSdeQAWLRREAFgfVFQGyhlIPSASAQENVEMPAI--YA--------GIPASERHTRARALLERLGLAERTANrph 150
Cdd:PRK10575 77 SWSS--KAFARKVAY--LPQQ---LPAAEGMTVRELVAIgrYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 151 QLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHDRDVAAR-AKRIIEVRDGEI 228
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
....*...
gi 15597586 229 VSDSANDE 236
Cdd:PRK10575 227 IAQGTPAE 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-209 |
9.21e-17 |
|
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: 79.07 E-value: 9.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaeldsDEQAWLRREAFGFVFQGYHLIPSAS 109
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENVEMpaiYAGIPASERHTRAralLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAE 189
Cdd:cd03231 90 VLENLRF---WHADHSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 15597586 190 VMALLDELASQGHVVILITH 209
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-241 |
1.01e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.77 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 8 VPLIELRDIRKRYGGNGTPeVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLD---RPSSGSYHFAGHDVAELD 83
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGVTKdnwRVTADRMRFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 84 SDEQAWLRREAFGFVFQGYH--LIPSasaqENVEMPAIYAgIPASE-----------RHTRARALLERLGLAERTA---N 147
Cdd:PRK15093 80 PRERRKLVGHNVSMIFQEPQscLDPS----ERVGRQLMQN-IPGWTykgrwwqrfgwRKRRAIELLHRVGIKDHKDamrS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 148 RPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVI-LITHDRDVAAR-AKRIIEVRD 225
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDLQMLSQwADKINVLYC 234
|
250
....*....|....*....
gi 15597586 226 GEIVSDSANDE---RPAHP 241
Cdd:PRK15093 235 GQTVETAPSKElvtTPHHP 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-274 |
1.74e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 6 QPVPLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELdSD 85
Cdd:PRK11831 3 SVANLVDMRGVSFTRG-----NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM-SR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 EQAWLRREAFGFVFQGYHLIPSASAQENVEMPAI-YAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIAR 164
Cdd:PRK11831 77 SRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 165 ALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHD-RDVAARAKRIIEVRDGEIVSDSANDERPAHPS 242
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDvPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
250 260 270
....*....|....*....|....*....|....*
gi 15597586 243 AGVERHLQAddlsqrLAEGSSE---PSGAWRAELL 274
Cdd:PRK11831 237 PRVRQFLDG------IADGPVPfryPAGDYHADLL 265
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
31-210 |
3.53e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGsyhfaghDVAELDSDEQAWLRREAFGFVFQGYHLIPSASA 110
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-------KISILGQPTRQALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 111 Q-ENVEMPAIYAG-----IPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDS 184
Cdd:PRK15056 96 LvEDVVMMGRYGHmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*.
gi 15597586 185 HSGAEVMALLDELASQGHVVILITHD 210
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-214 |
5.61e-16 |
|
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: 82.37 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 8 VPLIELRDIRKRYGGNGTPEVEVLkgvSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDV-AELDSde 86
Cdd:TIGR01257 926 VPGVCVKNLVKIFEPSGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA-- 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 qawlRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARAL 166
Cdd:TIGR01257 1001 ----VRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15597586 167 MNGGHIILADEPTGALDSHSGAEVMALLDELASqGHVVILITHDRDVA 214
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEA 1123
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-226 |
5.71e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 77.37 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 25 TPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLM-NILGCLdRPSSGSYHFAGHDVAELDSDEQAWLRREAFGFVFQGYH 103
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEM-QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 104 LIpSASAQENVEMpaiyaGIPASERhtRARALLERLGLAERTANRPH-----------QLSGGQQQRVSIARALMNGGHI 172
Cdd:cd03290 90 LL-NATVEENITF-----GSPFNKQ--RYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15597586 173 ILADEPTGALDSHSGAEVM--ALLDELASQGHVVILITHDRDVAARAKRIIEVRDG 226
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-241 |
6.17e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGsYHFAG------------HDVAELdsdeqawlrREAFGF 97
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGdvllggrsifnyRDVLEF---------RRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 98 VFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGL----AERTANRPHQLSGGQQQRVSIARALMNGGHII 173
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 174 LADEPTGALDSHSGAEVMALLDELASQgHVVILITHDRDVAAR-AKRIIEVRDGEIVSDSANDERPAHP 241
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-236 |
1.05e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 12 ELRDI---RKRYGGNGTPEVEVLKG------VSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAeL 82
Cdd:PRK11288 241 EIGDIygyRPRPLGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-I 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 83 DSDEQAwLR---------REAFGfvfqgyhLIPSASAQENVEmpaiyagIPASERHTRARALLERlGLAERTANR----- 148
Cdd:PRK11288 320 RSPRDA-IRagimlcpedRKAEG-------IIPVHSVADNIN-------ISARRHHLRAGCLINN-RWEAENADRfirsl 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 149 ------PHQ----LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARA 217
Cdd:PRK11288 384 niktpsREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVA 463
|
250
....*....|....*....
gi 15597586 218 KRIIEVRDGEIVSDSANDE 236
Cdd:PRK11288 464 DRIVVMREGRIAGELAREQ 482
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-210 |
2.14e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 8 VPLIELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLmniLGCLDRPSS--------GSYHFAGHDV 79
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQ-----KILEGVSMEIYQSKVTAIIGPSGCGKSTF---LKCLNRMNElesevrveGRVEFFNQNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 80 AELDSDEQAwLRREAfGFVFQGYHLIPsASAQENVEMPAIYAGI-PASERHTRARALLERLGLAERTANRPHQ----LSG 154
Cdd:PRK14258 77 YERRVNLNR-LRRQV-SMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 155 GQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILI-THD 210
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIvSHN 210
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
486-660 |
3.75e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442361 [Multi-domain] Cd Length: 830 Bit Score: 79.46 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 486 EYVIIAAADAQRVHQAERAIDQlmlRLHRGQRDYELTNNAAMIqaeAKTQNTLSLMLGSIAAISLLVGGIGVMNIMLMTV 565
Cdd:COG3127 206 RYRYLVAGPDADLEALRAWLEP---ALPAGQRVRTVEDARPEL---GRALDRAEQFLLLVALLALLLAGVAVANAARRYV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 566 RERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIAL--ALCIGGVLLLGQ-----VAVAFSLSAIVGAFSCALV 638
Cdd:COG3127 280 ARRLDTIALLRCLGASRRQIFRIYLLQLLLLGLLGSLLGLLLgaLLQALLAALLADllpvpLEPALSPLPLLLGLLVGLL 359
|
170 180
....*....|....*....|..
gi 15597586 639 TGLVFGFMPARKAAQLDPVAAL 660
Cdd:COG3127 360 VLLLFALPPLLRLRRVPPLRVL 381
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
538-662 |
1.79e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442361 [Multi-domain] Cd Length: 830 Bit Score: 77.15 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 538 LSLMLGSIAAISLLVGGIGVMNIMLMTVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALALCIGGVLL- 616
Cdd:COG3127 703 VSLAVEFLAGFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLAALLAELAGWALAr 782
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15597586 617 -LGQVAVAFSLSAIVGAFSCALVTGLVFGFMPARKAAQLDPVAALAS 662
Cdd:COG3127 783 fVFDLPFSPPWWLWLAGLLGGALLVLLAGLLGARRVLRQPPLEVLRE 829
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-228 |
1.92e-14 |
|
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: 77.29 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDRpSSGSYHFAGhDVAELDsdEQAWlrreafgfvfqgyhlIPSAS 109
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG-SVAYVP--QQAW---------------IQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENvempaIYAGIPASERHTR----ARALL---ERLGLAERT--ANRPHQLSGGQQQRVSIARALMNGGHIILADEPTG 180
Cdd:TIGR00957 715 LREN-----ILFGKALNEKYYQqvleACALLpdlEILPSGDRTeiGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15597586 181 ALDSHSGAEV-------MALLdelasQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:TIGR00957 790 AVDAHVGKHIfehvigpEGVL-----KNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
30-236 |
2.44e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKST-LMNILGCLDRpSSGSYHFAGHDVAELDSDEQAwlrREAFGFVFQGYHLIPSA 108
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGIVPR-DAGNIIIDDEDISLLPLHARA---RRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 109 SAQENV-EMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSG 187
Cdd:PRK10895 94 SVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15597586 188 AEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITDHNvRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| FtsX |
pfam02687 |
FtsX-like permease family; This is a family of predicted permeases and hypothetical ... |
543-656 |
3.31e-14 |
|
FtsX-like permease family; This is a family of predicted permeases and hypothetical transmembrane proteins. Swiss:P57382 has been shown to transport lipids targeted to the outer membrane across the inner membrane. Both Swiss:P57382 and Swiss:O54500 have been shown to require ATP. This region contains three transmembrane helices.
Pssm-ID: 460652 [Multi-domain] Cd Length: 120 Bit Score: 69.59 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 543 GSIAAISLLVGGIGVMNIMLMTVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALALCIGGVLLLGQVAV 622
Cdd:pfam02687 1 ILFSLLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVIGLLLGLLLAKLIAILLYSS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15597586 623 AFSLSAIVGAFSC------ALVTGLVFGFMPARKAAQLDP 656
Cdd:pfam02687 81 GISLPILVPPLSIlialllALLIALLASLLPALRIRKINP 120
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-211 |
6.05e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.97 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 13 LRDIRKRYGGNGtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFA-GHDVAELDSDEQAWLR 91
Cdd:TIGR03719 7 MNRVSKVVPPKK----EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 REAFGFVFQG----------YHLIPSASAQENVEMPAIYAG-------IPASERHTRARAL---LERLGLAERTANRPHq 151
Cdd:TIGR03719 83 KTVRENVEEGvaeikdaldrFNEISAKYAEPDADFDKLAAEqaelqeiIDAADAWDLDSQLeiaMDALRCPPWDADVTK- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDshsgAEVMALLDE-LASQGHVVILITHDR 211
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERhLQEYPGTVVAVTHDR 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-240 |
8.34e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGClDRPSSGSYHFA---------GHDVAELDSDEQAWLR-------RE 93
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAPRGArvtgdvtlnGEPLAAIDAPRLARLRavlpqaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 94 AFGFvfqgyhlipsaSAQENVEMP----AIYAGipASERHTR--ARALLERLGLAERTANRPHQLSGGQQQRVSIARAL- 166
Cdd:PRK13547 95 AFAF-----------SAREIVLLGryphARRAG--ALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 167 --------MNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDVAAR-AKRIIEVRDGEIVSDSANDE 236
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARhADRIAMLADGAIVAHGAPAD 241
|
....*.
gi 15597586 237 --RPAH 240
Cdd:PRK13547 242 vlTPAH 247
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-268 |
1.09e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 29 EVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawlrREAFGFVF-----QGYH 103
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 104 LIPSASAQENVeMPAIYAGIPASERHTRARALLER----LGLAERTANRP-HQLSGGQQQRVSIARALMNGGHIILADEP 178
Cdd:PRK15439 352 LYLDAPLAWNV-CALTHNRRGFWIKPARENAVLERyrraLNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 179 TGALDSHSGAEVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIvsdsanderpahpSAGVERHLQADDLSQR 257
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEeIEQMADRVLVMHQGEI-------------SGALTGAAINVDTIMR 497
|
250
....*....|.
gi 15597586 258 LAEGSSEPSGA 268
Cdd:PRK15439 498 LAFGEHQAQEA 508
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-228 |
1.53e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.51 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGclDRPSSGSYHFA------Ghdvae 81
Cdd:PRK10938 259 PRIVLNNGVVSYN-----DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlITG--DHPQGYSNDLTlfgrrrG----- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 82 ldSDEQAWLRREAFGFVFQGYHL--IPSASAQeNVEMPA------IYAGIPASERHtRARALLERLGLAERTANRP-HQL 152
Cdd:PRK10938 327 --SGETIWDIKKHIGYVSSSLHLdyRVSTSVR-NVILSGffdsigIYQAVSDRQQK-LAQQWLDILGIDKRTADAPfHSL 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 153 SGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILIT--HDRDV-AARAKRIIEVRDGEI 228
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVshHAEDApACITHRLEFVPDGDI 481
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
31-229 |
2.14e-13 |
|
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: 70.72 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILG-CLDRPSsgsyHFAGHDVAELDSDEQA----WLR------------- 91
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYpALARRL----HLKKEQPGNHDRIEGLehidKVIvidqspigrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 ------------REAFGFVFQG-----------YHlipSASAQENVEMPA-----IYAGIPASERHTRAralLERLGLAE 143
Cdd:cd03271 87 npatytgvfdeiRELFCEVCKGkrynretlevrYK---GKSIADVLDMTVeealeFFENIPKIARKLQT---LCDVGLGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 144 RTANRP-HQLSGGQQQRVSIARALMN---GGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKR 219
Cdd:cd03271 161 IKLGQPaTTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADW 240
|
250
....*....|....*.
gi 15597586 220 IIE------VRDGEIV 229
Cdd:cd03271 241 IIDlgpeggDGGGQVV 256
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-209 |
5.38e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 15 DIRKRYGGNGTP--------EVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSgsyhFAGHDVAELDSDE 86
Cdd:PLN03211 60 NIKRILGHKPKIsdetrqiqERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 87 QAWLRREafGFVFQGYHLIPSASAQENVEMPAIYAgIPAS----ERHTRARALLERLGLA--ERTA---NRPHQLSGGQQ 157
Cdd:PLN03211 136 KQILKRT--GFVTQDDILYPHLTVRETLVFCSLLR-LPKSltkqEKILVAESVISELGLTkcENTIignSFIRGISGGER 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597586 158 QRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITH 209
Cdd:PLN03211 213 KRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-236 |
6.35e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.46 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDRPSSGSYHFAGhDVAELDsdEQAWlrreafgfvfqgyhlIPSAS 109
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-TVAYVP--QVSW---------------IFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENvempaIYAGIP-ASERHTRA---RALLERLGL---------AERTANrphqLSGGQQQRVSIARALMNGGHIILAD 176
Cdd:PLN03130 695 VRDN-----ILFGSPfDPERYERAidvTALQHDLDLlpggdlteiGERGVN----ISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 177 EPTGALDSHSGAEVM--ALLDELasQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:PLN03130 766 DPLSALDAHVGRQVFdkCIKDEL--RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEE 825
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-211 |
1.34e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVaelDSDEQAWlrREAFGFVFQGYHLIPSAS 109
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTY--QKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENVEMpaiyagipasERHTRARAL----LERLGLAERTANRP-HQLSGGQQQRVSIARALMNGGHIILADEPTGALDS 184
Cdd:PRK13540 91 LRENCLY----------DIHFSPGAVgiteLCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*..
gi 15597586 185 HSGAEVMALLDELASQGHVVILITHDR 211
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-314 |
2.32e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 34 VSLSIHAGEFVAIVGASGSGKSTLMNIL-GCLDrPSSGSYHFAGHdvaELDSDEQAWLRReaFGFVFQGYHLIPSASAQE 112
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLP-ASEGEAWLFGQ---PVDAGDIATRRR--VGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 113 NVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTgaldshSGAEVMA 192
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT------SGVDPVA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 193 ------LLDELASQGHVVILI-THDRDVAARAKRIIEVRDGEI-VSDSanderpahPSAGVERHlQADDLSQ-------- 256
Cdd:NF033858 433 rdmfwrLLIELSREDGVTIFIsTHFMNEAERCDRISLMHAGRVlASDT--------PAALVAAR-GAATLEEafiaylee 503
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 257 ----RLAEGSSEPSGAWRAELLEAVRAAWRVMWINR----------------FRTALTLLGiiigvaSVVVMLAVGEG 314
Cdd:NF033858 504 aagaAAAPAAAAAPAAAAAAPAAPAPAPRRRFSLRRllayarrealellrdpIRLTFALLG------SVILMFVMGYG 575
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-230 |
2.42e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 36 LSIHAGEFVAIVGASGSGKSTLMNILG---CLDrpsSGSYHFAGhD--VAELDSDEQawlRREA---FGFVFQG------ 101
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRIIYEQ-DliVARLQQDPP---RNVEgtvYDFVAEGieeqae 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 102 ----YHLI-------PS-------ASAQENVEmpaiYAGIPASErhTRARALLERLGLaerTANRP-HQLSGGQQQRVSI 162
Cdd:PRK11147 97 ylkrYHDIshlvetdPSeknlnelAKLQEQLD----HHNLWQLE--NRINEVLAQLGL---DPDAAlSSLSGGWLRKAAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 163 ARALMNGGHIILADEPTGALDshsgAEVMALLDE-LASQGHVVILITHDRD-VAARAKRIIEVRDGEIVS 230
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD----IETIEWLEGfLKTFQGSIIFISHDRSfIRNMATRIVDLDRGKLVS 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-228 |
3.91e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.00 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDRPSSGSYHFAGhDVAELDsdEQAWlrreafgfvfqgyhlIPSAS 109
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-SVAYVP--QVSW---------------IFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENVEMPAIYAgipaSERHTRA---RALLERLGL---------AERTANrphqLSGGQQQRVSIARALMNGGHIILADE 177
Cdd:PLN03232 695 VRENILFGSDFE----SERYWRAidvTALQHDLDLlpgrdlteiGERGVN----ISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15597586 178 PTGALDSHSGAEVM--ALLDELasQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:PLN03232 767 PLSALDAHVAHQVFdsCMKDEL--KGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
31-223 |
5.07e-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: 64.65 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLmnilgCLDrpssgsyhfaghdvaeldsdeqawlrreafGFVFQGYHLIPSaSA 110
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----VNE------------------------------GLYASGKARLIS-FL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 111 QENVEMPAIYAGipaserhtRARALLErLGLAERTANRPHQ-LSGGQQQRVSIARALMNGGH--IILADEPTGALDSHSG 187
Cdd:cd03238 55 PKFSRNKLIFID--------QLQFLID-VGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*.
gi 15597586 188 AEVMALLDELASQGHVVILITHDRDVAARAKRIIEV 223
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-209 |
5.12e-12 |
|
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: 65.34 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 29 EVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGclDRPSS----GSYHFAGHdvaELDSDeqawLRREAfGFVFQGYHL 104
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAgvitGEILINGR---PLDKN----FQRST-GYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 105 IPSASAQENVEMpaiyagipaserhtraRALLERLGLAERtanrphqlsggqqQRVSIARALMNGGHIILADEPTGALDS 184
Cdd:cd03232 91 SPNLTVREALRF----------------SALLRGLSVEQR-------------KRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....*
gi 15597586 185 HSGAEVMALLDELASQGHVVILITH 209
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-211 |
5.61e-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: 68.81 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAghDVAELDSDEQAwl 90
Cdd:TIGR03719 323 IEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYVDQS-- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rREAfgfvfqgyhLIPSASAQE------------NVEMPAiyagipaserhtraRALLERLGL-AERTANRPHQLSGGQQ 157
Cdd:TIGR03719 394 -RDA---------LDPNKTVWEeisggldiiklgKREIPS--------------RAYVGRFNFkGSDQQKKVGQLSGGER 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15597586 158 QRVSIARALMNGGHIILADEPTGALDSHSgaeVMALLDELASQGHVVILITHDR 211
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVET---LRALEEALLNFAGCAVVISHDR 500
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-208 |
6.27e-12 |
|
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: 64.98 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 19 RYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILgCLDRPS----SGSYHFAGHDVAEldsdeqawlrrea 94
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL-ANRTEGnvsvEGDIHYNGIPYKE------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 95 FGFVFQGyHLIpsASAQENVEMPAIyagipaSERHT---RARAllerlglaertanRPHQ----LSGGQQQRVSIARALM 167
Cdd:cd03233 77 FAEKYPG-EII--YVSEEDVHFPTL------TVRETldfALRC-------------KGNEfvrgISGGERKRVSIAEALV 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15597586 168 NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILIT 208
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-229 |
1.27e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.27 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 29 EVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYhFAGHDVAELDsdEQAWlrreafgfvfqgyhlIPSA 108
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVP--QQAW---------------IMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 109 SAQENV-----EMPAIYAGIPaseRHTRARALLERL--GLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGA 181
Cdd:PTZ00243 736 TVRGNIlffdeEDAARLADAV---RVSQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15597586 182 LDSHSGAEVM--ALLDELAsqGHVVILITHDRDVAARAKRIIEVRDGEIV 229
Cdd:PTZ00243 813 LDAHVGERVVeeCFLGALA--GKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-210 |
1.28e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYhfaghdvaeldsDEQA 88
Cdd:PRK09544 3 SLVSLENVSVSFG-----QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLRreaFGFVFQGYHLIPSASAQENVEM---PAIYAG--IPASERhTRARALLERlglaertanrPHQ-LSGGQQQRVSI 162
Cdd:PRK09544 66 KLR---IGYVPQKLYLDTTLPLTVNRFLrlrPGTKKEdiLPALKR-VQAGHLIDA----------PMQkLSGGETQRVLL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15597586 163 ARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ-GHVVILITHD 210
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-213 |
1.41e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRyggngtpeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCL-DRPSSGSyhfagHDVAELDSDEQA 88
Cdd:COG2401 36 VELRVVERY----------VLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGALkGTPVAGC-----VDVPDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 89 WLrreafgfvfqgyhlipsasaqenVEmpAIYAGIPASErhtrARALLERLGLAERTA--NRPHQLSGGQQQRVSIARAL 166
Cdd:COG2401 101 SL-----------------------ID--AIGRKGDFKD----AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15597586 167 MNGGHIILADEPTGALDSHSGAEVMALLDELASQGHV-VILITHDRDV 213
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGItLVVATHHYDV 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-228 |
2.05e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 27 EVEVLKG-----VSLSIHAGEFVAIVGASGSGKSTLMNIL-GCLDRpSSGSYHFAGHDVaELDSDEQAWlrreAFGFVF- 99
Cdd:PRK10762 259 KVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEV-VTRSPQDGL----ANGIVYi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 100 ----QGYHLIPSASAQENVEMPAIYAgipASERHTRARALLERLGLAE-------RTANRPHQ---LSGGQQQRVSIARA 165
Cdd:PRK10762 333 sedrKRDGLVLGMSVKENMSLTALRY---FSRAGGSLKHADEQQAVSDfirlfniKTPSMEQAiglLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597586 166 LMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDR-DVAARAKRIIEVRDGEI 228
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRI 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-236 |
2.53e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpevevLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDV---AELDSD 85
Cdd:PRK09700 264 TVFEVRNVTSRDRKK-------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 EQ--AWL---RREAfGFvfqgyhlIPSASAQENVEMP-----AIYAGI-----PASERHTrARALLERLGLAERTANRP- 149
Cdd:PRK09700 337 KKgmAYItesRRDN-GF-------FPNFSIAQNMAISrslkdGGYKGAmglfhEVDEQRT-AENQRELLALKCHSVNQNi 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 150 HQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEI 228
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
....*...
gi 15597586 229 VSDSANDE 236
Cdd:PRK09700 488 TQILTNRD 495
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
11-251 |
3.88e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.14 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTlmnilGCLdrPSsgsyHFAGHDVAELDSDEQAWL 90
Cdd:NF000106 14 VEVRGLVKHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**R-----GAL--PA----HV*GPDAGRRPWRF*TWC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 -RREAFGFVFQGYHLI-----PSASAQENVEMpaIYAGIPASERHTRARA--LLERLGLAERTANRPHQLSGGQQQRVSI 162
Cdd:NF000106 78 aNRRALRRTIG*HRPVr*grrESFSGRENLYM--IGR*LDLSRKDARARAdeLLERFSLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 163 ARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRD-GEIVSDSANDE----- 236
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDrGRVIADGKVDElktkv 235
|
250 260
....*....|....*....|..
gi 15597586 237 -------RPAHpSAGVERHLQA 251
Cdd:NF000106 236 ggrtlqiRPAH-AAELDRMVGA 256
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-229 |
4.21e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGclDRPS----SGSYHFAGHDVAELDS 84
Cdd:CHL00131 6 PILEIKNLHASVN-----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPAykilEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 85 DEQAwlRREAFgFVFQGYHLIPSAS--------------AQENVEMPAIyagipasERHTRARALLERLGLAERTANR-- 148
Cdd:CHL00131 79 EERA--HLGIF-LAFQYPIEIPGVSnadflrlaynskrkFQGLPELDPL-------EFLEIINEKLKLVGMDPSFLSRnv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 149 PHQLSGGQQQRVSIAR-ALMNGGHIILaDEPTGALDSHSGAEVMALLDELASQGHVVILITHdrdvaarAKRIIE----- 222
Cdd:CHL00131 149 NEGFSGGEKKRNEILQmALLDSELAIL-DETDSGLDIDALKIIAEGINKLMTSENSIILITH-------YQRLLDyikpd 220
|
250
....*....|.
gi 15597586 223 ----VRDGEIV 229
Cdd:CHL00131 221 yvhvMQNGKII 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-179 |
5.47e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgngtpEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAElDSDEQAWL 90
Cdd:NF033858 2 ARLEGVSHRYG-----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-ARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAF---GFvfqGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAeRTANRPH-QLSGGQQQRVSIARAL 166
Cdd:NF033858 76 PRIAYmpqGL---GKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLA-PFADRPAgKLSGGMKQKLGLCCAL 151
|
170
....*....|....*..
gi 15597586 167 MnggH----IILaDEPT 179
Cdd:NF033858 152 I---HdpdlLIL-DEPT 164
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-236 |
6.83e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 26 PEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDRPSSGSYHFAGHDVaELDSDEQAwLR---------REAF 95
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPV-KIRNPQQA-IAqgiamvpedRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 96 GfvfqgyhLIPSASAQENVEMPAI--YAG---IPASERHTRARALLERLGLaeRTANrPHQ----LSGGQQQRVSIARAL 166
Cdd:PRK13549 351 G-------IVPVMGVGKNITLAALdrFTGgsrIDDAAELKTILESIQRLKV--KTAS-PELaiarLSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 167 MNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGDLINHN 491
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-224 |
7.20e-11 |
|
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: 61.22 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMnilgcldrpssgsyhfaghdvaeldsdeqawlrrEAFGFVFQGyhlipsasa 110
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTIL----------------------------------DAIGLALGG--------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 111 qenvEMPAIYAGIPASERHTRARALLERLGLAertanrpHQLSGGQQQRVSIARAL----MNGGHIILADEPTGALDSHS 186
Cdd:cd03227 48 ----AQSATRRRSGVKAGCIVAAVSAELIFTR-------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|....*...
gi 15597586 187 GAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVR 224
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-212 |
1.37e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.42 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRREAFGFVFQG---YHLIP 106
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGdreYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 107 S--ASAQENVEMPAIYA------GIPASERHTRARALLERLGLAERTANRP-HQLSGGQQQRVSIARALMNGGHIILADE 177
Cdd:PRK10636 96 AqlHDANERNDGHAIATihgkldAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 15597586 178 PTGALDSHSgaeVMALLDELASQGHVVILITHDRD 212
Cdd:PRK10636 176 PTNHLDLDA---VIWLEKWLKSYQGTLILISHDRD 207
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-207 |
1.47e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 35 SLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSD------EQAWLRR---------EAFGfvf 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEqlqklvSDEWQRNntdmlspgeDDTG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 100 qgyhLIPSASAQENVEMPAiyagipaserhtRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPT 179
Cdd:PRK10938 100 ----RTTAEIIQDEVKDPA------------RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180
....*....|....*....|....*...
gi 15597586 180 GALDSHSGAEVMALLDELASQGHVVILI 207
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-209 |
1.71e-10 |
|
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: 64.65 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGTPEVEVLkgvSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQaw 89
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRL---CVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH-- 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lrrEAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNG 169
Cdd:TIGR01257 2012 ---QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15597586 170 GHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITH 209
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-211 |
1.87e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 13 LRDIRKRYGGNGtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGsyhfaghdvaeldsdeQAWLRR 92
Cdd:PRK11819 9 MNRVSKVVPPKK----QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----------------EARPAP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 93 EA-FGFVFQGYHLIPSASAQENVEM------------PAIYAGIpaSERHTRARALLERLG-LAERTANR---------- 148
Cdd:PRK11819 69 GIkVGYLPQEPQLDPEKTVRENVEEgvaevkaaldrfNEIYAAY--AEPDADFDALAAEQGeLQEIIDAAdawdldsqle 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 149 --------PH------QLSGGQQQRVSIARALMNGGHIILADEPTGALDshsgAEVMALLDE-LASQGHVVILITHDR 211
Cdd:PRK11819 147 iamdalrcPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQfLHDYPGTVVAVTHDR 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-227 |
2.01e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 62.18 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKST-LMNILGCLDrPSSGSYHFAGHDVAeldSDEQAWlrreafgfvfqgyhlIPSA 108
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSlLMLILGELE-PSEGKIKHSGRISF---SSQFSW---------------IMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 109 SAQENvempaIYAGIPASErhTRARALLERLGLAERTANRPHQ-----------LSGGQQQRVSIARALMNGGHIILADE 177
Cdd:cd03291 113 TIKEN-----IIFGVSYDE--YRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597586 178 PTGALDSHSGAEVM--ALLDELASQGHvvILITHDRDVAARAKRIIEVRDGE 227
Cdd:cd03291 186 PFGYLDVFTEKEIFesCVCKLMANKTR--ILVTSKMEHLKKADKILILHEGS 235
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-229 |
3.16e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpevEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAghdvaeldsdEQAWL 90
Cdd:PRK15064 320 LEVENLTKGFDNG-----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS----------ENANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 rreafgfvfqGYHLIPSASAQENVEMPAIYAGIPASERH--TRARALLERLGLAERTANRPHQ-LSGGQQQRVSIARALM 167
Cdd:PRK15064 385 ----------GYYAQDHAYDFENDLTLFDWMSQWRQEGDdeQAVRGTLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597586 168 NGGHIILADEPTGALDSHSgaeVMALLDELASQGHVVILITHDRD-VAARAKRIIEVRDGEIV 229
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMES---IESLNMALEKYEGTLIFVSHDREfVSSLATRIIEITPDGVV 514
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-231 |
3.47e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGgNGTPEVevLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqawL 90
Cdd:PTZ00243 1309 LVFEGVQMRYR-EGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---L 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREafgfvfqgYHLIPS------ASAQENVEmPAIYAGiPAserhtRARALLERLGLAERTANRPHQL-----------S 153
Cdd:PTZ00243 1383 RRQ--------FSMIPQdpvlfdGTVRQNVD-PFLEAS-SA-----EVWAALELVGLRERVASESEGIdsrvleggsnyS 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 154 GGQQQRVSIARALMN-GGHIILADEPTG----ALDSHSGAEVMAlldelASQGHVVILITHDRDVAARAKRIIeVRDGEI 228
Cdd:PTZ00243 1448 VGQRQLMCMARALLKkGSGFILMDEATAnidpALDRQIQATVMS-----AFSAYTVITIAHRLHTVAQYDKII-VMDHGA 1521
|
...
gi 15597586 229 VSD 231
Cdd:PTZ00243 1522 VAE 1524
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-183 |
5.46e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeqAWL 90
Cdd:PLN03130 1238 IKFEDVVLRYRPELPP---VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG----LMD 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 91 RREAFGfvfqgyhLIPSAsaqenvemPAIYAGI------PASErHTRA-------RALLE------RLGLAERTANRPHQ 151
Cdd:PLN03130 1311 LRKVLG-------IIPQA--------PVLFSGTvrfnldPFNE-HNDAdlwesleRAHLKdvirrnSLGLDAEVSEAGEN 1374
|
170 180 190
....*....|....*....|....*....|..
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALD 183
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-241 |
9.88e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 15 DIRK-RYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqaWLRRe 93
Cdd:PRK10789 317 NIRQfTYPQTDHP---ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS--WRSR- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 94 aFGFVFQGYHLI------------PSASaQENVEMPAIYAGIpaserHTRARALLErlGLAERTANRPHQLSGGQQQRVS 161
Cdd:PRK10789 391 -LAVVSQTPFLFsdtvannialgrPDAT-QQEIEHVARLASV-----HDDILRLPQ--GYDTEVGERGVMLSGGQKQRIS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 162 IARALMNGGHIILADEPTGALDSHSGAEVMALLDELaSQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDERPAHP 241
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-210 |
1.20e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNGTpeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYH---------FAGHDV 79
Cdd:PLN03073 507 PIISFSDASFGYPGGPL----LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavFSQHHV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 80 AELDsdeqawlrreafgfvfqgyhlipsASAQENVEMPAIYAGIPaserHTRARALLERLGLAERTANRP-HQLSGGQQQ 158
Cdd:PLN03073 583 DGLD------------------------LSSNPLLYMMRCFPGVP----EQKLRAHLGSFGVTGNLALQPmYTLSGGQKS 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597586 159 RVSIARALMNGGHIILADEPTGALDSHSgaeVMALLDELASQGHVVILITHD 210
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLMVSHD 683
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
47-211 |
1.76e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 47 VGASGSGKSTLMNILGCLDRPSSGSYHfaghdvaeLDSDEQ-AWLRREAFGF--------VFQGYHLIPSAsaqeNVEMP 117
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVS--------LDPNERlGKLRQDQFAFeeftvldtVIMGHTELWEV----KQERD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 118 AIYAGIPASER--------------------HTRARALLERLGLAERTANRP-HQLSGGQQQRVSIARALMNGGHIILAD 176
Cdd:PRK15064 101 RIYALPEMSEEdgmkvadlevkfaemdgytaEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLD 180
|
170 180 190
....*....|....*....|....*....|....*
gi 15597586 177 EPTGALDSHSgaeVMALLDELASQGHVVILITHDR 211
Cdd:PRK15064 181 EPTNNLDINT---IRWLEDVLNERNSTMIIISHDR 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-236 |
1.95e-09 |
|
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: 60.61 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 26 PEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDRPSSGSYHFAGHDVAeLDSDEQAWlrREAFGFVFQG--- 101
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD-IRNPAQAI--RAGIAMVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 102 YHLIPSASAQENVEMPAI--YAG---IPASERHTRARALLERLGLAERTANRP-HQLSGGQQQRVSIARALMNGGHIILA 175
Cdd:TIGR02633 348 HGIVPILGVGKNITLSVLksFCFkmrIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597586 176 DEPTGALDSHSGAEVMALLDELASQGHVVILITHD-RDVAARAKRIIEVRDGEIVSDSANDE 236
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGDFVNHA 489
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-210 |
3.03e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.15 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 41 GEFVAIVGASGSGKSTLMNILGCLDRPSSGSYhfaghdvaeldSDEQAW--LRREAFGFVFQGY-------HLIPSASAQ 111
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF-----------DDPPDWdeILDEFRGSELQNYftkllegDVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 112 ENVEMPAIYAGI------PASERHTRARaLLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSH 185
Cdd:cd03236 95 YVDLIPKAVKGKvgellkKKDERGKLDE-LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*
gi 15597586 186 SGAEVMALLDELASQGHVVILITHD 210
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-226 |
3.36e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.31 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 24 GTPeveVLKGVSLSIHAGEFVAIVGASGSGKST-LMNILGCLDrPSSGSYHFAGHdvaeldsdeqawlrreaFGFVFQGY 102
Cdd:TIGR01271 438 VTP---VLKNISFKLEKGQLLAVAGSTGSGKSSlLMMIMGELE-PSEGKIKHSGR-----------------ISFSPQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 103 HLIPsASAQENvempaIYAGIPASErhTRARALLERLGLAERTANRPHQ-----------LSGGQQQRVSIARALMNGGH 171
Cdd:TIGR01271 497 WIMP-GTIKDN-----IIFGLSYDE--YRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 172 IILADEPTGALDSHSGAEVM--ALLDELASQGHvvILITHDRDVAARAKRIIEVRDG 226
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIFesCLCKLMSNKTR--ILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-211 |
3.72e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtpeveVL-KGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFaGHDV---------A 80
Cdd:PRK11819 325 IEAENLSKSFGDR------LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVklayvdqsrD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELDSDEQAWlrrEAfgfVFQGYHLIPSAsaqeNVEMPAiyagipaserhtraRALLERLGLAERTANRP-HQLSGGQQQR 159
Cdd:PRK11819 398 ALDPNKTVW---EE---ISGGLDIIKVG----NREIPS--------------RAYVGRFNFKGGDQQKKvGVLSGGERNR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15597586 160 VSIARALMNGGHIILADEPTGALDshsgAEVMALLDE--LASQGHVVIlITHDR 211
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD----VETLRALEEalLEFPGCAVV-ISHDR 502
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-210 |
3.78e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.80 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpEVEVLKGvslSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFaGHDVA------EL 82
Cdd:COG1245 340 TLVEYPDLTKSYGGF---SLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKISykpqyiSP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 83 DSDE--QAWLRREAFGFVFQGYHlipsasaqeNVEmpaiyagipaserhtraraLLERLGLaERTANRP-HQLSGGQQQR 159
Cdd:COG1245 413 DYDGtvEEFLRSANTDDFGSSYY---------KTE-------------------IIKPLGL-EKLLDKNvKDLSGGELQR 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597586 160 VSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELA-SQGHVVILITHD 210
Cdd:COG1245 464 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHD 515
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-251 |
4.26e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 10 LIELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEqaw 89
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPP---VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD--- 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 LRReafgfvfqGYHLIPSAsaqenvemPAIYAGI------PASErHTRAR--ALLERLGLAERTANRPHQL--------- 152
Cdd:PLN03232 1308 LRR--------VLSIIPQS--------PVLFSGTvrfnidPFSE-HNDADlwEALERAHIKDVIDRNPFGLdaevsegge 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 153 --SGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDElASQGHVVILITHDRDVAARAKRIIEVRDGEIVS 230
Cdd:PLN03232 1371 nfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
250 260
....*....|....*....|.
gi 15597586 231 DSANDERPAHPSAGVERHLQA 251
Cdd:PLN03232 1450 YDSPQELLSRDTSAFFRMVHS 1470
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
31-230 |
5.64e-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: 56.88 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLM---------------------NILGCLDRPssgsyhfaghDVAELD------ 83
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKP----------DVDSIEglspai 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 84 SDEQAWLR---REAFGFVFQGYHLipsasaqenveMPAIYAGIPASERhtraRALLERLGLA----ERTANrphQLSGGQ 156
Cdd:cd03270 81 AIDQKTTSrnpRSTVGTVTEIYDY-----------LRLLFARVGIRER----LGFLVDVGLGyltlSRSAP---TLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 157 QQRVSIARALMNG--GHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEV------RDGEI 228
Cdd:cd03270 143 AQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEI 222
|
..
gi 15597586 229 VS 230
Cdd:cd03270 223 VA 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-242 |
1.35e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIE-------LRDIRK------RYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFa 75
Cdd:PTZ00265 366 PLVEnnddgkkLKDIKKiqfknvRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 76 gHDVAELDSDEQAWLRREaFGFVFQG----------------YHL----------------------------------- 104
Cdd:PTZ00265 445 -NDSHNLKDINLKWWRSK-IGVVSQDpllfsnsiknnikyslYSLkdlealsnyynedgndsqenknkrnscrakcagdl 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 105 ---IPSASAQENVEMPAIYAGIPASER---------HTRARALLERLglAERTANRPHQLSGGQQQRVSIARALMNGGHI 172
Cdd:PTZ00265 523 ndmSNTTDSNELIEMRKNYQTIKDSEVvdvskkvliHDFVSALPDKY--ETLVGSNASKLSGGQKQRISIARAIIRNPKI 600
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 173 ILADEPTGALDSHSGAEVMALLDEL-ASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDERPAHPS 242
Cdd:PTZ00265 601 LILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDPT 671
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-229 |
1.63e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELdsdEQAWLRREAfgFVFQGYHLIPSAS 109
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL---SHSVLRQGV--AMVQQDPVVLADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENVEM------PAIYAGIPASERHTRARALLErlGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALD 183
Cdd:PRK10790 431 FLANVTLgrdiseEQVWQALETVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15597586 184 SHSGAEVMALLDELASQGHVVIlITHDRDVAARAKRIIEVRDGEIV 229
Cdd:PRK10790 509 SGTEQAIQQALAAVREHTTLVV-IAHRLSTIVEADTILVLHRGQAV 553
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-228 |
1.64e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.03 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 7 PVPLIELRDIRKRYggngTPEVE-VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSD 85
Cdd:TIGR00957 1281 PRGRVEFRNYCLRY----REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 86 EqawLRREAF-----GFVFQG---YHLIPSASAQENvempAIYAGIPASERHTRARALLErlGLAERTANRPHQLSGGQQ 157
Cdd:TIGR00957 1357 D---LRFKITiipqdPVLFSGslrMNLDPFSQYSDE----EVWWALELAHLKTFVSALPD--KLDHECAEGGENLSVGQR 1427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597586 158 QRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLdELASQGHVVILITHDRDVAARAKRIIEVRDGEI 228
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-229 |
1.84e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNgtPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCL-----------------------DRP 67
Cdd:PTZ00265 1166 IEIMDVNFRYISR--PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqDYQ 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 68 SSGSYHFAGHDVAELDSDEQAW-------------------------LR--REAFGFVFQGYHLIpSASAQENVEMPAIY 120
Cdd:PTZ00265 1244 GDEEQNVGMKNVNEFSLTKEGGsgedstvfknsgkilldgvdicdynLKdlRNLFSIVSQEPMLF-NMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 121 AGIPASERHTRARAL---LERLGLAERTANRPH--QLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSgaevmallD 195
Cdd:PTZ00265 1323 ATREDVKRACKFAAIdefIESLPNKYDTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS--------E 1394
|
250 260 270
....*....|....*....|....*....|....*
gi 15597586 196 ELASQGHVVILITHDRDVAARAKRIIEV-RDGEIV 229
Cdd:PTZ00265 1395 KLIEKTIVDIKDKADKTIITIAHRIASIkRSDKIV 1429
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-210 |
2.55e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 19 RYGGNG-------TPEvevlkgvslsihAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSY-----------HFAGhdvA 80
Cdd:PRK13409 82 RYGVNGfklyglpIPK------------EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRG---T 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 81 ELdsdeQAWLRREAFGFV-----FQGYHLIPSA---SAQENVEmpaiyagiPASERhTRARALLERLGLaERTANRP-HQ 151
Cdd:PRK13409 147 EL----QNYFKKLYNGEIkvvhkPQYVDLIPKVfkgKVRELLK--------KVDER-GKLDEVVERLGL-ENILDRDiSE 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELAsQGHVVILITHD 210
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHD 270
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-183 |
2.70e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 20 YGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDsdeqawlRREAFGFVF 99
Cdd:PRK13543 19 FSRNEEP---VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 100 QGYHLIPSASAQENVEMPAIYAGIPASERHTRARALlerLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPT 179
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....
gi 15597586 180 GALD 183
Cdd:PRK13543 166 ANLD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-225 |
3.00e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 9 PLIELRDIRKRYGGNgtpEVEVLKGvslSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYhFAGHDVA------EL 82
Cdd:PRK13409 339 TLVEYPDLTKKLGDF---SLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKISykpqyiKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 83 DSDE--QAWLRREAFGFvfqgyhlipsASAQENVEmpaiyagipaserhtraraLLERLGLaERTANRP-HQLSGGQQQR 159
Cdd:PRK13409 412 DYDGtvEDLLRSITDDL----------GSSYYKSE-------------------IIKPLQL-ERLLDKNvKDLSGGELQR 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 160 VSIARALMNGGHIILADEPTGALDShsgaevmalldelasqghvvilitHDRDVAARA-KRIIEVRD 225
Cdd:PRK13409 462 VAIAACLSRDADLYLLDEPSAHLDV------------------------EQRLAVAKAiRRIAEERE 504
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
43-230 |
3.50e-08 |
|
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: 54.15 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 43 FVAIVGASGSGKSTlmnILGCLD-------RPSSGSYHFAGHDVAELDSDEQAWLR-REAFGfvfQGYHLIPSASAQENV 114
Cdd:cd03240 24 LTLIVGQNGAGKTT---IIEALKyaltgelPPNSKGGAHDPKLIREGEVRAQVKLAfENANG---KKYTITRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 115 empaIYagIPASErhtrARALLERlglaERTanrphQLSGGQQQ------RVSIARALMNGGHIILADEPTGALDSHSGA 188
Cdd:cd03240 98 ----IF--CHQGE----SNWPLLD----MRG-----RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15597586 189 EVMA-LLDELASQGHV-VILITHDRDVAARAKRIIEV-RDGEIVS 230
Cdd:cd03240 159 ESLAeIIEERKSQKNFqLIVITHDEELVDAADHIYRVeKDGRQKS 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-183 |
4.30e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.86 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 11 IELRDIRKRYGGNGTPeveVLKGVSLSIHAGEFVAIVGASGSGKSTLMN-ILGCLDrpSSGSYHFAGhdVAELDSDEQAW 89
Cdd:cd03289 3 MTVKDLTAKYTEGGNA---VLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDG--VSWNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 90 lrREAFGFVFQGYhLIPSASAQENVEmPaiyAGIPASERHTRaraLLERLGLAERTANRPHQ-----------LSGGQQQ 158
Cdd:cd03289 76 --RKAFGVIPQKV-FIFSGTFRKNLD-P---YGKWSDEEIWK---VAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQ 145
|
170 180
....*....|....*....|....*
gi 15597586 159 RVSIARALMNGGHIILADEPTGALD 183
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-210 |
4.40e-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: 56.33 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 19 RYGGNG-------TPEvevlkgvslsihAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHfaghdvAELDSDEQawLR 91
Cdd:COG1245 82 RYGENGfrlyglpVPK------------KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD------EEPSWDEV--LK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 ReafgfvFQGYHL-----------IPSASAQENVEM-PAIYAGIP------ASERhTRARALLERLGLaERTANRP-HQL 152
Cdd:COG1245 142 R------FRGTELqdyfkklangeIKVAHKPQYVDLiPKVFKGTVrellekVDER-GKLDELAEKLGL-ENILDRDiSEL 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 153 SGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHD 210
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-211 |
1.43e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMNI-LGCLdRPSSGSYHFAGH-DVAELDSdeqawlRREAfgfvfqgyhLIPSA 108
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRIHCGTKlEVAYFDQ------HRAE---------LDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 109 SAQENVEMPAIYAGIPASERHtrARALLERLGLAERTANRP-HQLSGGQQQRVSIARALMNGGHIILADEPTGALDshsg 187
Cdd:PRK11147 399 TVMDNLAEGKQEVMVNGRPRH--VLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD---- 472
|
170 180
....*....|....*....|....*.
gi 15597586 188 AEVMALLDELAS--QGhVVILITHDR 211
Cdd:PRK11147 473 VETLELLEELLDsyQG-TVLLVSHDR 497
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-229 |
2.22e-07 |
|
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: 54.25 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARALM---NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIE------ 222
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDlgpegg 909
|
....*..
gi 15597586 223 VRDGEIV 229
Cdd:TIGR00630 910 DGGGTVV 916
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-209 |
2.86e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 29 EVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLD--RPSSGSYHFAGHDVAELDSDEQAwlrREAFGFVFQGYHLIP 106
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 107 SAS----AQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQ-----LSGGQQQRVSIARALMNGGHIILADE 177
Cdd:PRK09580 92 GVSnqffLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRsvnvgFSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190
....*....|....*....|....*....|..
gi 15597586 178 PTGALDSHSGAEVMALLDELASQGHVVILITH 209
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-209 |
3.50e-07 |
|
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: 50.62 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFaghdvaeldsdeqawLRREAFGFVFQ-GYhlIPSA 108
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQrPY--LPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 109 SAQENVempaIYagiPASERhtrarallerlglaertanrphqLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGA 188
Cdd:cd03223 79 TLREQL----IY---PWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 15597586 189 EVMALLDELasqGHVVILITH 209
Cdd:cd03223 129 RLYQLLKEL---GITVISVGH 146
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-226 |
3.98e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.68 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 134 ALLERLGLAERTANRP-HQLSGGQQQRVSIARAL---MNGGHIILaDEPTGALDSHSGAEVMALLDELASQGHVVILITH 209
Cdd:PRK00635 458 SILIDLGLPYLTPERAlATLSGGEQERTALAKHLgaeLIGITYIL-DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536
|
90
....*....|....*..
gi 15597586 210 DRDVAARAKRIIEVRDG 226
Cdd:PRK00635 537 DEQMISLADRIIDIGPG 553
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-208 |
7.80e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 16 IRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGC----LDRPSSGSYHFAGHDVAELdsdeqawLR 91
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEI-------KK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 92 REAFGFVFQG---YHLiPSASAQENVEMPAI-------YAGIPASERHTRARALLER-LGLAErTANRP------HQLSG 154
Cdd:TIGR00956 135 HYRGDVVYNAetdVHF-PHLTVGETLDFAARcktpqnrPDGVSREEYAKHIADVYMAtYGLSH-TRNTKvgndfvRGVSG 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15597586 155 GQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILIT 208
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
41-227 |
1.37e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.52 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 41 GEFVAIVGASGSGKSTLMNILGcldrpssGSYHFAGHDVAELDSDeqawlrreafgfvfqgyhlipsasaqenvempaiy 120
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA-------RELGPPGGGVIYIDGE----------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 121 agipaserhtRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQ 200
Cdd:smart00382 40 ----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 15597586 201 GHV------VILITHDRDV------AARAKRIIEVRDGE 227
Cdd:smart00382 110 LLKseknltVILTTNDEKDlgpallRRRFDRRIVLLLIL 148
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-223 |
2.50e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 129 HTRARALLErLGLAERTANRP-HQLSGGQQQRVSIARALMNGGH---IILADEPTGALDSHSGAEVMALLDELASQGHVV 204
Cdd:PRK00635 787 HEKIHALCS-LGLDYLPLGRPlSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTV 865
|
90
....*....|....*....
gi 15597586 205 ILITHDRDVAARAKRIIEV 223
Cdd:PRK00635 866 VIIEHNMHVVKVADYVLEL 884
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-183 |
4.43e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 30 VLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLdRPSSGSYHFAGhdVAELDSDEQAWlrREAFGFVFQGYhLIPSAS 109
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG--VSWNSVTLQTW--RKAFGVIPQKV-FIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 110 AQENVEMPAIYagipASERHTRaraLLERLGLAERTANRPHQ-----------LSGGQQQRVSIARALMNGGHIILADEP 178
Cdd:TIGR01271 1308 FRKNLDPYEQW----SDEEIWK---VAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
....*
gi 15597586 179 TGALD 183
Cdd:TIGR01271 1381 SAHLD 1385
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
31-61 |
1.13e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.92 E-value: 1.13e-05
10 20 30
....*....|....*....|....*....|..
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMN-IL 61
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTL 656
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
152-208 |
1.21e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILIT 208
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-207 |
1.78e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 26 PEVEVLKGVSLSIHAGEFVAIVGASGSGKSTL-MNILG-CLDRPSSGSYHFAGHDVaELDSDEQAWlrREAFGFVFQ--- 100
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrSYGRNISGTVFKDGKEV-DVSTVSDAI--DAGLAYVTEdrk 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 101 GYHLIPSASAQENVEMPAIYA----GIPASERHTR-ARALLERL-----GLAERTANrphqLSGGQQQRVSIARALMNGG 170
Cdd:NF040905 348 GYGLNLIDDIKRNITLANLGKvsrrGVIDENEEIKvAEEYRKKMniktpSVFQKVGN----LSGGNQQKVVLSKWLFTDP 423
|
170 180 190
....*....|....*....|....*....|....*....
gi 15597586 171 HIILADEPTGALDshSGA--EVMALLDELASQGHVVILI 207
Cdd:NF040905 424 DVLILDEPTRGID--VGAkyEIYTIINELAAEGKGVIVI 460
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
152-229 |
2.59e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARALM---NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEV----- 223
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLgpegg 906
|
....*..
gi 15597586 224 -RDGEIV 229
Cdd:COG0178 907 dGGGEIV 913
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
31-61 |
4.22e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 4.22e-05
10 20 30
....*....|....*....|....*....|..
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMN-IL 61
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
152-230 |
6.86e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.57 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARAL------MNGGHIILA----DEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRII 221
Cdd:cd03279 124 LSGGETFLASLSLALalsevlQNRGGARLEalfiDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRL 203
|
....*....
gi 15597586 222 EVRDGEIVS 230
Cdd:cd03279 204 EVIKTPGGS 212
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-209 |
1.06e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 24 GTPE--VEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGcldRPSSGSYHFAGHDVAELDSDEQAWLRREafGFVFQG 101
Cdd:PLN03140 887 GVTEdrLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA---GRKTGGYIEGDIRISGFPKKQETFARIS--GYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 102 -YHlipsaSAQENVEMPAIYAG-------IPASERHT---RARALLERLGLAERTANRP--HQLSGGQQQRVSIARALMN 168
Cdd:PLN03140 962 dIH-----SPQVTVRESLIYSAflrlpkeVSKEEKMMfvdEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVA 1036
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15597586 169 GGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITH 209
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
44-210 |
1.51e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 44 VAIVGASGSGKSTLMNIL-----GCLDRPSSGSYHFAGHDVA------ELDSDEQAW-LRReafgfvFQG-YHLIPSASA 110
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryalyGKARSRSKLRSDLINVGSEeasvelEFEHGGKRYrIER------RQGeFAEFLEAKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 111 QENVEMPAIYAGIPASER--------HTRARALLERLGLAERTANR----------PHQLSGGQQQRVSIARALmnggHI 172
Cdd:COG0419 100 SERKEALKRLLGLEIYEElkerlkelEEALESALEELAELQKLKQEilaqlsgldpIETLSGGERLRLALADLL----SL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 15597586 173 ILaDepTGALDSHSGAEVMALLDELAsqghvviLITHD 210
Cdd:COG0419 176 IL-D--FGSLDEERLERLLDALEELA-------IITHV 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
31-70 |
1.78e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 1.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSG 70
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG 79
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
66-257 |
2.99e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 66 RPSSGSYHFAGHDVAELdsdeQAWLRREAFGFvFQGYHLIPSasaQENVEMPAIyagipaserhtraRALLERL------ 139
Cdd:TIGR00630 417 KPEALAVTVGGKSIADV----SELSIREAHEF-FNQLTLTPE---EKKIAEEVL-------------KEIRERLgflidv 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 140 GLA----ERTANrphQLSGGQQQRVSIARALMNG--GHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDV 213
Cdd:TIGR00630 476 GLDylslSRAAG---TLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDT 552
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15597586 214 AARAKRIIE------VRDGEIVSDSANDERPAHPSAgverhLQADDLSQR 257
Cdd:TIGR00630 553 IRAADYVIDigpgagEHGGEVVASGTPEEILANPDS-----LTGQYLSGR 597
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
123-212 |
4.61e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 123 IPASERHTRARALLERLGL-AERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSgaeVMALLDELASQG 201
Cdd:PLN03073 315 IDAYTAEARAASILAGLSFtPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWP 391
|
90
....*....|.
gi 15597586 202 HVVILITHDRD 212
Cdd:PLN03073 392 KTFIVVSHARE 402
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
488-654 |
5.81e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 42.76 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 488 VIIAAADAQRVHQAERAIDQL--MLRLHRGQRDYELTNNAA-----MIQAEAKTQNTLSLMLGSIAAISLLvggIGVMNI 560
Cdd:pfam12698 103 VYINSSNLLVSKLILNALQSLlqQLNASALVLLLEALSTSApipveSTPLFNPQSGYAYYLVGLILMIIIL---IGAAII 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 561 MLMTVRERTREIGIRM-ATGARqgdILRQFLTEAAMLSVVGGL-AGIALALCIGGVLLLGQVAVAFsLSAIVGAFSCALV 638
Cdd:pfam12698 180 AVSIVEEKESRIKERLlVSGVS---PLQYWLGKILGDFLVGLLqLLIILLLLFGIGIPFGNLGLLL-LLFLLYGLAYIAL 255
|
170
....*....|....*.
gi 15597586 639 TGLVFGFMPARKAAQL 654
Cdd:pfam12698 256 GYLLGSLFKNSEDAQS 271
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
152-227 |
7.18e-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: 41.02 E-value: 7.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597586 152 LSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGH-VVILITHDRDVAARAKRIIEVRDGE 227
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
31-76 |
9.24e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 9.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAG 76
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
46-209 |
1.73e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 46 IVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAEldsdeqawLRREAFGFVFQGYHLIPSASAQENVEMPA-IY---A 121
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN--------IAKPYCTYIGHNLGLKLEMTVFENLKFWSeIYnsaE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 122 GIPASERHTRARALLERlglaertanRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQG 201
Cdd:PRK13541 103 TLYAAIHYFKLHDLLDE---------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSG 173
|
....*...
gi 15597586 202 HVVILITH 209
Cdd:PRK13541 174 GIVLLSSH 181
|
|
| FtsX |
COG2177 |
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning]; |
536-648 |
1.98e-03 |
|
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441780 [Multi-domain] Cd Length: 292 Bit Score: 40.58 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 536 NTLSLMLGSIAAISLLVGGIGVMNIMLMTVRERTREIGI-RMAtGARQGDILRQFLTEAAMLSVVGGLagIALALCIGGV 614
Cdd:COG2177 164 NLLRLVGLVLAALLLLAAVLLIGNTIRLAIYSRREEIEImKLV-GATDGFIRRPFLLEGALLGLLGGL--LALLLLALLY 240
|
90 100 110
....*....|....*....|....*....|....
gi 15597586 615 LLLGQvAVAFSLsAIVGAFSCALVTGLVFGFMPA 648
Cdd:COG2177 241 LLLVS-ALADGL-AFLSLLSLGGLLLLLLLLLLL 272
|
|
| PRK11146 |
PRK11146 |
lipoprotein-releasing ABC transporter permease subunit LolE; |
551-663 |
2.29e-03 |
|
lipoprotein-releasing ABC transporter permease subunit LolE;
Pssm-ID: 236860 [Multi-domain] Cd Length: 412 Bit Score: 41.04 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 551 LVGGIGVMNI---MLMTVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALalcigGVLllgqvaVAFSLS 627
Cdd:PRK11146 276 LVIGVACFNIvstLVMAVKDKSGDIAILRTLGAKDGLIRAIFVWYGLLAGLKGSLIGVVI-----GVV------VSLNLT 344
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597586 628 AIVGAFS----------------------------CALVTGLVFGFM----PARKAAQLDPVAALASQ 663
Cdd:PRK11146 345 PIIKGIEklighqflsgdiyfidflpselhwldvfYVLVTALVLSLLaswyPARRASKLDPARVLSGQ 412
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
43-63 |
3.80e-03 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 38.60 E-value: 3.80e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
31-57 |
5.02e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 5.02e-03
10 20
....*....|....*....|....*..
gi 15597586 31 LKGVSLSIHAGEFVAIVGASGSGKSTL 57
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
152-229 |
6.23e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597586 152 LSGGQQQRVSIARALM---NGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIE------ 222
Cdd:PRK00349 831 LSGGEAQRVKLAKELSkrsTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDlgpegg 910
|
....*..
gi 15597586 223 VRDGEIV 229
Cdd:PRK00349 911 DGGGEIV 917
|
|
|