|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-644 |
0e+00 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 746.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDL 82
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKHQVKSAVKNP------ 236
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTepvvnt 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 237 ----SVFKGRFgfskdqlMEAFRMSVSAIVAHKMRSLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGTNTMTIFN 312
Cdd:PRK10535 244 asgwRQFVSGF-------REALTMAWRAMAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRAIGTNTIDIYP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 313 GNGFGDRRSRHIQNLKISDANTLSKQSYIQSVTPNTSSSGILVVGNKSfTSANLYGISEQYFDVEGLKLKQGRLLTEDDV 392
Cdd:PRK10535 317 GKDFGDDDPQYQQALKYDDLIAIQKQPWVASATPAVSQSLRLRYGNID-VAASANGVSGDYFNVYGMTFSEGNTFNQEQL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 393 DQSNQVVVLDESAKKAIFANE-NPLGKTVIFNKRPFRVIGVVSDQQLGGFPGNSLNLYSPYSTVLNKITGGSRIGSITVK 471
Cdd:PRK10535 396 NGRAQVVVLDSNTRRQLFPHKaDVVGEVILVGNMPATVIGVAEEKQSMFGSSKVLRVWLPYSTMSGRVMGQSWLNSITVR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 472 ISDDVNSTVAEKSLTELLKSLHGKKDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEI 551
Cdd:PRK10535 476 VKEGYDSAEAEQQLTRLLTLRHGKKDFFTWNMDSVLKTAEKTTRTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREI 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 552 GVRMAIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFNSFITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKK 631
Cdd:PRK10535 556 GIRMAVGARASDVLQQFLIEAVLVCLVGGALGITLSLLIAFTLQLFLPGWEIGFSPLALLSAFLCSTVTGILFGWLPARN 635
|
650
....*....|...
gi 1040783748 632 AAELNPITALAQE 644
Cdd:PRK10535 636 AARLDPVDALARE 648
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
3.11e-127 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 374.38 E-value: 3.11e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MN-IIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQL 79
Cdd:COG1136 1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALM 159
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAASANRIIEIKDGEIISDTQ 225
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-220 |
3.91e-110 |
|
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: 330.22 E-value: 3.91e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| SalY |
COG0577 |
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms]; |
252-644 |
3.47e-102 |
|
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
Pssm-ID: 440342 [Multi-domain] Cd Length: 339 Bit Score: 314.53 E-value: 3.47e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 252 EAFRMSVSAIVAHKMRSLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGTNTMTIFNGNGFGDrrsrhiQNLKISD 331
Cdd:COG0577 1 EYLRLALRSLRRNKLRSLLTVLGIAIGIALVIAILALGRGLRRSLLRDLDSLGFDLLTVSRTPGGSR------ATLSYED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 332 A-NTLSKQSYIQSVTPNTSSSGILVVGNKSFTSANLYGISEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIF 410
Cdd:COG0577 75 LrEALRALPGVESVAPSSSGSATVRYGGGEPPSVRVLGVDPDYFRVLGIPLLAGRFFTAADDLGAPPVVVIGEALARRLF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 411 ANENPLGKTVIFNKRPFRVIGVVSDQqlggfpgnslnlyspystvlnkitggsrigsitvkisddvnstvaeksLTELLK 490
Cdd:COG0577 155 GGEDPVGKTIRLNGRPFTVVGVVEAE------------------------------------------------LRALLR 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 491 SLHGKKDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLI 570
Cdd:COG0577 187 RRDPGDDFEVQTLDEILAALYGVLRTLTLLLGAIAGLALLVACIGIMNLMLASVTERTREIGIRKALGASRRDILRQFLT 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 571 EAVLICLIGGVAGILLSVLIGVLFNSFiTDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALAQE 644
Cdd:COG0577 267 EALLLALLGGLLGLLLALLLLRLLAAL-LGLPVSLDPWVLLLALALSLLVGLLAGLYPARRAARLDPVEALRSE 339
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-225 |
4.61e-84 |
|
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: 263.53 E-value: 4.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSD 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQrlERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAASANRIIEIKDGEIISDTQ 225
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-226 |
7.73e-77 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 244.19 E-value: 7.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDL 82
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASAN-RIIEIKDGEIISDTQK 226
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEAR 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-236 |
4.91e-71 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 229.88 E-value: 4.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGkETIELTNDQLSDL 82
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDG-EDLTDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRYNLLSSLTAAENVALPAIYA-GMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 162 GEIILADEPTGALDShsgENVMEIL---RQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKSAVKNP 236
Cdd:COG1126 155 PKVMLFDEPTSALDP---ELVGEVLdvmRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-221 |
1.31e-70 |
|
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: 228.23 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDL 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKH-IAASANRIIEIKDGEII 221
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEvVKRICDRVAVMEKGEVV 220
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
22-220 |
4.96e-70 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 226.52 E-value: 4.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLT 101
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1040783748 182 VMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:NF038007 180 VLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-221 |
1.03e-69 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 229.58 E-value: 1.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDL 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD----KHIaasANRIIEIKDGEII 221
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEmdvvRRI---CDRVAVLENGRIV 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-202 |
1.71e-68 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 223.81 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDqls 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 dlrsqkFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMN 160
Cdd:COG1116 82 ------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD 202
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHD 198
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-223 |
7.88e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 219.16 E-value: 7.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDL 82
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQkFGFIFQRYNLLSSLTAAENV---------ALPAIYAGMPQNQRlERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVS 153
Cdd:COG3638 79 RRR-IGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSLLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 154 IARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVVFD 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-213 |
1.14e-65 |
|
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: 215.03 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQlsdlr 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sqkfGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03293 76 ----GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 164 IILADEPTGALDSHSGENVM-EILRQLHEEGHTIIMVTHDKHIAAS-ANRII 213
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQeELLDIWRETGKTVLLVTHDIDEAVFlADRVV 203
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-215 |
1.80e-65 |
|
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: 214.02 E-value: 1.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 21 HVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSL 100
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGE 180
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1040783748 181 NVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEI 215
Cdd:TIGR03608 172 EVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-220 |
1.78e-63 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 208.92 E-value: 1.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELTNDQLSDLR 83
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK-LTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYA-GMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIA-ASANRIIEIKDGEI 220
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-219 |
1.97e-63 |
|
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: 208.64 E-value: 1.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDL 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGE 219
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-220 |
2.75e-60 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 201.16 E-value: 2.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSD 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-223 |
7.32e-59 |
|
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: 197.79 E-value: 7.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLR 83
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQkFGFIFQRYNLLSSLTAAENV---------ALPAIYAGMPQNQRlERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSI 154
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENVlsgrlgrrsTWRSLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 155 ARALMNGGEIILADEPTGALDSHSGENVMEILRQLH-EEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFD 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-223 |
1.97e-58 |
|
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: 196.01 E-value: 1.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLN-RYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETielTNDQLSDL 82
Cdd:COG1122 1 IELENLSfSYPGG----TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:COG1122 74 R-RKVGLVFQNPdDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISD 223
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-221 |
7.73e-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: 194.26 E-value: 7.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDL 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSqKFGFIFQryNLLSSL----TAAENVALPAIYAGMP--QNQRLERAKQLLEKLGLGDKWQNK-PNQLSGGQQQRVSIA 155
Cdd:cd03257 81 RK-EIQMVFQ--DPMSSLnprmTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 156 RALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
2.17e-57 |
|
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: 202.06 E-value: 2.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGE-GENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSD 81
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRsQKFGFIFQryNLLSSL----TAAENVALPA-IYAGMPQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGGQQQRVSIA 155
Cdd:COG1123 340 LR-RRVQMVFQ--DPYSSLnprmTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 156 RALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-221 |
7.16e-57 |
|
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: 192.12 E-value: 7.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSD 81
Cdd:COG1127 4 PMIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRsQKFGFIFQRYNLLSSLTAAENVALPAI-YAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMN 160
Cdd:COG1127 80 LR-RRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-221 |
2.39e-56 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 194.55 E-value: 2.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqLS 80
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD--------VT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQK--FGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:COG3842 71 GLPPEKrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALAlADRIAVMNDGRIE 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-233 |
8.96e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 189.12 E-value: 8.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIEltndQLSDLR 83
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQKHQVKSAV 233
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-223 |
1.35e-55 |
|
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: 189.05 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLSDL 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTD---ITKLRGKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RS--QKFGFIFQRYNLLSSLTAAENVALPAIYA--------GMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRV 152
Cdd:TIGR02315 75 RKlrRRIGMIFQHYNLIERLTVLENVLHGRLGYkptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKyADRIVGLKAGEIVFD 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
22-219 |
7.58e-55 |
|
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: 185.75 E-value: 7.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdlrsQKFGFIFQRYNL-LSSL 100
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPDDqFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGE 180
Cdd:cd03225 92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1040783748 181 NVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGE 219
Cdd:cd03225 172 ELLELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-221 |
8.11e-55 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 190.40 E-value: 8.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLR 83
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD----KHIaasANRIIEIKDGEII 221
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEmdvvKRI---CDRVAVIDAGRLV 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-220 |
1.07e-54 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 186.17 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 8 QLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRSQKF 87
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 88 GFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILA 167
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 168 DEPTGALDSHSGENVMEILRQLH-EEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-238 |
6.45e-54 |
|
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: 184.24 E-value: 6.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLR 83
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAG-MPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKsAVKNPSV 238
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELR-ASDDPLV 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-221 |
1.10e-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: 182.72 E-value: 1.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetieltndQLSDLR 83
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR--------DVTGVP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQK--FGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:cd03259 69 PERrnIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALAlADRIAVMNEGRIV 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-220 |
2.02e-53 |
|
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: 182.22 E-value: 2.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLR 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHI-AASANRIIEIKDGEI 220
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-223 |
5.47e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 179.13 E-value: 5.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltNDQLSDL 82
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV----NDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RS--QKFGFIFQRYNLLSSLTAAENVAL-PAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALM 159
Cdd:PRK09493 73 RLirQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAED 217
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-220 |
8.62e-52 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 179.23 E-value: 8.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGkETIELTND------ 77
Cdd:COG4598 9 LEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG-EEIRLKPDrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 78 -----QLSDLRSQkFGFIFQRYNLLSSLTAAENVALPAIYA-GMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQR 151
Cdd:COG4598 84 padrrQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEAPVHVlGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDShsgENVMEIL---RQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDP---ELVGEVLkvmRDLAEEGRTMLVVTHEMGFARDvSSHVVFLHQGRI 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
6.13e-51 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 179.88 E-value: 6.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqLS 80
Cdd:COG3839 1 MASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD--------VT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQK--FGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:COG3839 69 DLPPKDrnIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTlADRIAVMNDGRI 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
1.90e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 175.20 E-value: 1.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKE---TIELTNDQLS 80
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRsQKFGFIFQRYNLLSSLTAAEN-VALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALM 159
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIA-ASANRIIEIKDGEII 221
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRII 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-221 |
3.96e-50 |
|
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: 175.14 E-value: 3.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFG-----------EGENRVHVLK---------DISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGS 63
Cdd:cd03294 1 IKIKGLYKIFGknpqkafkllaKGKSKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 64 YKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQ 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 144 LSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRlGDRIAIMKDGRLV 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-219 |
4.51e-50 |
|
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: 171.99 E-value: 4.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGkETIELTNDQLSDLR 83
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG-EDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPaiyagmpqnqrlerakqlleklglgdkwqnkpnqLSGGQQQRVSIARALMNGGE 163
Cdd:cd03229 76 -RRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGE 219
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-236 |
1.07e-49 |
|
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: 173.45 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetiELTNDQLSDLR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYnlLSSL----TAAENVALPAIYAGMPQNQrlERAKQLLEKLGLGDKWQNK-PNQLSGGQQQRVSIARAL 158
Cdd:COG1124 79 -RRVQMVFQDP--YASLhprhTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKH-IAASANRIIEIKDGEIISDTQKHQVKSAVKNP 236
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAvVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-220 |
1.89e-49 |
|
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: 176.00 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqLSDLR 83
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRD--------ITRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQK--FGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:TIGR03265 73 PQKrdYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:TIGR03265 153 PGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSmADRIVVMNHGVI 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-240 |
4.94e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 174.56 E-value: 4.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetieltnDQLSDLR 83
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR-------DLFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQ--KFGFIFQRYNLLSSLTAAENVA--LPAiyAGMPQNQRLERAKQLLEKL---GLGDKwqnKPNQLSGGQQQRVSIAR 156
Cdd:COG1118 72 PRerRVGFVFQHYALFPHMTVAENIAfgLRV--RPPSKAEIRARVEELLELVqleGLADR---YPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKSAVK 234
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
....*.
gi 1040783748 235 NPSVFK 240
Cdd:COG1118 227 TPFVAR 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-229 |
1.08e-48 |
|
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: 178.17 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATG---GSYKIDGKETIELTndql 79
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELS---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRSQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:COG1123 78 EALRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQV 229
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-229 |
3.32e-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: 168.51 E-value: 3.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTL---MN-IIGCLDTA-TGGSYKIDGKETIELTNDQ 78
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLlrlLNrLNDLIPGApDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 79 LSdLRsQKFGFIFQRYNLLSsLTAAENVALPAIYAGMPQNQRL-ERAKQLLEKLGLGDKWQNKPN--QLSGGQQQRVSIA 155
Cdd:cd03260 77 LE-LR-RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 156 RALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQV 229
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-220 |
4.21e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 167.69 E-value: 4.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLSDLR 83
Cdd:COG4619 1 LELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP---LSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQkFGFIFQRynllSSL---TAAENVALPAIYAGMPQNQrlERAKQLLEKLGLGDKWQNKP-NQLSGGQQQRVSIARALM 159
Cdd:COG4619 74 RQ-VAYVPQE----PALwggTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKH-IAASANRIIEIKDGEI 220
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
4.25e-48 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 169.16 E-value: 4.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFgegeNRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYK-----IDGKETIELT 75
Cdd:PRK11264 1 MSAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 NDQLSDLRsQKFGFIFQRYNLLSSLTAAENVAL-PAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSI 154
Cdd:PRK11264 77 KGLIRQLR-QHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 155 ARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIV 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
7.65e-48 |
|
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: 167.80 E-value: 7.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQlsdlr 83
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTmSDRIAVMNKGKI 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-221 |
2.76e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 166.73 E-value: 2.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKE---TIELTNDQLS 80
Cdd:PRK11124 3 IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRsQKFGFIFQRYNLLSSLTAAEN-VALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALM 159
Cdd:PRK11124 79 ELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIA-ASANRIIEIKDGEII 221
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIV 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
3.17e-47 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 166.96 E-value: 3.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQls 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 dlrsqkfGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMN 160
Cdd:COG4525 79 -------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHD 202
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-264 |
6.96e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 165.65 E-value: 6.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqlS 80
Cdd:COG1121 4 MPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP---------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQKFGFIFQRYNLLSS--LTAAENVALpAIYAGMPQNQRL-----ERAKQLLEKLGLGDKWqNKP-NQLSGGQQQRV 152
Cdd:COG1121 71 RRARRRIGYVPQRAEVDWDfpITVRDVVLM-GRYGRRGLFRRPsradrEAVDEALERVGLEDLA-DRPiGELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIkDGEIISDTQKHQVks 231
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDlGAVREYFDRVLLL-NRGLVAHGPPEEV-- 225
|
250 260 270
....*....|....*....|....*....|...
gi 1040783748 232 avknpsvfkgrfgFSKDQLMEAFRMSVSAIVAH 264
Cdd:COG1121 226 -------------LTPENLSRAYGGPVALLAHG 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-221 |
1.20e-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: 162.08 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVhvlKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELtndQLSDLR 83
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDK--WQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-223 |
2.94e-45 |
|
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: 161.36 E-value: 2.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLN-RYfgegeNRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqLSD 81
Cdd:COG1120 1 MLEAENLSvGY-----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD--------LAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 L----RSQKFGFIFQRYNLLSSLTAAENVAL---PAIYA-GMPQNQRLERAKQLLEKLGLGDkWQNKP-NQLSGGQQQRV 152
Cdd:COG1120 68 LsrreLARRIAYVPQEPPAPFGLTVRELVALgryPHLGLfGRPSAEDREAVEEALERTGLEH-LADRPvDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 153 SIARALMNGGEIILADEPTGALD-SHSGEnVMEILRQL-HEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISD 223
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlAHQLE-VLELLRRLaRERGRTVVMVLHDlNLAARYADRLVLLKDGRIVAQ 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-206 |
5.40e-45 |
|
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: 162.92 E-value: 5.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLD--TATGGSYKIDGKETIELTNDQL 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRSQKFGFIFQryNLLSSL----TAAENVALP-AIYAGMPQNQRLERAKQLLEKLGLGDKWQ--NK-PNQLSGGQQQR 151
Cdd:COG0444 81 RKIRGREIQMIFQ--DPMTSLnpvmTVGDQIAEPlRIHGGLSKAEARERAIELLERVGLPDPERrlDRyPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD----KHIA 206
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDlgvvAEIA 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-220 |
9.77e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 162.95 E-value: 9.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqlsdLR 83
Cdd:PRK10851 3 IEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH------AR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQKFGFIFQRYNLLSSLTAAENVALpaiyaG---MPQNQRLERA------KQLLEKLGLGDKWQNKPNQLSGGQQQRVSI 154
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAF-----GltvLPRRERPNAAaikakvTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 155 ARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
1.08e-43 |
|
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: 157.59 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLnrYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieLTNDQLSDLR 83
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQR-YNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL-MNg 161
Cdd:TIGR04520 77 -KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLaMR- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLH-EEGHTIIMVTHDKHIAASANRIIEIKDGEIISD 223
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNkEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-216 |
1.39e-42 |
|
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: 152.69 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 18 NRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqLSDLRSqKFGFIFQRYNLL 97
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP--------LEKERK-RIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SS--LTAAENVALpAIYAGMPQNQRL-----ERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEP 170
Cdd:cd03235 81 RDfpISVRDVVLM-GLYGHKGLFRRLskadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1040783748 171 TGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIK 216
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYFDRVLLLN 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-239 |
5.24e-42 |
|
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: 152.11 E-value: 5.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELtndqlsDLR 83
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQKFGFIFQRYNLLSSLTAAENVA----LPAIYAGMPQNQRLERAKQLLEKLGLgDKWQNK-PNQLSGGQQQRVSIARAL 158
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQL-DWLADRyPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKSAVKNP 236
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
...
gi 1040783748 237 SVF 239
Cdd:cd03296 232 FVY 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-219 |
8.01e-42 |
|
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: 149.07 E-value: 8.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNryFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLR 83
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG---VDLRDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQkFGFIFQRYNLLSSlTAAENValpaiyagmpqnqrlerakqlleklglgdkwqnkpnqLSGGQQQRVSIARALMNGGE 163
Cdd:cd03228 76 KN-IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHeEGHTIIMVTHDKHIAASANRIIEIKDGE 219
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-223 |
1.23e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 150.68 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 21 HVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTnDQLSDLRsqKFGFIFQRYNLLSSL 100
Cdd:COG3840 13 DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LT-ALPPAER--PVSMLFQENNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENVALpAIYAGM----PQNQRLERAkqlLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDS 176
Cdd:COG3840 87 TVAQNIGL-GLRPGLkltaEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1040783748 177 HSGENVMEILRQLHEE-GHTIIMVTHD-KHIAASANRIIEIKDGEIISD 223
Cdd:COG3840 163 ALRQEMLDLVDELCRErGLTVLMVTHDpEDAARIADRVLLVADGRIAAD 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-236 |
3.04e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 150.50 E-value: 3.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELTND---- 77
Cdd:PRK10619 4 NKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQT-INLVRDkdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 78 -------QLSDLRSqKFGFIFQRYNLLSSLTAAENV-ALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGGQ 148
Cdd:PRK10619 79 lkvadknQLRLLRT-RLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 149 QQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKH 227
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPE 237
|
....*....
gi 1040783748 228 QVKSAVKNP 236
Cdd:PRK10619 238 QLFGNPQSP 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-202 |
6.22e-41 |
|
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: 148.77 E-value: 6.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLsdlrsqkfgFIFQRYNLLSSLTA 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 103 AENVALpAIYAGMPQNQRLERAK---QLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSG 179
Cdd:TIGR01184 72 RENIAL-AVDRVLPDLSKSERRAiveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|....
gi 1040783748 180 ENVMEILRQLHEEGH-TIIMVTHD 202
Cdd:TIGR01184 151 GNLQEELMQIWEEHRvTVLMVTHD 174
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-221 |
6.52e-41 |
|
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: 156.84 E-value: 6.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLN-RYfgegENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDL 82
Cdd:COG4988 337 IELEDVSfSY----PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING---VDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQkFGFIFQRyNLLSSLTAAENVALPAIYAGMpqnQRLERAkqlLEKLGLGDKWQNKPN-----------QLSGGQQQR 151
Cdd:COG4988 410 RRQ-IAWVPQN-PYLFAGTIRENLRLGRPDASD---EELEAA---LEAAGLDEFVAALPDgldtplgeggrGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHeEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-221 |
7.64e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 151.01 E-value: 7.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELtndQLSDLR 83
Cdd:COG1125 2 IEFENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDL---DPVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGL-----GDKwqnKPNQLSGGQQQRVSIARAL 158
Cdd:COG1125 76 -RRIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpeeyRDR---YPHELSGGQQQRVGVARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:COG1125 152 AADPPILLMDEPFGALDPITREQLQDELLRLQRElGKTIVFVTHDIDEALKlGDRIAVMREGRIV 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-238 |
1.03e-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: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDL- 82
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 --RSqkfgfiFQRYNLLSSLTAAENVALPA--------IYAGMPQNQR--LERAKQLLEKLGLGDKWQNKPNQLSGGQQQ 150
Cdd:cd03219 77 igRT------FQIPRLFPELTVLENVMVAAqartgsglLLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQV 229
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEV 230
|
....*....
gi 1040783748 230 ksaVKNPSV 238
Cdd:cd03219 231 ---RNNPRV 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-219 |
2.03e-40 |
|
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: 144.69 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 5 EIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDlrs 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 qKFGFIFQrynllssltaaenvalpaiyagmpqnqrlerakqlleklglgdkwqnkpnqLSGGQQQRVSIARALMNGGEI 164
Cdd:cd00267 74 -RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 165 ILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGE 219
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDGK 157
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-220 |
1.32e-39 |
|
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: 144.70 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqLSDLR 83
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD--------VTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQK--FGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:cd03301 69 PKDrdIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIA-ASANRIIEIKDGEI 220
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-232 |
1.68e-39 |
|
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: 154.61 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNryFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLR 83
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG---IDLRQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQkFGFIFQRYNLLSSlTAAENVALPAIYAGMpqnqrlERAKQLLEKLGLGDKWQNKPN-----------QLSGGQQQRV 152
Cdd:COG2274 549 RQ-IGVVLQDVFLFSG-TIRENITLGDPDATD------EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKHQVKSA 232
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-254 |
1.78e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 145.00 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLr 83
Cdd:COG4555 2 IEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sqkfGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:COG4555 77 ----GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGEIIsdtqkhqvksAVKNPSVFKGR 242
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQeVEALCDRVVILHKGKVV----------AQGSLDELREE 222
|
250
....*....|..
gi 1040783748 243 FGfsKDQLMEAF 254
Cdd:COG4555 223 IG--EENLEDAF 232
|
|
| LolE |
COG4591 |
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ... |
423-644 |
2.01e-39 |
|
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: 146.22 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 423 NKRPFRVIGVVSDqqlGGFPGNSLNLYSPYSTVLNKITGGSRIGSITVKISDDVNSTVAEKSLTELLKslhgkkDFFIMN 502
Cdd:COG4591 64 KTRRFTVVGIFES---GGYELDGSLVYVPLETAQELLGLGDQVSGILVKLKDGADAEAVAAALEAALP------GLEVKT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 503 SDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVA 582
Cdd:COG4591 135 WRELNAALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLERTREIGILKALGASRRQIRRIFLLEGLLLGLIGGLL 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 583 GILLSVLIGVLFNS-------FITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALAQE 644
Cdd:COG4591 215 GLLLGLLLALLLNAllgillpFIFALPVSLSPSDVLLALLLALLISLLASLYPARRAARLDPVEALRGE 283
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-220 |
3.86e-39 |
|
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: 141.77 E-value: 3.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLsdlr 83
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENValpaiyagmpqnqrlerakqlleklglgdkwqnkpnQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-222 |
6.47e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.77 E-value: 6.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLN-RYfgeGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLM-NIIGCLDTATGgSYKIDGketIELTNDQL 79
Cdd:PRK13635 4 EIIRVEHISfRY---PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLLLPEAG-TITVGG---MVLSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRsQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:PRK13635 77 WDVR-RQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKHIAASANRIIEIKDGEIIS 222
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
1.52e-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: 149.83 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKS-TLMNIIGCLDTA---TGGSYKIDGKETIELTN 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 77 DQLSDLRSQKFGFIFQryNLLSSL----TAAENVALP-AIYAGMPQNQRLERAKQLLEKLGLGDKwQNK----PNQLSGG 147
Cdd:COG4172 84 RELRRIRGNRIAMIFQ--EPMTSLnplhTIGKQIAEVlRLHRGLSGAAARARALELLERVGIPDP-ERRldayPHQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 148 QQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRfADRVAVMRQGEIV 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
2.29e-38 |
|
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: 141.42 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MN-IIEIKQLNRYF---GEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGS--YKIDGkETIEL 74
Cdd:COG4778 1 MTtLLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDG-GWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 75 TN---DQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDK-WQNKPNQLSGGQQQ 150
Cdd:COG4778 80 AQaspREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDG 218
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEvREAVADRVVDVTPF 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-223 |
2.44e-38 |
|
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: 139.88 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 5 EIKQLNryFGEGENRVhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLsdlrs 84
Cdd:cd03214 1 EVENLS--VGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 qkfgfifqrynllssltaAENVALpaiyagMPQnqrlerakqLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEI 164
Cdd:cd03214 72 ------------------ARKIAY------VPQ---------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 165 ILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-243 |
2.80e-38 |
|
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: 144.56 E-value: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 38 IMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqlSDLRSqkFGFIFQRYNLLSSLTAAENVALPAIYAGMPQ 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP----PHLRH--INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 118 NQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTI 196
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1040783748 197 IMVTHDKHIA-ASANRIIEIKDGEIISDTQKHQVKSAVKNpsVFKGRF 243
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIAQIGTPEEIYEEPAN--LFVARF 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-237 |
2.95e-38 |
|
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: 141.70 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQlsdlr 83
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03299 71 -RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD-KHIAASANRIIEIKDGEIIsdtQKHQVKSAVKNPS 237
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDfEEAWALADKVAIMLNGKLI---QVGKPEEVFKKPK 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-223 |
3.05e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 142.53 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEG-ENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQlsd 81
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 lRSQKFGFIFQryNLL----SSLTAAENVALpAIYAGMP-------QNQRLERAKQLLEKLGLG--DKWQNKPNQLSGGQ 148
Cdd:COG1101 78 -RAKYIGRVFQ--DPMmgtaPSMTIEENLAL-AYRRGKRrglrrglTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 149 QQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHD-KHIAASANRIIEIKDGEIISD 223
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNmEQALDYGNRLIMMHEGRIILD 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
5.74e-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: 137.78 E-value: 5.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLSDLRsQKFGFIFQRYNLLSSLTA 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLR-KEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 103 AENVALPAIYAGMPQNQRLERAKQLLEKLGLGD----KWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-221 |
7.65e-38 |
|
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: 148.38 E-value: 7.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLN-RYFGEGENrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdl 82
Cdd:COG4987 334 LELEDVSfRYPGAGRP---VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 rsQKFGFIFQRYNLLSSlTAAENVALPAIYAGMpqnqrlERAKQLLEKLGLGDKWQNKPN-----------QLSGGQQQR 151
Cdd:COG4987 409 --RRIAVVPQRPHLFDT-TLRENLRLARPDATD------EELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDSHSGENVMEILRQlHEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-229 |
9.78e-38 |
|
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: 140.60 E-value: 9.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTAT-GGSYKIDGKEtieLTNDQL 79
Cdd:COG1119 1 DPLLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGER---RGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRsQKFGF----IFQRYNllSSLTAaENVALPAIYA--GMPQN---QRLERAKQLLEKLGLGDKwQNKP-NQLSGGQQ 149
Cdd:COG1119 74 WELR-KRIGLvspaLQLRFP--RDETV-LDVVLSGFFDsiGLYREptdEQRERARELLELLGLAHL-ADRPfGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 150 QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKH-IAASANRIIEIKDGEIISDTQKH 227
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKE 228
|
..
gi 1040783748 228 QV 229
Cdd:COG1119 229 EV 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-223 |
1.12e-37 |
|
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: 140.56 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLS 80
Cdd:COG0411 2 DPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DL---RSqkfgfiFQRYNLLSSLTAAENVALpAIYAGMPQN----------------QRLERAKQLLEKLGLGDKWQNKP 141
Cdd:COG0411 78 RLgiaRT------FQNPRLFPELTVLENVLV-AAHARLGRGllaallrlprarreerEARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 142 NQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGE 219
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGlADRIVVLDFGR 230
|
....
gi 1040783748 220 IISD 223
Cdd:COG0411 231 VIAE 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-220 |
2.29e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 138.85 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRSQkFGFIFQRYNLLSSLTA 102
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 103 AENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENV 182
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1040783748 183 MEILRQLHEEGHTIIMVTHDKHIAASAN-RIIEIKDGEI 220
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| MacB_PCD |
pfam12704 |
MacB-like periplasmic core domain; This family represents the periplasmic core domain found in ... |
268-488 |
2.31e-37 |
|
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: 138.43 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 268 SLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGtNTMTIFNGNGFGDRRSRhiqNLKISDANTLSKQSYIQSVTPn 347
Cdd:pfam12704 1 TALTVLGIAIGVAAVIAILSLGDGLLSAVPEQISDSD-NLVVVQPGAAGGGGTRP---PLSDPDAEALRRAVPVEAVAP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 348 tSSSGILVVGNKSFTSANLYGISEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIFANENPLGKTVIFNKRPF 427
Cdd:pfam12704 76 -VVSTVRYGNSTTERLVTVVGVDPDFFKVFGLPLAEGRFFTEADVLGGPNVVVLGESLAEKLFGGDDPVGKTIRLNGQPF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 428 RVIGVVSDQQlgGFPGNSLNLYSPYSTVlnKITGGSRIGSITVKISDDVNSTVAEKSLTEL 488
Cdd:pfam12704 155 TVVGVLPDFP--GSDGGGDLVYVPLTTL--QRRLGDSVSTILVRLKDGADLAAAAAELRAL 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-223 |
8.91e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.01 E-value: 8.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltnDQLSDL 82
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-----RFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQKFG--FIFQRYNLLSSLTAAENVAL---PAIYAGMPQNQRLERAKQLLEKLGLG-DkwqnkPNQ----LSGGQQQRV 152
Cdd:COG1129 75 DAQAAGiaIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDiD-----PDTpvgdLSVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISD 223
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRlDEVFEIADRVTVLRDGRLVGT 221
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-235 |
5.31e-36 |
|
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: 135.50 E-value: 5.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGsYKIDGK---ETIELTNDQL 79
Cdd:TIGR00972 1 AIEIENLNLFYGEK----EALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPG-VRIEGKvlfDGQDIYDKKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SD--LRsQKFGFIFQRYNLLSsLTAAENVAL-PAIYAGMPQNQRLERAKQLLEKLGLGDKWQNK----PNQLSGGQQQRV 152
Cdd:TIGR00972 76 DVveLR-RRVGMVFQKPNPFP-MSIYDNIAYgPRLHGIKDKKELDEIVEESLKKAALWDEVKDRlhdsALGLSGGQQQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKS 231
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARiSDRTAFFYDGELVEYGPTEQIFT 232
|
....
gi 1040783748 232 AVKN 235
Cdd:TIGR00972 233 NPKE 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-201 |
5.94e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.93 E-value: 5.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTL------MN--IIGCldtATGGSYKIDGKETIEL 74
Cdd:COG1117 11 KIEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNdlIPGA---RVEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 75 TNDqLSDLRsQKFGFIFQRYNLLSsLTAAENVALPAIYAGMPQNQRL-ERAKQLLEKLGLGDKWQNKPNQ----LSGGQQ 149
Cdd:COG1117 84 DVD-VVELR-RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELdEIVEESLRKAALWDEVKDRLKKsalgLSGGQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 150 QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTH 201
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTH 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-221 |
7.48e-36 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 133.92 E-value: 7.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 5 EIKQLNRYFGEGENrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqlsdlRS 84
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 QKFGFIFQ--RYNLLSSLTAAEnvalpaIYAGMPQ-NQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:cd03226 71 KSIGYVMQdvDYQLFTDSVREE------LLLGLKElDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-202 |
7.52e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 135.60 E-value: 7.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltndqlsDLRSQKFGFIFQRYNLLSSLT 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV---------EGPGAERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 1040783748 182 VMEILRQL-HEEGHTIIMVTHD 202
Cdd:PRK11248 167 MQTLLLKLwQETGKQVLLITHD 188
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
9.39e-36 |
|
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: 132.17 E-value: 9.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltnDQLSDLR 83
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-----SFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQKFGfifqrynllssltaaenVALpaIYagmpqnqrlerakqlleklglgdkwqnkpnQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03216 72 ARRAG-----------------IAM--VY------------------------------QLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-234 |
1.26e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 136.37 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSY----------KIDGKETIELTNDQLSDLRSQKFGFI- 90
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKLVIQKTRFKKIKKIk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 91 -----------FQRYNLLSSlTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKW-QNKPNQLSGGQQQRVSIARAL 158
Cdd:PRK13651 102 eirrrvgvvfqFAEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYlQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQKHQVKSAVK 234
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-223 |
1.66e-35 |
|
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: 133.19 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIE---KGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGkeTIELTNDQLSDLRSQ--KFGFIFQRYNLL 97
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKINLPPQqrKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVALpaIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:cd03297 88 PHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1040783748 178 SGENVMEILRQLHEEGH-TIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:cd03297 166 LRLQLLPELKQIKKNLNiPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
1.79e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.86 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLSD 81
Cdd:PRK13647 3 NIIEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE---VNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRSqKFGFIFQRYN-LLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMN 160
Cdd:PRK13647 77 VRS-KVGLVFQDPDdQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIIS 222
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLA 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-220 |
3.25e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.00 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetieltndQLS 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--------DIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQK--FGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:PRK09452 80 HVPAENrhVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 159 MNGGEIILADEPTGALDsHSGENVMEI-LRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:PRK09452 160 VNKPKVLLLDESLSALD-YKLRKQMQNeLKALQRKlGITFVFVTHDQEEALTmSDRIVVMRDGRI 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-223 |
3.70e-35 |
|
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: 132.23 E-value: 3.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 25 DISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDlrsQKFGFIFQRYNLLSSLTAAE 104
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPAD---RPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 105 NVAL---PAIYAGMPQNQRLERAkqlLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:cd03298 90 NVGLglsPGLKLTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1040783748 182 VMEILRQLH-EEGHTIIMVTHD-KHIAASANRIIEIKDGEIISD 223
Cdd:cd03298 167 MLDLVLDLHaETKMTVLMVTHQpEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-220 |
5.33e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 133.26 E-value: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 6 IKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGsykidgketiELT--NDQLSDLR 83
Cdd:PRK11247 15 LNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG----------ELLagTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALpaiyaGMPQNQRlERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:PRK11247 81 -EDTRLMFQDARLLPWKKVIDNVGL-----GLKGQWR-DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 164 IILADEPTGALDSHSG---ENVMEILRQLHeeGHTIIMVTHDKHIA-ASANRIIEIKDGEI 220
Cdd:PRK11247 154 LLLLDEPLGALDALTRiemQDLIESLWQQH--GFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-228 |
1.15e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 132.44 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFgegeNRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCL---DTATGGSYKIDGKeTIELTNDQL 79
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGR-TVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRSQK--FGFIFQRYNLLSSLTAAENVALPAI---------YAGMPQNQRlERAKQLLEKLGLGDKWQNKPNQLSGGQ 148
Cdd:PRK09984 79 RDIRKSRanTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQK-QRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 149 QQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHE-EGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQK 226
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSS 237
|
..
gi 1040783748 227 HQ 228
Cdd:PRK09984 238 QQ 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-217 |
1.69e-34 |
|
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: 129.91 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenRVhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltNDQLSDLR 83
Cdd:COG4133 3 LEAENLSCRRGE---RL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQkFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQrlERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:COG4133 75 RR-LAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDkHIAASANRIIEIKD 217
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ-PLELAAARVLDLGD 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-221 |
1.85e-34 |
|
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: 130.01 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGenrvHVLKDISLSIEKGDFvAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIEltndQLSDLR 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
2.42e-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: 129.93 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltNDQLSDLR 83
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKH-IAASANRIIEIKDGEII 221
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDeAEALCDRIAIMSDGKLR 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-220 |
4.42e-34 |
|
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: 129.21 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 21 HVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQlsdlrsQKFGFIFQRYNLLSSL 100
Cdd:TIGR01277 12 HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENVAL---PAIYAGMPQNQRLERAKQlleKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:TIGR01277 86 TVRQNIGLglhPGLKLNAEQQEKVVDAAQ---QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1040783748 178 SGENVMEILRQL-HEEGHTIIMVTHD-KHIAASANRIIEIKDGEI 220
Cdd:TIGR01277 163 LREEMLALVKQLcSERQRTLLMVTHHlSDARAIASQIAVVSQGKI 207
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
345-644 |
5.48e-34 |
|
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: 138.41 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 345 TPNTSSSGILVVG-----NKSFTSANLYGISEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIFANENPLGKT 419
Cdd:TIGR03434 503 SGNGWSGGVTIEGrppppPGEEPLADYRRVSPGYFETMGIPLLRGRDFTERDTAGSPPVAIVNEAFARRYFPGEDPIGKR 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 420 VIF---NKRPFRVIGVVSDQQLGGfpgnsLN------LYSPYSTvlnkitGGSRIGSITVKISDDVNSTVAekSLTELLK 490
Cdd:TIGR03434 583 IRLggdDGPWFEIVGVVGDVRYAG-----LDepprpeVYLPYAQ------SPDRGMTLVVRTAGDPAALAA--AVRRAVR 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 491 SLHGkkDFFIMNSDTIKQTIENTTGT---MKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQ 567
Cdd:TIGR03434 650 AIDP--NLPVYDVRTMEEQVDRSLAQerfLALLLGLFAALALLLAAIGLYGVLAYSVAQRTREIGIRMALGAQRGDVLRL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 568 FLIEAVLICLIGGVAGILLSVLIGVLFNSFItdF---SMDFSTASIVTAVLFSTliGVLFGYMPAKKAAELNPITALAQE 644
Cdd:TIGR03434 728 VLRQGLRLAAAGLAIGLAAALALARLLASLL--FgvsPTDPLTFAAVAALLLAV--ALLACYLPARRAARVDPMIALRAE 803
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-223 |
7.58e-34 |
|
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: 128.86 E-value: 7.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLR 83
Cdd:cd03245 3 IEFRNVSFSYPNQEI--PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG---TDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSlTAAENVALPAIYAgmpQNQRLERAkqlLEKLGLGDKWQNKPN-----------QLSGGQQQRV 152
Cdd:cd03245 78 -RNIGYVPQDVTLFYG-TLRDNITLGAPLA---DDERILRA---AELAGVTDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEIISD 223
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-213 |
9.68e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.78 E-value: 9.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYF-------GEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELT 75
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 NDQLSDLRsQKFGFIFQryNLLSSL----TAAENVALPAIYAGM-PQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGGQQ 149
Cdd:COG4608 87 GRELRPLR-RRMQMVFQ--DPYASLnprmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRyPHEFSGGQR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 150 QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD----KHIaasANRII 213
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDlsvvRHI---SDRVA 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-221 |
2.08e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 129.75 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIdGKETI--ELTNDQLSDLRsQKFGFIFQ-RYNLLSS 99
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVItaGKKNKKLKPLR-KKVGIVFQfPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHS 178
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1040783748 179 GENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:PRK13634 181 RKEMMEMFYKLHKEkGLTTVLVTHSMEDAARyADQIVVMHKGTVF 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-221 |
2.28e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 135.29 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqLSDLRSQkFGFIFQRYNLLsSLT 101
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQ-IGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGMpqnQRLERAkqlLEKLGLGDKWQNKPN-----------QLSGGQQQRVSIARALMNGGEIILADEP 170
Cdd:COG1132 430 IRENIRYGRPDATD---EEVEEA---AKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 171 TGALDSHSGENVMEILRQLHeEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:COG1132 504 TSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-234 |
7.64e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 127.90 E-value: 7.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLN-RYFGEGENRVH-VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNdqL 79
Cdd:PRK13633 3 EMIKCKNVSyKYESNEESTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRsQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:PRK13633 81 WDIR-NKAGMVFQNPdNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKHQVKSAVK 234
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-215 |
9.58e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 125.29 E-value: 9.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLDTA--TGGSYKIDGKEtieltndqLSDL--RSQKFGFIFQRYNLL 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRR--------LTALpaEQRRIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVALpAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:COG4136 89 PHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1040783748 178 SGENVME-ILRQLHEEGHTIIMVTHDKHIAASANRIIEI 215
Cdd:COG4136 168 LRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-213 |
1.07e-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: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLN-RYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDqlsDL 82
Cdd:TIGR02857 322 LEFSGVSvAYPGRRP----ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---SW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQkFGFIFQRYNLLSSlTAAENVALPAIYAGMPQNQRLERAKQLLEKL-GLGDKWQNK----PNQLSGGQQQRVSIARA 157
Cdd:TIGR02857 395 RDQ-IAWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVaALPQGLDTPigegGAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 158 LMNGGEIILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRII 213
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIV 527
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
2.87e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.96 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELTNDQLSDL 82
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP-IKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:PRK13639 77 R-KTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIIS 222
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIK 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-236 |
5.73e-32 |
|
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: 131.91 E-value: 5.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNryFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTndQL--SD 81
Cdd:TIGR03375 464 IEFRNVS--FAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG---VDIR--QIdpAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRsQKFGFIFQRYNLLSSlTAAENVALPAIYAGmpqNQRLERAkqlLEKLGLGDKWQNKPN-----------QLSGGQQQ 150
Cdd:TIGR03375 537 LR-RNIGYVPQDPRLFYG-TLRDNIALGAPYAD---DEEILRA---AELAGVTEFVRRHPDgldmqigergrSLSGGQRQ 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKHQVK 230
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVL 687
|
....*.
gi 1040783748 231 SAVKNP 236
Cdd:TIGR03375 688 EALRKG 693
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-221 |
6.38e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.76 E-value: 6.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELTNDQlsDL 82
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-VRIRSPR--DA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQKFGFIFQRYNLLSSLTAAENVALpaiyaGMPQNQRL--------ERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSI 154
Cdd:COG3845 78 IALGIGMVHQHFMLVPNLTVAENIVL-----GLEPTKGGrldrkaarARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 155 ARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKlREVMAIADRVTVLRRGKVV 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
6.62e-32 |
|
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: 123.25 E-value: 6.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDG----KETIELtndql 79
Cdd:cd03265 1 IEVENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 sdlrSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALM 159
Cdd:cd03265 72 ----RRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIA-ASANRIIEIKDGEII 221
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAeQLCDRVAIIDHGRII 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-221 |
9.65e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 124.94 E-value: 9.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKE-TIELTNDQLSDLRsQKFGFIFQ-RYNLLSSL 100
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHiTPETGNKNLKKLR-KKVSLVFQfPEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSG 179
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1040783748 180 ENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLI 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
1.01e-31 |
|
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: 122.54 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqLSDLR 83
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD--------ITGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQKF-----GFIFQRYNLLSSLTAAENVALpAIYAGMPQN--QRLERAKQLLEKlgLGDKWQNKPNQLSGGQQQRVSIAR 156
Cdd:cd03224 69 PHERaragiGYVPEGRRIFPELTVEENLLL-GAYARRRAKrkARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-223 |
1.02e-31 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 122.48 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltNDQLSDL 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:cd03266 77 R-RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGEIISD 223
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
1.53e-31 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 122.00 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetieltndQLSDLR 83
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK--------PLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-221 |
1.66e-31 |
|
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: 122.34 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 11 RYFGEGENrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqLSDLRSQkFGFI 90
Cdd:cd03251 9 RYPGDGPP---VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ-IGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 91 FQRYNLLSSlTAAENVALPAIYAGMPQNQRLERAKQLLE-----KLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEII 165
Cdd:cd03251 82 SQDVFLFND-TVAENIAYGRPGATREEVEEAARAANAHEfimelPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 166 LADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
2.36e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.18 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 6 IKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLRSq 85
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKENLKEIRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 86 KFGFIFQRY-NLLSSLTAAENVALpaiyaGMpQNQRLERAK------QLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:PRK13632 84 KIGIIFQNPdNQFIGATVEDDIAF-----GL-ENKKVPPKKmkdiidDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-222 |
8.59e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 8.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNryFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCL---DTATGGSYKIDGketIELTNDQ 78
Cdd:PRK13640 4 NIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG---ITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 79 LSDLRsQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARA 157
Cdd:PRK13640 79 VWDIR-EKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 158 LMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAASANRIIEIKDGEIIS 222
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLLA 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-222 |
1.41e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 121.38 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLN-RYFGEGENrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQL 79
Cdd:PRK13650 2 SNIIEVKNLTfKYKEDQEK--YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRsQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:PRK13650 77 WDIR-HKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAASANRIIEIKDGEIIS 222
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-206 |
1.70e-30 |
|
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: 118.29 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 17 ENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELTNDQLSDLRsQKFGFIFQRY-N 95
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEP-LDYSRKGLLERR-QRVGLVFQDPdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 96 LLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALD 175
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 1040783748 176 SHSGENVMEILRQLHEEGHTIIMVTHDKHIA 206
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-220 |
2.28e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 122.83 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetieLTNDQLS 80
Cdd:PRK11000 1 MASVTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK----RMNDVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSqkFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMN 160
Cdd:PRK11000 73 AERG--VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 161 GGEIILADEPTGALDSHSGENV-MEILRqLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMrIEISR-LHKRlGRTMIYVTHDQVEAMTlADKIVVLDAGRV 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-221 |
2.67e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 123.02 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFgEGEnrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQlsdl 82
Cdd:PRK11607 19 LLEIRNLTKSF-DGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 rsQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:PRK11607 91 --RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 163 EIILADEPTGALDSHSGENV-MEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFV 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-201 |
5.36e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.86 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCL-----DTATGGSYKIDGKETIELt 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 ndQLSDLRsQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQR--LERAKQLLEKLGLGDKWQNKPN----QLSGGQQ 149
Cdd:PRK14247 76 --DVIELR-RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLWDEVKDRLDapagKLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 150 QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTH 201
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-223 |
7.12e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 118.68 E-value: 7.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLdTATGGSYKIDGKETIELTNDQLSDLR---SQK----FGFifqr 93
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARRRavlPQHsslaFPF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 94 ynllsslTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL------MNGGE-IIL 166
Cdd:COG4559 91 -------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPrWLF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 167 ADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:COG4559 164 LDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQ 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-221 |
9.05e-30 |
|
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: 116.93 E-value: 9.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtielTNDQLSDLR 83
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS----YQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sqKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQnqrlERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03268 73 --RIGALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGEII 221
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSeIQKVADRIGIINKGKLI 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-223 |
1.03e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 118.66 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFgEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLSDL 82
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:PRK13642 80 R-RKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKHIAASANRIIEIKDGEIISD 223
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-239 |
1.06e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.06 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLDtATGGSYKIDGKEtieltndqLSD 81
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIlGILA-PDSGEVLWDGEP--------LDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRSQKFGfifqrY-----NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIAR 156
Cdd:COG4152 68 EDRRRIG-----YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQKHQVKSAVKN 235
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
....
gi 1040783748 236 PSVF 239
Cdd:COG4152 223 NTLR 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-223 |
1.09e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 117.38 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 27 SLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQ--LSDLrsqkfgfiFQRYNLLSSLTAAE 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpVSML--------FQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 105 NVAL---PAIYAGMPQNQRLErakQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:PRK10771 91 NIGLglnPGLKLNAAQREKLH---AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1040783748 182 VMEILRQL-HEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:PRK10771 168 MLTLVSQVcQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWD 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-221 |
1.25e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 118.02 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGE-----GENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELT 75
Cdd:COG4167 2 SALLEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK-LEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 NDQLsdlRSQKFGFIFQRYNllSSLTAAENVA----LPAIYA-GMPQNQRLERAKQLLEKLGL-GDKWQNKPNQLSGGQQ 149
Cdd:COG4167 81 DYKY---RCKHIRMIFQDPN--TSLNPRLNIGqileEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 150 QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD----KHIaasANRIIEIKDGEII 221
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHlgivKHI---SDKVLVMHQGEVV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-221 |
1.78e-29 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.87 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYF-------GEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTL-MNIIGCLdtATGGSYKIDGKETIEL 74
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 75 TNDQLSDLRSQkFGFIFQryNLLSSL----TAAENVA--LPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGG 147
Cdd:COG4172 353 SRRALRPLRRR-MQVVFQ--DPFGSLsprmTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 148 QQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDlAVVRALAHRVMVMKDGKVV 505
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
2.75e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 122.63 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLnrYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLsdlR 83
Cdd:PRK11160 339 LTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---R 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQkFGFIFQRYNLLSSlTAAENVALPAIYAGMpqnqrlERAKQLLEKLGLGDKWQNKP----------NQLSGGQQQRVS 153
Cdd:PRK11160 414 QA-ISVVSQRVHLFSA-TLRDNLLLAAPNASD------EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLG 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 154 IARALMNGGEIILADEPTGALDSHSGENVMEILRQlHEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-229 |
3.41e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.46 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEG---ENRVhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQ-- 78
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKA--LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG---VDITDKKvk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 79 LSDLRsQKFGFIFQ--RYNLLSSlTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLG-DKWQNK-PNQLSGGQQQRVSI 154
Cdd:PRK13637 78 LSDIR-KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKsPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 155 ARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQKHQV 229
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSmEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-213 |
4.53e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.25 E-value: 4.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIeltndqlsdlrsqkfGFIFQRYNLLSSL- 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV---------------AYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 -TAAENVALpAIYAGMPQNQRLERAKQL-----LEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGAL 174
Cdd:NF040873 72 lTVRDLVAM-GRWARRGLWRRLTRDDRAavddaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1040783748 175 DSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRII 213
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-224 |
4.61e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.19 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRSQKFGFIFQrynLLSSLTA 102
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ---FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 103 AENVALPAIYA----GMPQNQRLERAKQLLEKLGLG-DKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:PRK13646 100 EDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1040783748 178 SGENVMEILRQLH-EEGHTIIMVTHDKH-IAASANRIIEIKDGEIISDT 224
Cdd:PRK13646 180 SKRQVMRLLKSLQtDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQT 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-220 |
4.93e-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: 113.47 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLN-RYfgeGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDL 82
Cdd:cd03246 1 LEVENVSfRY---PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG---ADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RsQKFGFIFQRYNLLSSlTAAENValpaiyagmpqnqrlerakqlleklglgdkwqnkpnqLSGGQQQRVSIARALMNGG 162
Cdd:cd03246 75 G-DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
7.14e-29 |
|
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: 115.08 E-value: 7.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGcLDTATGGSYKIDGKEtieltndqL 79
Cdd:COG0410 1 MPMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRFDGED--------I 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRSQK-----FGFIFQRYNLLSSLTAAENVALPAIYAGMPQN--QRLERAKQLLEKLGlgDKWQNKPNQLSGGQQQRV 152
Cdd:COG0410 68 TGLPPHRiarlgIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEvrADLERVYELFPRLK--ERRRQRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 153 SIARALMNGGEIILADEPTgaldshSG------ENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPS------LGlaplivEEIFEIIRRLNREGVTILLVEQNARFALEiADRAYVLERGRIV 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-221 |
7.55e-29 |
|
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: 118.28 E-value: 7.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 25 DISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGkETieltndqLSDLRSQKF--------GFIFQRYNL 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EV-------LQDSARGIFlpphrrriGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 97 LSSLTAAENVAlpaiYaGM---PQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGA 173
Cdd:COG4148 89 FPHLSVRGNLL----Y-GRkraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1040783748 174 LDSHSGENVMEILRQLHEEGHT-IIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIpILYVSHSlDEVARLADHVVLLEQGRVV 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-221 |
1.62e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 118.21 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVHV--------------------LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGS 63
Cdd:PRK10070 5 LEIKNLYKIFGEHPQRAFKyieqglskeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 64 YKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQ 143
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 144 LSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLH-EEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-223 |
1.65e-28 |
|
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: 113.97 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketiELTNDQLSDLRSQkFGFIF-QRYNLLS 98
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLRR-IGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAENVAL-PAIYaGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:cd03267 109 DLPVIDSFYLlAAIY-DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1040783748 178 SGENVMEILRQLHEE-GHTIIMVTHDKH-IAASANRIIEIKDGEIISD 223
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMKdIEALARRVLVIDKGRLLYD 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-221 |
2.13e-28 |
|
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: 113.86 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 10 NRYFGEGENRVhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLRSQkFGF 89
Cdd:cd03253 5 NVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---QDIREVTLDSLRRA-IGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 90 IFQRYNLLSSlTAAENVALPAIYAGMPQNQRLERAKQLLEK-LGLGDKWQNKPNQ----LSGGQQQRVSIARALMNGGEI 164
Cdd:cd03253 80 VPQDTVLFND-TIGYNIRYGRPDATDEEVIEAAKAAQIHDKiMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 165 ILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-222 |
3.51e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 3.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIeltndqlsdlrsqkfGFIFQRYNLLSSLT 101
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRI---------------GYLPQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENV------------ALPAIYAGMPQN-----------QRLE---------RAKQLLEKLGLGDKWQNKP-NQLSGGQ 148
Cdd:COG0488 78 VLDTVldgdaelraleaELEELEAKLAEPdedlerlaelqEEFEalggweaeaRAEEILSGLGFPEEDLDRPvSELSGGW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 149 QQRVSIARALMNGGEIILADEPTGALDSHSgenvMEILRQ-LHEEGHTIIMVTHDKH-IAASANRIIEIKDGEIIS 222
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEfLKNYPGTVLVVSHDRYfLDRVATRILELDRGKLTL 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-201 |
3.65e-28 |
|
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: 112.75 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 11 RYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLD---TATGGSYKIDGKEtieLTNDQLSDlrsqKF 87
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQP---RKPDQFQK----CV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 88 GFIFQRYNLLSSLTAAENVALPAIYAG---MPQNQRLERAKQLLEK-LGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTH 201
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
4.20e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 113.25 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQL---- 79
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELakrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRsqkfgfifQRYNLLSSLTAAENVALpaiyaG-MPQNQ-RL--------ERAkqlLEKLGLGDkWQNKP-NQLSGGQ 148
Cdd:COG4604 78 AILR--------QENHINSRLTVRELVAF-----GrFPYSKgRLtaedreiiDEA---IAYLDLED-LADRYlDELSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 149 QQRVSIARALMNGGEIILADEPTGALD-SHSGEnVMEILRQL-HEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQ-MMKLLRRLaDELGKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-207 |
4.51e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 113.40 E-value: 4.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCL-----DTATGGSYKIDGKETIELT 75
Cdd:PRK14267 2 KFAIETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 NDQLSDLRsqKFGFIFQRYNLLSSLTAAENVALPAIYAGM--PQNQRLERAKQLLEKLGLGDKWQNK----PNQLSGGQQ 149
Cdd:PRK14267 78 VDPIEVRR--EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 150 QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTHDKHIAA 207
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAA 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-201 |
6.33e-28 |
|
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: 111.10 E-value: 6.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATG--GSYKIDGKetieltNDQLSDLRSQkFGFIFQRYNLLSS 99
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGR------PLDKRSFRKI-IGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAENVALPAiyagmpqnqrlerakqlleklglgdkwqnKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSG 179
Cdd:cd03213 97 LTVRETLMFAA-----------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|..
gi 1040783748 180 ENVMEILRQLHEEGHTIIMVTH 201
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIH 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-243 |
1.63e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIEltndqlSD 81
Cdd:PRK11432 5 NFVVLKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKL---GLGDKWQNkpnQLSGGQQQRVSIARAL 158
Cdd:PRK11432 75 IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVdlaGFEDRYVD---QISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIA-ASANRIIEIKDGEIIsdtQKHQVKSAVKNP 236
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAfAVSDTVIVMNKGKIM---QIGSPQELYRQP 228
|
....*...
gi 1040783748 237 -SVFKGRF 243
Cdd:PRK11432 229 aSRFMASF 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-222 |
1.80e-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: 110.78 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqLSDLR 83
Cdd:cd03254 3 IEFENVNFSYDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SqKFGFIFQRYNLLSSlTAAENVALPAIYAGMPQNQRLERAKQ---LLEKL--GLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:cd03254 77 S-MIGVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGahdFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEIIS 222
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-223 |
2.19e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 21 HVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLdTATGGSYKIDGKETIELTNDQLSDLRsqkfGFIFQRYNLLSS 99
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRR----AVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAENVALpaiyAGMPQNQRLERAKQL----LEKLGLGDKWQNKPNQLSGGQQQRVSIARALM------NGGEIILADE 169
Cdd:PRK13548 91 FTVEEVVAM----GRAPHGLSRAEDDALvaaaLAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 170 PTGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVAD 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
6.48e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNryFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIdgkETIELTNDQLSD 81
Cdd:PRK13648 6 SIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRsQKFGFIFQR-YNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMN 160
Cdd:PRK13648 81 LR-KHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-223 |
7.44e-27 |
|
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: 109.50 E-value: 7.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 11 RYFGEGEnrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLRSQkFGFI 90
Cdd:cd03252 9 RYKPDGP---VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRQ-VGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 91 FQRyNLLSSLTAAENVALPAiyAGMPQNQ-----RLERAKQLLEKL--GLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03252 82 LQE-NVLFNRSIRDNIALAD--PGMSMERvieaaKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEIISD 223
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-201 |
8.60e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 115.53 E-value: 8.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 18 NRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTA---TGGSYKIDGKEtieLTNDQLSdLRSqkfGFIFQRY 94
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMP---IDAKEMR-AIS---AYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 95 NLLSSLTAAENVALPA---IYAGMPQNQRLERAKQLLEKLGLGDKWQNK---PNQ---LSGGQQQRVSIARALMNGGEII 165
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAhlrMPRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 1040783748 166 LADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTH 201
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-221 |
1.26e-26 |
|
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: 108.78 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELtndQLSDLRSQkFGFIFQRYNLLSS 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRSQ-IGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 lTAAENVALPAIYAGMPQNQRLERAKQLLEKL-GLGDKWQ----NKPNQLSGGQQQRVSIARALMNGGEIILADEPTGAL 174
Cdd:cd03249 92 -TIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1040783748 175 DSHSGENVMEILRQLHeEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:cd03249 171 DAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-206 |
1.33e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.82 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 8 QLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRsQKF 87
Cdd:PRK11308 16 PVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 88 GFIFQryNLLSSLTAAENV----ALP-AIYAGMPQNQRLERAKQLLEKLGL-GDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:PRK11308 95 QIVFQ--NPYGSLNPRKKVgqilEEPlLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEEGHT-IIMVTHD----KHIA 206
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsYVFISHDlsvvEHIA 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-221 |
2.70e-26 |
|
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: 105.86 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNryFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLDtATGGSYKIDGKETIELtndqlSDL 82
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLK-PQQGEITLDGVPVSDL-----EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQKFGFIFQRYNLLSSltaaenvalpaiyagmpqnqrlerakQLLEKLGLgdkwqnkpnQLSGGQQQRVSIARALMNGG 162
Cdd:cd03247 73 LSSLISVLNQRPYLFDT--------------------------TLRNNLGR---------RFSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQlHEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-223 |
2.70e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.79 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYF-----GEG-----------ENR-VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLdTATGGSY 64
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGlkgalkglfrrEYReVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 65 KIDG----KETIELtndqlsdlrSQKFGFIF-QRYNLLSSLTAAENVAL-PAIYaGMPQNQRLERAKQLLEKLGLGDKWq 138
Cdd:COG4586 80 RVLGyvpfKRRKEF---------ARRIGVVFgQRSQLWWDLPAIDSFRLlKAIY-RIPDAEYKKRLDELVELLDLGELL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 139 NKP-NQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD-KHIAASANRIIEI 215
Cdd:COG4586 149 DTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDmDDIEALCDRVIVI 228
|
....*...
gi 1040783748 216 KDGEIISD 223
Cdd:COG4586 229 DHGRIIYD 236
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-221 |
3.63e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 113.40 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 26 ISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLdtATGGSYKIDGketIELTNDQLSDLRsQKFGFIFQRYNLLSSlTAAE 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKING---IELRELDPESWR-KHLSWVGQNPQLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 105 NVALPAIYAGMPQ-NQRLERAK--QLLEKLGLGDKWQNKPNQ--LSGGQQQRVSIARALMNGGEIILADEPTGALDSHSG 179
Cdd:PRK11174 442 NVLLGNPDASDEQlQQALENAWvsEFLPLLPQGLDTPIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1040783748 180 ENVMEILRQLHeEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:PRK11174 522 QLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
3.66e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.78 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKeTIELTNDQLSD 81
Cdd:PRK13636 4 YILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRsQKFGFIFQRY-NLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLgDKWQNKPNQ-LSGGQQQRVSIARALM 159
Cdd:PRK13636 80 LR-ESVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAA-SANRIIEIKDGEII 221
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRVI 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-218 |
3.75e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 112.70 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqlsdlrsQKFG----------- 88
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--------------MRFAsttaalaagva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 89 FIFQRYNLLSSLTAAENV---ALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEII 165
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 166 LADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDG 218
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRmEEIFALCDAITVFKDG 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-202 |
3.96e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 109.81 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKS-TLMNIIGCL--DTATGGSYKIDGKETIELTND 77
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLaaNGRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 78 QLSDLRSQKFGFIFQryNLLSSLTAAENVA-----LPAIYAGMPQNQRLERAKQLLE--KLGLGDKWQNK-PNQLSGGQQ 149
Cdd:PRK09473 90 ELNKLRAEQISMIFQ--DPMTSLNPYMRVGeqlmeVLMLHKGMSKAEAFEESVRMLDavKMPEARKRMKMyPHEFSGGMR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 150 QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHT-IIMVTHD 202
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHD 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-220 |
4.39e-26 |
|
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: 110.20 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 25 DISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDG------KETIELTNDQlsdlrsQKFGFIFQRYNLLS 98
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsRKGIFLPPEK------RRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAENValpaIYaGMPQ---NQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALD 175
Cdd:TIGR02142 89 HLSVRGNL----RY-GMKRarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1040783748 176 SHSGENVMEILRQLHEE-GHTIIMVTHD-KHIAASANRIIEIKDGEI 220
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEfGIPILYVSHSlQEVLRLADRVVVLEDGRV 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-236 |
9.22e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 108.68 E-value: 9.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKS-TLMNIIGCLD---TATGGSYKIDGKETIELTN 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 77 DQLSDLRSQKFGFIFQryNLLSSLTAAENVALPAIYA-----GMPQNQRLERAKQLLEKLGLGD---KWQNKPNQLSGGQ 148
Cdd:PRK11022 81 KERRNLVGAEVAMIFQ--DPMTSLNPCYTVGFQIMEAikvhqGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 149 QQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHE-EGHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQK 226
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDlALVAEAAHKIIVMYAGQVVETGKA 238
|
250
....*....|
gi 1040783748 227 HQVKSAVKNP 236
Cdd:PRK11022 239 HDIFRAPRHP 248
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-229 |
1.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.01 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEG-ENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLDTATG----GSYKIDGKETIELTN 76
Cdd:PRK13631 21 ILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThFNGLIKSKYGtiqvGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 77 DQLSDLRSQKF-------GFIFQ--RYNLLSSlTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKW-QNKPNQLSG 146
Cdd:PRK13631 101 TNPYSKKIKNFkelrrrvSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYlERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 147 GQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQ 225
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKILKTGT 259
|
....
gi 1040783748 226 KHQV 229
Cdd:PRK13631 260 PYEI 263
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-221 |
1.22e-25 |
|
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: 111.73 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 11 RYFGEGenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqLSDLRSQkFGFI 90
Cdd:TIGR02203 339 RYPGRD---RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQ-VALV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 91 FQRYNLLSSlTAAENVAlpaiYAGMPQ--NQRLERA------KQLLEKLGLGDKWQNKPN--QLSGGQQQRVSIARALMN 160
Cdd:TIGR02203 412 SQDVVLFND-TIANNIA----YGRTEQadRAEIERAlaaayaQDFVDKLPLGLDTPIGENgvLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-221 |
1.26e-25 |
|
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: 105.27 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLN-RYFGEGENrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDL 82
Cdd:cd03244 3 IEFKNVSlRYRPNLPP---VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG---VDISKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQkFGFIFQRYNLLSSlTAAENVAlpaiyagmPQNQ----RLERAkqlLEKLGLGDKWQNKP-----------NQLSGG 147
Cdd:cd03244 77 RSR-ISIIPQDPVLFSG-TIRSNLD--------PFGEysdeELWQA---LERVGLKEFVESLPggldtvveeggENLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 148 QQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQlHEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-201 |
2.16e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKE-TIELTNDQLSDLRsQKFGFIFQ-RYNLLSSL 100
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDIKQIR-KKVGLVFQfPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSG 179
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180
....*....|....*....|..
gi 1040783748 180 ENVMEILRQLHEEGHTIIMVTH 201
Cdd:PRK13649 182 KELMTLFKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-233 |
6.02e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.07 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndQLSDLRsQKFGFIFQR-YNLLSSLT 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIR-KLVGIVFQNpETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 182 VMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKHQVKSAV 233
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-220 |
7.63e-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: 101.74 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLSDLRSQKFGFI---FQRYNLLS 98
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP---VTRRSPRDAIRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAENVALPAiyagmpqnqrlerakqlleklglgdkwqnkpnQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHS 178
Cdd:cd03215 92 DLSVAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1040783748 179 GENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGEI 220
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-206 |
1.00e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 105.56 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 5 EIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGcLDTATGGSYKIDGKETIELTNDQLSDLR 83
Cdd:PRK15079 19 DIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGEVAWLGKDLLGMKDDEWRAVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQkFGFIFQryNLLSSL----TAAENVALP--AIYAGMPQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGGQQQRVSIAR 156
Cdd:PRK15079 98 SD-IQMIFQ--DPLASLnprmTIGEIIAEPlrTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD----KHIA 206
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDlavvKHIS 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
1.37e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 105.70 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFgegENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELtndqls 80
Cdd:PRK11650 1 MAGLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQKFGFIFQRYNLLSSLTAAENVAlpaiY----AGMPQ---NQRLERAKQLLEklgLGDKWQNKPNQLSGGQQQRVS 153
Cdd:PRK11650 72 EPADRDIAMVFQNYALYPHMSVRENMA----YglkiRGMPKaeiEERVAEAARILE---LEPLLDRKPRELSGGQRQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 154 IARALMNGGEIILADEPTGALDS----HsgenvMEI-LRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAklrvQ-----MRLeIQRLHRRlKTTSLYVTHDQVEAMTlADRVVVMNGGVA 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-235 |
2.34e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKeTIELTND--QLSDLRSQK-FGFIFQRYNLLS 98
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK-VLYFGKDifQIDAIKLRKeVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAENVALPAIYAGMPQNQRLER-AKQLLEKLGLG----DKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGA 173
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 174 LDSHSGENVMEILRQLHEEgHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQKHQVKSAVKN 235
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-222 |
2.39e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.66 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIdGKETIELTNDQ--LSDLRsQKFGFIFQ-RYNLLSS 99
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkeIKPVR-KKVGVVFQfPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDK-WQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHS 178
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1040783748 179 GENVMEILRQLHEEGHTIIMVTH-DKHIAASANRIIEIKDGEIIS 222
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIIS 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-219 |
3.35e-24 |
|
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: 100.62 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLdTATGGSYKIDGKetieltndqlsdlrsqkFGFIFQRYNLLSSl 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS-----------------IAYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENvalpaIYAGMPQN-QRLE---RAKQL---LEKLGLGDKWQ--NKPNQLSGGQQQRVSIARALMNGGEIILADEPT 171
Cdd:cd03250 81 TIREN-----ILFGKPFDeERYEkviKACALepdLEILPDGDLTEigEKGINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1040783748 172 GALDSHSGENVME-ILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGE 219
Cdd:cd03250 156 SAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-221 |
3.73e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIdGKETieltndqlsdl 82
Cdd:COG0488 315 VLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 rsqKFGFIFQRYNLL-SSLTAAENVAlpaiyAGMPQNQRLErAKQLLEKLGL-GDKWQNKPNQLSGGQQQRVSIARALMN 160
Cdd:COG0488 379 ---KIGYFDQHQEELdPDKTVLDELR-----DGAPGGTEQE-VRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 161 GGEIILADEPTGALDshsgenvMEILRQLHE-----EGhTIIMVTHDKH-IAASANRIIEIKDGEII 221
Cdd:COG0488 450 PPNVLLLDEPTNHLD-------IETLEALEEalddfPG-TVLLVSHDRYfLDRVATRILEFEDGGVR 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-220 |
5.76e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 105.90 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQlsdlrSQKFG--FIFQRYNLL 97
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-----AHQLGiyLVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVALpaiyaGMPQNQR-LERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDS 176
Cdd:PRK15439 99 PNLSVKENILF-----GLPKRQAsMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1040783748 177 HSGENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGEI 220
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPeIRQLADRISVMRDGTI 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-239 |
8.26e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 8.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLnrYFGEGENRVhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdl 82
Cdd:PRK11231 2 TLRTENL--TVGYGTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 rsQKFGFIFQRYNLLSSLTAAENVAlpaiYAGMP-----------QNQRLERAKQLLEKLGLGDKwqnKPNQLSGGQQQR 151
Cdd:PRK11231 76 --RRLALLPQHHLTPEGITVRELVA----YGRSPwlslwgrlsaeDNARVNQAMEQTRINHLADR---RLTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 152 VSIARALMNGGEIILADEPTGALD-SHSGEnVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQV 229
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDiNHQVE-LMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEV 225
|
250
....*....|
gi 1040783748 230 KSAVKNPSVF 239
Cdd:PRK11231 226 MTPGLLRTVF 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-218 |
8.32e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.64 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLr 83
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sqKFGFIFQRYNLLSSLTAAENV---ALPA-IYAGMP---QNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIAR 156
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLyigRHLTkKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDG 218
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-213 |
1.85e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdlrsQKFGFIFQRYNLLSSlT 101
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR----QQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALP-AIYAGMPQNQRLERAkqlLEKLGLGDKWQNKP-NQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSG 179
Cdd:PRK10247 97 VYDNLIFPwQIRNQQPDPAIFLDD---LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1040783748 180 ENVMEILRQL-HEEGHTIIMVTHDKHIAASANRII 213
Cdd:PRK10247 174 HNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-238 |
3.65e-23 |
|
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: 98.38 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 18 NRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQlsdlRSQK-FGFIFQRYNL 96
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARLgIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 97 LSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDS 176
Cdd:cd03218 87 FRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 177 HSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQKHQVksaVKNPSV 238
Cdd:cd03218 167 IAVQDIQKIIKILKDRGIGVLITDHNvRETLSITDRAYIIYEGKVLAEGTPEEI---AANELV 226
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-248 |
3.82e-23 |
|
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: 98.38 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 28 LSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqlSDLRSQKFGFIFQRYNLLSSLTAAENVA 107
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---------PGKGWRHIGYVPQRHEFAWDFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 108 LPAIYAGM------PQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:TIGR03771 72 VMSGRTGHigwlrrPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 182 VMEILRQLHEEGHTIIMVTHDKHIA-ASANRIIeIKDGEIISDTQKHQvksaVKNPSVFKGRFGFSKD 248
Cdd:TIGR03771 152 LTELFIELAGAGTAILMTTHDLAQAmATCDRVV-LLNGRVIADGTPQQ----LQDPAPWMTTFGVSDS 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-207 |
4.12e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.09 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGsYKIDGKETIELTNDQLSDL 82
Cdd:PRK14243 10 VLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTFHGKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RS----QKFGFIFQRYNLLSSlTAAENVALPAIYAGMPQN--QRLERAkqlLEKLGLGDKWQNKPNQ----LSGGQQQRV 152
Cdd:PRK14243 85 DPvevrRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmdELVERS---LRQAALWDEVKDKLKQsglsLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTHDKHIAA 207
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAA 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-223 |
5.20e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.23 E-value: 5.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 9 LNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKET--IELtndqlsdlrsqk 86
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSalLEL------------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 87 fGFIFQrynllSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIIL 166
Cdd:COG1134 96 -GAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 167 ADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISD 223
Cdd:COG1134 170 VDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSmGAVRRLCDRAIWLEKGRLVMD 227
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-229 |
5.67e-23 |
|
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: 98.75 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENrvhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGS--YKIDGKETIELTndQLS 80
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTatYIMRSGAELELY--QLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 D-----LRSQKFGFIFQ--RYNLLSSLTAAENVA--LPAIYAGMPQNQRlERAKQLLEKLGLG-DKWQNKPNQLSGGQQQ 150
Cdd:TIGR02323 77 EaerrrLMRTEWGFVHQnpRDGLRMRVSAGANIGerLMAIGARHYGNIR-ATAQDWLEEVEIDpTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKHIAA-SANRIIEIKDGEIISDTQKHQ 228
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVVESGLTDQ 235
|
.
gi 1040783748 229 V 229
Cdd:TIGR02323 236 V 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-223 |
9.22e-23 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.22 E-value: 9.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 6 IKQLNRYFGEGENR-VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKET--IELTNdqlsdl 82
Cdd:cd03220 20 LKKLGILGRKGEVGeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSslLGLGG------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 rsqkfGFifqrynlLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKwQNKP-NQLSGGQQQRVSIARALMNG 161
Cdd:cd03220 94 -----GF-------NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDF-IDLPvKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISD 223
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-244 |
1.07e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLM---NIIGCL--DTATGGSYKIDGKETIELTND 77
Cdd:PRK14239 5 ILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 78 QLsDLRsQKFGFIFQRYNLLSsLTAAENVALPAIYAGMPQNQRLERAkqlLEKLGLG--------DKWQNKPNQLSGGQQ 149
Cdd:PRK14239 81 TV-DLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEA---VEKSLKGasiwdevkDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 150 QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTHDKHIAAS-ANRIIEIKDGEIIsdtQKHQ 228
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRiSDRTGFFLDGDLI---EYND 230
|
250 260
....*....|....*....|..
gi 1040783748 229 VKSAVKNPS------VFKGRFG 244
Cdd:PRK14239 231 TKQMFMNPKhketedYISGKFG 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-202 |
1.31e-22 |
|
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: 102.05 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTL-MNIIGCLDTaTGGSYKIDGKETIELTNDQLSDLRSqkfgFIFQRYNLLSSl 100
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLlATLAGLLDP-LQGEVTLDGVPVSSLDQDEVRRRVS----VCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENVALpaiyaGMPQ--NQRLERAkqlLEKLGLGDKWQNKPN-----------QLSGGQQQRVSIARALMNGGEIILA 167
Cdd:TIGR02868 424 TVRENLRL-----ARPDatDEELWAA---LERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*
gi 1040783748 168 DEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHD 202
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
361-644 |
1.61e-22 |
|
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: 102.59 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 361 FTSANlygiseqYFDVEGLKLKQGRLLT-EDDVDQSNQVVVLDESAKKAIF-ANENPLGKTVIFNKRPFRVIGVVSDqql 438
Cdd:TIGR03434 114 FVSAN-------FFPVLGVQPALGRLFTpEDDRPGAPPVVVLSYALWQRRFgGDPAVVGRTIRLNGRPYTVVGVMPP--- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 439 gGF--PGNSLNLYSP---YSTVLNKITGGSRIGSITVKISDDVNSTVAEKSLTELLKSLHgkKDFFIMNSDtikQTIE-- 511
Cdd:TIGR03434 184 -GFtfPGRDPDVWVPlamDPALAGSANRGSRWLRVIGRLKPGVTLAQAQAELDAIAARLA--AAYPDTNAG---RGLAvt 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 512 --------NTTGTMKLLISSIAFISLIvGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAG 583
Cdd:TIGR03434 258 plreslvgDVRPPLLVLLGAVGLVLLI-ACANVANLLLARAAARQREIAVRLALGAGRGRLVRQLLTESLLLALAGGALG 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 584 ILLS-----VLIGVLFNSF--ITDFSMDFSTAsIVTAVLfSTLIGVLFGYMPAKKAAELNPITALAQE 644
Cdd:TIGR03434 337 LLLAywglrLLLALLPASLprLLEISLDGRVL-LFALAL-SLLTGLLFGLAPALQATRSDLAEALKEG 402
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
1.83e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGegenRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLS 80
Cdd:PRK11614 3 KVMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQ-NQRLERAKQLLEKLGlgDKWQNKPNQLSGGQQQRVSIARALM 159
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPRLH--ERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-222 |
2.17e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.77 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLDTATG----GSYKID-GKETIEltndQLSDLRsQKFGFIFQ--RY 94
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGqtivGDYAIPaNLKKIK----EVKRLR-KEIGLVFQfpEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 95 NLLSSlTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKW-QNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGA 173
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYvKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 174 LDSHSGENVMEILRQLHEE-GHTIIMVTHD-KHIAASANRIIEIKDGEIIS 222
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNmDQVLRIADEVIVMHEGKVIS 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-221 |
2.26e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.92 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGS--YKIDGKETIELTNDQLS 80
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLR---SQKFGFIFQ--RYNLLSSLTAAENVALPAIYAGMPQNQRL-ERAKQLLEKLGLG-DKWQNKPNQLSGGQQQRVS 153
Cdd:PRK11701 82 ERRrllRTEWGFVHQhpRDGLRMQVSAGGNIGERLMAVGARHYGDIrATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 154 IARALMNGGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVV 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-224 |
3.93e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 96.68 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQL-NRYFGEGENRVH----VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELT 75
Cdd:PRK10419 1 MTLLNVSGLsHHYAHGGLSGKHqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 NDQLSDLRsQKFGFIFQryNLLSSLTAAENVAlpAIYA-------GMPQNQRLERAKQLLEKLGLGDKWQNK-PNQLSGG 147
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQ--DSISAVNPRKTVR--EIIReplrhllSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 148 QQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHT-IIMVTHD-KHIAASANRIIEIKDGEIISDT 224
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDlRLVERFCQRVMVMDNGQIVETQ 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
6.40e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 99.88 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDT------------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 59 -------ATGGSYKIDGKETIELTNDQLSDLRsQKFGFIFQR-YNLLSSLTAAENV--ALPAIyaGMPQNQRLERAKQLL 128
Cdd:TIGR03269 77 kvgepcpVCGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRtFALYGDDTVLDNVleALEEI--GYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 129 EKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTH-DKHIA 206
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHwPEVIE 233
|
250
....*....|....*
gi 1040783748 207 ASANRIIEIKDGEII 221
Cdd:TIGR03269 234 DLSDKAIWLENGEIK 248
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-219 |
9.02e-22 |
|
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: 91.74 E-value: 9.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIeltndqlsdlr 83
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sqkfgfifqrynllssltaaenvalpAIYAgmpqnqrlerakqlleklglgdkwqnkpnQLSGGQQQRVSIARALMNGGE 163
Cdd:cd03221 66 --------------------------GYFE-----------------------------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 164 IILADEPTGALDShsgENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGE 219
Cdd:cd03221 91 LLLLDEPTNHLDL---ESIEALEEALKEYPGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-236 |
9.14e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKS----TLMNIIgcldTATGGSYKIDG-------KE 70
Cdd:PRK10261 11 DVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL----EQAGGLVQCDKmllrrrsRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 71 TIEL---TNDQLSDLRSQKFGFIFQR--YNLLSSLTAAENVALPA-IYAGMPQNQRLERAKQLLEKLGLGDK---WQNKP 141
Cdd:PRK10261 87 VIELseqSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 142 NQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGE 219
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEiADRVLVMYQGE 246
|
250
....*....|....*..
gi 1040783748 220 IISDTQKHQVKSAVKNP 236
Cdd:PRK10261 247 AVETGSVEQIFHAPQHP 263
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-218 |
2.11e-21 |
|
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: 93.16 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 6 IKQLNRYFGEGENrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLM-NIIGCLDTATGGSYKIDGKETIELTNDQLSDLRS 84
Cdd:cd03290 1 VQVTNGYFSWGSG-LATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 QkFGFIFQRYNLLSSlTAAENVALpaiyaGMPQNQrlERAKQLLEKLGL---------GDKWQ--NKPNQLSGGQQQRVS 153
Cdd:cd03290 80 S-VAYAAQKPWLLNA-TVEENITF-----GSPFNK--QRYKAVTDACSLqpdidllpfGDQTEigERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 154 IARALMNGGEIILADEPTGALDSHSGENVME--ILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDG 218
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-222 |
2.42e-21 |
|
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: 93.36 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 5 EIKQLNRYFGEGenrvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLDTaTGGSYKIDGKEtieltndqLSDLR 83
Cdd:TIGR03410 2 EVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLLPV-KSGSIRLDGED--------ITKLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQK-----FGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERA-------KQLLEKLGlGDkwqnkpnqLSGGQQQR 151
Cdd:TIGR03410 69 PHEraragIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIyelfpvlKEMLGRRG-GD--------LSGGQQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKHIA-ASANRIIEIKDGEIIS 222
Cdd:TIGR03410 140 LAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFArELADRYYVMERGRVVA 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-236 |
2.59e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.85 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKS-TLMNIIGCLDTA----TGGSYKIDGKETIELT 75
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 NDQLSDLRSQKFGFIFQR----YNLLSSLTA--AENVALpaiYAGMpqnqRLERAK----QLLEKLGL---GDKWQNKPN 142
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEpmvsLNPLHTLEKqlYEVLSL---HRGM----RREAARgeilNCLDRVGIrqaAKRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 143 QLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNGRC 235
|
250
....*....|....*.
gi 1040783748 221 ISDTQKHQVKSAVKNP 236
Cdd:PRK15134 236 VEQNRAATLFSAPTHP 251
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-221 |
3.55e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.78 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLR 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPA--LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---HDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SQkFGFIFQRYNLLSSlTAAENVAlpaiYAGMPQNQR--LERAKQLLEKLGLGDKWQNKPNQ--------LSGGQQQRVS 153
Cdd:PRK11176 417 NQ-VALVSQNVHLFND-TIANNIA----YARTEQYSReqIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 154 IARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEgHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-222 |
4.67e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 96.78 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIgcldtaTG----GSY--KI--DGKETieltndQLSDLR-SQKFGF- 89
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SGvyphGSYegEIlfDGEVC------RFKDIRdSEALGIv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 90 -IFQRYNLLSSLTAAENVAL---PAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEII 165
Cdd:NF040905 82 iIHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 166 LADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIIS 222
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIRRVADSITVLRDGRTIE 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-237 |
5.45e-21 |
|
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: 97.13 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 16 GENRVhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLdTATGGSYKIDGKETIELTNDQLSdlrsQKFGFIFQRY 94
Cdd:COG4618 342 GSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELG----RHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 95 NLLSSlTAAENVA-LP-----AIYAGMpqnqRLERAKQLLEKL--G----LGDKwqnkPNQLSGGQQQRVSIARALMNGG 162
Cdd:COG4618 416 ELFDG-TIAENIArFGdadpeKVVAAA----KLAGVHEMILRLpdGydtrIGEG----GARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKHQVKSAVKNPS 237
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPA 561
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-220 |
5.83e-21 |
|
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: 92.15 E-value: 5.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetiELTNDQLSDLRSQkFGFIFQRyNLLSSLT 101
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK---PISQYEHKYLHSK-VSLVGQE-PVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALpaiyaGMPQNQrLERAKQLLEKLGLGDKWQ-----------NKPNQLSGGQQQRVSIARALMNGGEIILADEP 170
Cdd:cd03248 104 LQDNIAY-----GLQSCS-FECVKEAAQKAHAHSFISelasgydtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1040783748 171 TGALDSHSGENVMEILRQLHEEgHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-229 |
6.68e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.72 E-value: 6.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGkETIEltndQLSDL 82
Cdd:PRK13537 7 PIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVP----SRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQV 229
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAL 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-244 |
7.32e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 26 ISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdlrsqKFGFI--FQRYNLLSSLTAA 103
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-----RMGVVrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 104 ENVaLPA--------IYAGM--------PQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILA 167
Cdd:PRK11300 99 ENL-LVAqhqqlktgLFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 168 DEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQKHQVKSavkNPSVFKGRFG 244
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDmKLVMGISDRIYVVNQGTPLANGTPEEIRN---NPDVIKAYLG 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-202 |
8.49e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.52 E-value: 8.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLnrYFGEGeNRVhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLS 80
Cdd:PRK11831 5 ANLVDMRGV--SFTRG-NRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRsQKFGFIFQRYNLLSSLTAAENVALPAI-YAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALM 159
Cdd:PRK11831 81 TVR-KRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHD 202
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHD 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-236 |
9.87e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 9.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 21 HVLKDISLSIEKGDFVAIMGQSGSGKST----LMNIIgcldtATGGSYKIDGKETIELTNDQLSDLRSQkFGFIFQRYNl 96
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPN- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 97 lSSLTAAENVA------LPAIYAGMPQNQRLERAKQLLEKLGLG-DKWQNKPNQLSGGQQQRVSIARALMNGGEIILADE 169
Cdd:PRK15134 373 -SSLNPRLNVLqiieegLRVHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 170 PTGALDSHSGENVMEILRQLHEEgHTI--IMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKSAVKNP 236
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQK-HQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQE 520
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-218 |
1.80e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKI-DGKETIeltndqlsdlrsqkfgFIFQR-YNLLSS 99
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----------------FLPQRpYLPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAenVALPAIYAGMPQnqrlERAKQLLEKLGLG------DKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGA 173
Cdd:COG4178 442 LREA--LLYPATAEAFSD----AELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1040783748 174 LDSHSGENVMEILRQLHEEGhTIIMVTHDKHIAASANRIIEIKDG 218
Cdd:COG4178 516 LDEENEAALYQLLREELPGT-TVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-222 |
1.94e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.00 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIgcldtaTG----GSYK----IDGKEtieL 74
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL------SGvyphGTYEgeiiFEGEE---L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 75 TNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVAL---PAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQR 151
Cdd:PRK13549 72 QASNIRDTERAGIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIIS 222
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDGRHIG 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-193 |
4.11e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.70 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGegeNRvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLs 80
Cdd:COG1137 1 MMTLEAENLVKSYG---KR-TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED---ITHLPM- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQK-FGF------IFQRynllssLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVS 153
Cdd:COG1137 73 HKRARLgIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1040783748 154 IARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEG 193
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG 186
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-207 |
4.37e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLS 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 dlrsQKFGFIFQRYNLLSSLTAAENVALpaiyAGMPQNQRLERA--------KQLLEKLGLgDKWQNKP-NQLSGGQQQR 151
Cdd:PRK09536 77 ----RRVASVPQDTSLSFEFDVRQVVEM----GRTPHRSRFDTWtetdraavERAMERTGV-AQFADRPvTSLSGGERQR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAA 207
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAA 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-221 |
5.28e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.53 E-value: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETielTNDQLSDLRSQKFGFIFQRYNLLSS 99
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV---TFNGPKSSQEAGIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAENVAL----PAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALD 175
Cdd:PRK10762 94 LTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1040783748 176 SHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:PRK10762 174 DTETESLFRVIRELKSQGRGIVYISHRlKEIFEICDDVTVFRDGQFI 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-212 |
8.44e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 91.12 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLD---TATGGSYKIDGKETIELTN 76
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 77 DQLSDLRSQKFGFIFQryNLLSSLTAAENV------ALPAIYAGMP----QNQRLERAKQLLEKLGLGDK---WQNKPNQ 143
Cdd:COG4170 81 RERRKIIGREIAMIFQ--EPSSCLDPSAKIgdqlieAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDHkdiMNSYPHE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 144 LSGGQQQRVSIARALMNGGEIILADEPTGALDShsgENVMEILR------QLHeeGHTIIMVTHD-KHIAASANRI 212
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMES---TTQAQIFRllarlnQLQ--GTSILLISHDlESISQWADTI 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-201 |
8.54e-20 |
|
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: 87.80 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqlsDLRSQKFGFIFQRYNLLSSLT 101
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-----DEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGMPQNQrlerAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|
gi 1040783748 182 VMEILRQLHEEGHTIIMVTH 201
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTH 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-222 |
8.59e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.13 E-value: 8.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLdTATGGSYKIDGKETIELTNDQLSDLRS-----QKFGFIFQRYNLL 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAylsqqQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SsLTAAENVALPAIyagmpqNQRLErakQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMN-------GGEIILADEP 170
Cdd:COG4138 91 A-LHQPAGASSEAV------EQLLA---QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 171 TGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIIS 222
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKLVA 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-232 |
8.95e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.66 E-value: 8.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdlrsQKFGFIFQRYNLLSSLT 101
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVAlPAIYAGMPQNQRLERAKQ-----LLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDS 176
Cdd:PRK10253 98 VQELVA-RGRYPHQPLFTRWRKEDEeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 177 HSGENVMEILRQLH-EEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKSA 232
Cdd:PRK10253 177 SHQIDLLELLSELNrEKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTA 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
10-233 |
1.81e-19 |
|
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: 92.41 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 10 NRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdlrsQKFGF 89
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 90 IFQRYNLLSSlTAAENVAL-------PAIYAGmpqnQRLERAKQLLEKL------GLGDKWQNkpnqLSGGQQQRVSIAR 156
Cdd:TIGR01842 397 LPQDVELFPG-TVAENIARfgenadpEKIIEA----AKLAGVHELILRLpdgydtVIGPGGAT----LSGGQRQRIALAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKHQVKSAV 233
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAKL 544
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-201 |
1.91e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketiELTNDQLSDLRSqKFGFIFQRYNLLSSLT 101
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG----VPVPARARLARA-RIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180
....*....|....*....|
gi 1040783748 182 VMEILRQLHEEGHTIIMVTH 201
Cdd:PRK13536 211 IWERLRSLLARGKTILLTTH 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-220 |
4.46e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 91.19 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 13 FGEGENRVHVlKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLSDLRSQkFGFIFQ 92
Cdd:PRK10522 330 FAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEDYRKL-FSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 93 RYNLLSSLTAAEN-VALPAIYAgmpqnqrlerakQLLEKLGLGDKWQNKPN-----QLSGGQQQRVSIARALMNGGEIIL 166
Cdd:PRK10522 405 DFHLFDQLLGPEGkPANPALVE------------KWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 167 ADEPTGALDSH-SGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:PRK10522 473 LDEWAADQDPHfRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-221 |
6.74e-19 |
|
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: 85.27 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLD-TATGGSYKIDGKETIELTNDQlsd 81
Cdd:cd03217 1 LEIKDLHVSVGGKE----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKyEVTEGEILFKGEDITDLPPEE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 lRSQKFGFI-FQRynllssltaaenvalPAIYAGMpqnqrleRAKQLLEKLGLGdkwqnkpnqLSGGQQQRVSIARALMN 160
Cdd:cd03217 74 -RARLGIFLaFQY---------------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAA--SANRIIEIKDGEII 221
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-224 |
6.83e-19 |
|
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: 90.27 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTAtgGSYkiDGK---ETIELTNDQL 79
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH--GTW--DGEiywSGSPLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 SDLRSQKFGFIFQRYNLLSSLTAAENVAL--PAIYAG--MPQNQRLERAKQLLEKLGLGDKWQNKP-NQLSGGQQQRVSI 154
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLgnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 155 ARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISDT 224
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQHVATK 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-221 |
8.52e-19 |
|
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: 89.86 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLN-RYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLDTATGGSYKIDGKETIELTnDQLS 80
Cdd:TIGR03269 279 IIKVRNVSkRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIaGVLEPTSGEVNVRVGDEWVDMT-KPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLR---SQKFGFIFQRYNL------LSSLTAAENVALPAIYAGMPQNQRL-------ERAKQLLEKLglgdkwqnkPNQL 144
Cdd:TIGR03269 358 DGRgraKRYIGILHQEYDLyphrtvLDNLTEAIGLELPDELARMKAVITLkmvgfdeEKAEEILDKY---------PDEL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 145 SGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVME-ILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIV 507
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-248 |
1.09e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCL-DTATGGSYKID---GKETIELTNDQLSDLRsqKFGFIFQRYNLL 97
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGYRYSGDvllGGRSIFNYRDVLEFRR--RVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SsLTAAENVaLPAIYAG--MPQNQRLERAKQLLEKLGL----GDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPT 171
Cdd:PRK14271 114 P-MSIMDNV-LAGVRAHklVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 172 GALDSHSGENVMEILRQLHEEgHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKSAVKNPSVFKGRFGFSKD 248
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGD 268
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-221 |
1.11e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.89 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 5 EIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLD--TATGGSYKIDGKETIELTNDQlsdl 82
Cdd:COG0396 2 EIKNLHVSVEGKE----ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQK-FGFIFQR---------YNLLSslTAAENVALPAIYAGmpqnQRLERAKQLLEKLGLGDKWQNKP-NQ-LSGGQQQ 150
Cdd:COG0396 74 RARAgIFLAFQYpveipgvsvSNFLR--TALNARRGEELSAR----EFLKLLKEKMKELGLDEDFLDRYvNEgFSGGEKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD----KHIAasANRIIEIKDGEII 221
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqrilDYIK--PDFVHVLVDGRIV 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-217 |
1.98e-18 |
|
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: 82.97 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIeltndqlsdlrsqkFgFIFQR-YnlLSSL 100
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDL--------------L-FLPQRpY--LPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAENVALPaiyagmpqnqrlerakqlleklglgdkWQNKpnqLSGGQQQRVSIARALMNGGEIILADEPTGALDshsGE 180
Cdd:cd03223 79 TLREQLIYP---------------------------WDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSALD---EE 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 1040783748 181 NVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKD 217
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-201 |
3.48e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIeltndqLSDLRSQkFGFIFQRYNLLSSLT 101
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID------DPDVAEA-CHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGmpqnQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:PRK13539 90 VAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 1040783748 182 VMEILRQLHEEGHTIIMVTH 201
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-213 |
4.43e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.93 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 25 DISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieltndqLSDLRSQkfgfiFQRyNLL------- 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--------IRRQRDE-----YHQ-DLLylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 --SSLTAAENVAlpaIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALD 175
Cdd:PRK13538 85 ikTELTALENLR---FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1040783748 176 SHSGENVMEILRQLHEEGHTIIMVTH-DKHIAASANRII 213
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGGMVILTTHqDLPVASDKVRKL 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-220 |
6.15e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.86 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdlrsQKFGFIFQRyNLLSS 99
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH----RQVALVGQE-PVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAENVALPAIYAGMPQNQ---RLERAKQLLEKL--GLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGAL 174
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEEIMaaaKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1040783748 175 DSHSGENVMEILRQlheEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:TIGR00958 649 DAECEQLLQESRSR---ASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-224 |
7.49e-18 |
|
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: 87.16 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 11 RYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetiELTNDQLSDLRsQKFGFI 90
Cdd:COG4615 336 RYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAYR-QLFSAV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 91 FQRYNLLSSLTAAENVALPaiyagmpqnqrlERAKQLLEKLGLGDKWQNKPN-----QLSGGQQQRVSIARALMNGGEII 165
Cdd:COG4615 412 FSDFHLFDRLLGLDGEADP------------ARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPIL 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 166 LADE------P-------TgaldshsgenvmEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDT 224
Cdd:COG4615 480 VFDEwaadqdPefrrvfyT------------ELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELT 539
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-221 |
8.70e-18 |
|
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: 86.91 E-value: 8.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 21 HVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGG------SYKI---------DGKETI-ELTNDQLSDLRS 84
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpGIKVgylpqepqlDPTKTVrENVEEGVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 qkfgfIFQRYNLLSSLTAAENVALPAIYAGMPQ-------------NQRLERAkqlLEKLGLGDkWQNKPNQLSGGQQQR 151
Cdd:TIGR03719 99 -----ALDRFNEISAKYAEPDADFDKLAAEQAElqeiidaadawdlDSQLEIA---MDALRCPP-WDADVTKLSGGERRR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDShsgENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGEII 221
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPGTVVAVTHDRYfLDNVAGWILELDRGRGI 237
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-222 |
9.79e-18 |
|
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: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLN-RYfgeGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDL 82
Cdd:cd03369 7 IEVENLSvRY---APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG---IDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSqKFGFIFQRYNLLSSlTAAENVAlpaiyagmPQNQRLEraKQLLEKLGLGDKWQNkpnqLSGGQQQRVSIARALMNGG 162
Cdd:cd03369 81 RS-SLTIIPQDPTLFSG-TIRSNLD--------PFDEYSD--EEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHeEGHTIIMVTHDKHIAASANRIIEIKDGEIIS 222
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-221 |
1.26e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.69 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 11 RYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLRSqKFGFI 90
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD---IPLTKLQLDSWRS-RLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 91 FQRYNLLSSlTAAENVALpaiyaGMPQ--NQRLERAKQLL----EKLGLGDKWQNKPNQ----LSGGQQQRVSIARALMN 160
Cdd:PRK10789 395 SQTPFLFSD-TVANNIAL-----GRPDatQQEIEHVARLAsvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-229 |
2.10e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 24 KDISLSIEKGDFVAIMGQSGSGKStlMNIIGCLD------TATGGSYKIDGKETieltndQLSDLRSQKFGFIFQR---- 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPV------APCALRGRKIATIMQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 94 YNLLSSLTAAENVALPAIyAGMPQNQRLERAkqlLEKLGLGDK---WQNKPNQLSGGQQQRVSIARALMNGGEIILADEP 170
Cdd:PRK10418 92 FNPLHTMHTHARETCLAL-GKPADDATLTAA---LEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 171 TGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKHIAA---------SANRIIEIKDGEIISDTQKHQV 229
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVArladdvavmSHGRIVEQGDVETLFNAPKHAV 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
2.91e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.54 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFgegENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLS 80
Cdd:PRK13652 1 MHLIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP---ITKENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRsqKF-GFIFQRYN-LLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL 158
Cdd:PRK13652 75 EVR--KFvGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 159 MNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHDKHIAAS-ANRIIEIKDGEIIS 222
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVA 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-221 |
3.10e-17 |
|
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: 85.26 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 13 FGEGENRVhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndQLSdLRSQkFGFIFQ 92
Cdd:COG5265 365 FGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT--QAS-LRAA-IGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 93 RYNLLSSlTAAENVAlpaiYaGMPQNQRLE-----RAKQLLE-KLGLGDKWQN-------KpnqLSGGQQQRVSIARALM 159
Cdd:COG5265 440 DTVLFND-TIAYNIA----Y-GRPDASEEEveaaaRAAQIHDfIESLPDGYDTrvgerglK---LSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 160 NGGEIILADEPTGALDSHSGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| FtsX |
pfam02687 |
FtsX-like permease family; This is a family of predicted permeases and hypothetical ... |
522-637 |
3.19e-17 |
|
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: 78.06 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 522 SSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFN----SF 597
Cdd:pfam02687 1 ILFSLLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVIGLLLGLLLAKLIAillySS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1040783748 598 ITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNP 637
Cdd:pfam02687 81 GISLPILVPPLSILIALLLALLIALLASLLPALRIRKINP 120
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
22-229 |
3.57e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.48 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDgKETIELTndQLSDLRSQKFGFIFQRYNLLSSLT 101
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID-DEDISLL--PLHARARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENV-ALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGE 180
Cdd:PRK10895 95 VYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 181 NVMEILRQLHEEGHTIIMVTHD----------KHIAASANRIIEIKDGEIISDTQKHQV 229
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHNvretlavcerAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
504-644 |
3.57e-17 |
|
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: 85.62 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 504 DTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAG 583
Cdd:COG3127 690 DAILDQVRDILDQVSLAVEFLAGFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLA 769
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 584 ILLSVLIGVLFNSFITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALAQE 644
Cdd:COG3127 770 ALLAELAGWALARFVFDLPFSPPWWLWLAGLLGGALLVLLAGLLGARRVLRQPPLEVLREE 830
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-236 |
3.88e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.93 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIgCLDT-----ATGGSYKIDGKETIELT 75
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAI-CGVTkdnwrVTADRMRFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 NDQLSDLRSQKFGFIFQRYNllSSLTAAENV------ALPA-IYAG---MPQNQRLERAKQLLEKLGLGDK---WQNKPN 142
Cdd:PRK15093 80 PRERRKLVGHNVSMIFQEPQ--SCLDPSERVgrqlmqNIPGwTYKGrwwQRFGWRKRRAIELLHRVGIKDHkdaMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 143 QLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKHIAAS-ANRIIEIKDGEI 220
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHDLQMLSQwADKINVLYCGQT 237
|
250
....*....|....*.
gi 1040783748 221 ISDTQKHQVKSAVKNP 236
Cdd:PRK15093 238 VETAPSKELVTTPHHP 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-201 |
4.11e-17 |
|
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: 85.84 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 26 ISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELTNDQLSdlrsQKFGFIFQRYNLLSSLTAAEN 105
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD-IETNLDAVR----QSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 106 VALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEI 185
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170
....*....|....*.
gi 1040783748 186 LRQlHEEGHTIIMVTH 201
Cdd:TIGR01257 1104 LLK-YRSGRTIIMSTH 1118
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-221 |
6.13e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 15 EGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltndqlsDLRS------QKFG 88
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV---------RIRSprdairAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 89 FI---FQRYNLLSSLTAAENVALPAIYA---GMPQNQRLER--AKQLLEKLGLgdKWQNkPNQ----LSGGQQQRVSIAR 156
Cdd:COG1129 331 YVpedRKGEGLVLDLSIRENITLASLDRlsrGGLLDRRRERalAEEYIKRLRI--KTPS-PEQpvgnLSGGNQQKVVLAK 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:COG1129 408 WLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSElPELLGLSDRILVMREGRIV 473
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-205 |
1.86e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 5 EIKQLNRYFGEGENRV--HVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIgcldtaTGGSYKIDGKETIELTNDQLSdl 82
Cdd:COG2401 26 RVAIVLEAFGVELRVVerYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL------AGALKGTPVAGCVDVPDNQFG-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 rsqkfgfifQRYNLLSSLTAAENVALpaiyagmpqnqrlerAKQLLEKLGLGDK--WQNKPNQLSGGQQQRVSIARALMN 160
Cdd:COG2401 98 ---------REASLIDAIGRKGDFKD---------------AVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1040783748 161 GGEIILADEPTGALDshsGENVMEILRQLHEE----GHTIIMVTHDKHI 205
Cdd:COG2401 154 RPKLLVIDEFCSHLD---RQTAKRVARNLQKLarraGITLVVATHHYDV 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-202 |
5.15e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 9 LNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRsQKFG 88
Cdd:PRK10261 330 LNRVTRE----VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 89 FIFQR--YNLLSSLTAAENVALPAIYAGMPQNQRL-ERAKQLLEKLGLGDK--WQnKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:PRK10261 405 FIFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKAAaARVAWLLERVGLLPEhaWR-YPHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD 202
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHD 523
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-245 |
6.41e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.33 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIG---CLDTATGGS-----YKIDGKETIELTNDQLSDLRS-----QKFG 88
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdlTGGGAPRGArvtgdVTLNGEPLAAIDAPRLARLRAvlpqaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 89 FIFqrynllsslTAAENVAL---P-AIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARAL------ 158
Cdd:PRK13547 96 FAF---------SAREIVLLgryPhARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 159 ---MNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHT-IIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKSav 233
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLT-- 244
|
250
....*....|..
gi 1040783748 234 knPSVFKGRFGF 245
Cdd:PRK13547 245 --PAHIARCYGF 254
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-220 |
1.18e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.32 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKqlNRYFG-EGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLDTATGGSYKIDGkeTIELTnDQLSd 81
Cdd:PLN03130 615 ISIK--NGYFSwDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG--TVAYV-PQVS- 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 lrsqkfgFIFqrynllsSLTAAENvalpaIYAGMPQNQ-RLERA------KQLLEKLGLGDKWQ--NKPNQLSGGQQQRV 152
Cdd:PLN03130 689 -------WIF-------NATVRDN-----ILFGSPFDPeRYERAidvtalQHDLDLLPGGDLTEigERGVNISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVME--ILRQLheEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDEL--RGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-221 |
1.83e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqLSDLRsQKFGFIFQRYNLLSSlTA 102
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 103 AENVAL---PAIYAGMPQNQRLERAKQLLEK--LGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:PRK13657 426 EDNIRVgrpDATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1040783748 178 SGENVMEILRQLhEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:PRK13657 506 TEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-202 |
2.14e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELtndqlsdLRSQKFGFIFQRYNLLSSLTA 102
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-------LQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 103 -AENVALPAIYAGM-----PQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDS 176
Cdd:PRK15056 96 lVEDVVMMGRYGHMgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*.
gi 1040783748 177 HSGENVMEILRQLHEEGHTIIMVTHD 202
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-221 |
2.44e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLN---RYFGEGENRVHV--LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTND 77
Cdd:PRK15112 4 LLEVRNLSktfRYRTGWFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP---LHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 78 QLSdLRSQKFGFIFQryNLLSSLTAAENVA----LPAIY-AGMPQNQRLERAKQLLEKLGL-GDKWQNKPNQLSGGQQQR 151
Cdd:PRK15112 81 DYS-YRSQRIRMIFQ--DPSTSLNPRQRISqildFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD----KHIaasANRIIEIKDGEII 221
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHlgmmKHI---SDQVLVMHQGEVV 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-201 |
2.66e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.84 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltnDQLSDLRSQKFGFIFQRYNLLSSLT 101
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALpaiYAGMPQNQRLERAkqlLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGEN 181
Cdd:cd03231 90 VLENLRF---WHADHSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 1040783748 182 VMEILRQLHEEGHTIIMVTH 201
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-222 |
2.80e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGsykidgkeTIELTNDQLSDLRSQKFG----FIFQRYNLL 97
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEG--------EILLDAQPLESWSSKAFArkvaYLPQQLPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVAL---PAIYA----GMPQNQRLERAKQLLeklGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEP 170
Cdd:PRK10575 98 EGMTVRELVAIgryPWHGAlgrfGAADREKVEEAISLV---GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 171 TGALD-SHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIIS 222
Cdd:PRK10575 175 TSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIA 228
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
506-641 |
2.92e-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: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 506 IKQTIENTTGTMKLlissIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAGIL 585
Cdd:COG3127 245 LGRALDRAEQFLLL----VALLALLLAGVAVANAARRYVARRLDTIALLRCLGASRRQIFRIYLLQLLLLGLLGSLLGLL 320
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 586 LSVLIGVLFNSFITDF-----SMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITAL 641
Cdd:COG3127 321 LGALLQALLAALLADLlpvplEPALSPLPLLLGLLVGLLVLLLFALPPLLRLRRVPPLRVL 381
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-221 |
4.90e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRyfgEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKetiELTNDQLSDL 82
Cdd:COG3845 257 VLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE---DITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQKFGFI---FQRYNLLSSLTAAENVALPAIY------AGMPQNQRL-ERAKQLLEKLGL--GDKWQnKPNQLSGGQQQ 150
Cdd:COG3845 331 RRLGVAYIpedRLGRGLVPDMSVAENLILGRYRrppfsrGGFLDRKAIrAFAEELIEEFDVrtPGPDT-PARSLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEII 221
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDlDEILALSDRIAVMYEGRIV 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-220 |
1.02e-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: 78.06 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLDtatggsyKIDGKETIE-----------LTNDQLSDlrSQKFGFI 90
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMD-------KVEGHVHMKgsvayvpqqawIQNDSLRE--NILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 91 FQRYNLLSSLTAAenvALPAIYAGMPQNQRLErakqlleklgLGDKWQNkpnqLSGGQQQRVSIARALMNGGEIILADEP 170
Cdd:TIGR00957 725 LNEKYYQQVLEAC---ALLPDLEILPSGDRTE----------IGEKGVN----LSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 171 TGALDSHSGENVME--ILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:TIGR00957 788 LSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
1.14e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIeltndqls 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 dlrsqkfGFIFQRYNLLSS--LTAAENVAL-PAIYAG--MPQNQRLErAKQLLEKlglgdkwqnkPNQ-LSGGQQQRVSI 154
Cdd:PRK09544 70 -------GYVPQKLYLDTTlpLTVNRFLRLrPGTKKEdiLPALKRVQ-AGHLIDA----------PMQkLSGGETQRVLL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 155 ARALMNGGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHDKHI 205
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHL 183
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-204 |
1.60e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.92 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFgegeNRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLmniIGCLD--TATGGSYKIDGKetIELTNDQLSD 81
Cdd:PRK14258 8 IKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTF---LKCLNrmNELESEVRVEGR--VEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LR------SQKFGFIFQRYNLLSsLTAAENVALPAIYAGM-PQNQRLERAKQLLEKLGLGDKWQNKPNQ----LSGGQQQ 150
Cdd:PRK14258 79 RRvnlnrlRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKH 204
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLH 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-220 |
1.73e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLmniigcLDTATGgsykidgkeTIELTNDQLSDLRSqkFGFIFQRYNLLSSlT 101
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTL------LQSLLS---------QFEISEGRVWAERS--IAYVPQQAWIMNA-T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENValpaIYAGMPQNQRLE---RAKQL---LEKLG------LGDKWQNkpnqLSGGQQQRVSIARALMNGGEIILADE 169
Cdd:PTZ00243 737 VRGNI----LFFDEEDAARLAdavRVSQLeadLAQLGggleteIGEKGVN----LSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 170 PTGALDSHSGENVME--ILRQLHeeGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:PTZ00243 809 PLSALDAHVGERVVEecFLGALA--GKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-220 |
1.87e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYfgeGENRVhvlKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELTndqlSDL 82
Cdd:PRK09700 265 VFEVRNVTSR---DRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD-ISPR----SPL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 83 RSQKFGFIF----QRYN-LLSSLTAAENVALP-----AIYAGM------PQNQRLERAKQLLEKLGLGDKWQNKpNQLSG 146
Cdd:PRK09700 334 DAVKKGMAYitesRRDNgFFPNFSIAQNMAISrslkdGGYKGAmglfheVDEQRTAENQRELLALKCHSVNQNI-TELSG 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 147 GQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEI 220
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-215 |
5.11e-14 |
|
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: 72.65 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII--GCLD-------TATGGSYKIDGKETIE-LTN-DQLSDLRSQK- 86
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlyPALArrlhlkkEQPGNHDRIEGLEHIDkVIViDQSPIGRTPRs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 87 --------FGFIFQ---------RYN------LLSSLTAAENVALPA-----IYAGMPqnqRLERAKQLLEKLGLG--DK 136
Cdd:cd03271 87 npatytgvFDEIRElfcevckgkRYNretlevRYKGKSIADVLDMTVeealeFFENIP---KIARKLQTLCDVGLGyiKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 137 WQNKPNqLSGGQQQRVSIARALMN---GGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRII 213
Cdd:cd03271 164 GQPATT-LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
..
gi 1040783748 214 EI 215
Cdd:cd03271 243 DL 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-222 |
6.59e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.37 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 37 AIMGQSGSGKSTLMNIIGCLDTATGGSykidgketIELTNDQLSDLRSQ--------KFGFIFQRYNLLSSLTAAENVAl 108
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGR--------IVLNGRVLFDAEKGiclppekrRIGYVFQDARLFPHYKVRGNLR- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 109 paiYaGMpQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQ 188
Cdd:PRK11144 99 ---Y-GM-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1040783748 189 LHEEGHT-IIMVTHD-KHIAASANRIIEIKDGEIIS 222
Cdd:PRK11144 174 LAREINIpILYVSHSlDEILRLADRVVVLEQGKVKA 209
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-201 |
7.51e-14 |
|
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: 70.35 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTA--TGGSYKIDGKE-TIELTndqlsdlRSQkfGFIFQRYNLLSS 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPlDKNFQ-------RST--GYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAENVALPAIYAGmpqnqrlerakqlleklglgdkwqnkpnqLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSG 179
Cdd:cd03232 94 LTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|..
gi 1040783748 180 ENVMEILRQLHEEGHTIIMVTH 201
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTIH 166
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-215 |
1.79e-13 |
|
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: 69.98 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTLmniigCLDT--ATG----------------GSYKIDGKETIE-----LT 75
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSL-----AFDTiyAEGqrryveslsayarqflGQMDKPDVDSIEglspaIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 76 NDQLSDLRSQK--FGFIFQRYNLLSSLtaaenvalpaiYAGMPQNQRLerakQLLEKLGLGDKWQNK-PNQLSGGQQQRV 152
Cdd:cd03270 82 IDQKTTSRNPRstVGTVTEIYDYLRLL-----------FARVGIRERL----GFLVDVGLGYLTLSRsAPTLSGGEAQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 153 SIARALMNG--GEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEI 215
Cdd:cd03270 147 RLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-222 |
3.05e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIG---CLDtatggsykiDGKETIE-------LTNDQLSDLRSQKFGFI-- 90
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---------DGRIIYEqdlivarLQQDPPRNVEGTVYDFVae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 91 --------FQRYNLLSSLTAAEnvalpaiyagmPQNQRLERAKQLLEKLGLGDKWQ--NKPNQ---------------LS 145
Cdd:PRK11147 90 gieeqaeyLKRYHDISHLVETD-----------PSEKNLNELAKLQEQLDHHNLWQleNRINEvlaqlgldpdaalssLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 146 GGQQQRVSIARALMNGGEIILADEPTGALDSHSgenvMEILRQ-LHEEGHTIIMVTHDK-HIAASANRIIEIKDGEIIS 222
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGfLKTFQGSIIFISHDRsFIRNMATRIVDLDRGKLVS 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-243 |
7.70e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNdqlSDLR 83
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSlTAAENVAL------PAIYAGMPQNQRLERAKQLLEklGLGDKWQNKPNQLSGGQQQRVSIARA 157
Cdd:PRK10790 415 -QGVAMVQQDPVVLAD-TFLANVTLgrdiseEQVWQALETVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 158 LMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGhTIIMVTHDKHIAASANRIIEIKDGEIISDTQKHQVKSAvknps 237
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHT-TLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA----- 564
|
....*.
gi 1040783748 238 vfKGRF 243
Cdd:PRK10790 565 --QGRY 568
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-202 |
7.78e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.30 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 21 HVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGG------SYKI----------DGKETIELTNDQLSDLRS 84
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGearpapGIKVgylpqepqldPEKTVRENVEEGVAEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 qkfgfIFQRYNLLSSLTAAENVALPAIYAGMPQNQ-------------RLERAkqlLEKLGLGDkWQNKPNQLSGGQQQR 151
Cdd:PRK11819 101 -----ALDRFNEIYAAYAEPDADFDALAAEQGELQeiidaadawdldsQLEIA---MDALRCPP-WDAKVTKLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDShsgENVMEILRQLHEEGHTIIMVTHD 202
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-220 |
2.57e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLDTATGGSYKIDGK-----ETIELTNDQLSDlrSQKFGFIFQ--RY 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSvayvpQVSWIFNATVRE--NILFGSDFEseRY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 95 NLLSSLTAaenvalpaiyagMPQNQRLERAKQLLEklgLGDKWQNkpnqLSGGQQQRVSIARALMNGGEIILADEPTGAL 174
Cdd:PLN03232 711 WRAIDVTA------------LQHDLDLLPGRDLTE---IGERGVN----ISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1040783748 175 DSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-215 |
4.49e-12 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 65.04 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGcldtatggsykidGKETIELTNDQLSDLRSQKFGFIFQrynlLS 98
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------YASGKARLISFLPKFSRNKLIFIDQ----LQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTaaenvalpaiyagmpqnqrlerakqlleKLGLGDKWQNKP-NQLSGGQQQRVSIARALMNG--GEIILADEPTGALD 175
Cdd:cd03238 70 FLI----------------------------DVGLGYLTLGQKlSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1040783748 176 SHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEI 215
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-222 |
5.49e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.57 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTL-MNIIGCLDTATGgSYKIDGKeTIELTNDQLSDLRsQKFGFIFQRYNLLSSL 100
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQKG-AVLWQGK-PLDYSKRGLLALR-QQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAE-NVALPAIYAGMPQNqrlERAKQLLEKLGLGD--KWQNKPNQ-LSGGQQQRVSIARALMNGGEIILADEPTGALDS 176
Cdd:PRK13638 93 TDIDsDIAFSLRNLGVPEA---EITRRVDEALTLVDaqHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1040783748 177 HSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIIS 222
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDiDLIYEISDAVYVLRQGQILT 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-201 |
6.85e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNiigcldtATGGSYKIDGKETIELTND-QLSDLRSQKFGFIFQRYNLLSSL 100
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLN-------ALAGRIQGNNFTGTILANNrKPTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 101 TAAEN---VALPAIYAGMPQNQRLERAKQLLEKLGLGdKWQNKP------NQLSGGQQQRVSIARALMNGGEIILADEPT 171
Cdd:PLN03211 156 TVRETlvfCSLLRLPKSLTKQEKILVAESVISELGLT-KCENTIignsfiRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|
gi 1040783748 172 GALDSHSGENVMEILRQLHEEGHTIIMVTH 201
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-217 |
1.11e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.35 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 27 SLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRSQkfgfIFQRYN--LLS------ 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD----EWQRNNtdMLSpgeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAEnvalpAIYAGMPQNQRLErakQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHS 178
Cdd:PRK10938 99 GRTTAE-----IIQDEVKDPARCE---QLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1040783748 179 GENVMEILRQLHEEGHTIIMVThdkhiaasaNRIIEIKD 217
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVL---------NRFDEIPD 200
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-201 |
2.41e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 64.20 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 18 NRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII----GCldTATGGSYKIDGKETIELTNDQlsdlRSQKFGFI-FQ 92
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSY--EVTSGTILFKGQDLLELEPDE----RARAGLFLaFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 93 RYNLLSSLTAAE--NVALPAI--YAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQ-----LSGGQQQRVSIARALMNGGE 163
Cdd:TIGR01978 85 YPEEIPGVSNLEflRSALNARrsARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRsvnegFSGGEKKRNEILQMALLEPK 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTH 201
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-222 |
2.53e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 26 ISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLdTATGGSYKIDGKETIELTNDQLSDLR-----SQKFGFI---FQRYNLL 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFAmpvFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVALPAIYagmpqnqrlerakQLLEKLGLGDKWQNKPNQLSGGQQQRVSIA-------RALMNGGEIILADEP 170
Cdd:PRK03695 94 QPDKTRTEAVASALN-------------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 171 TGALDShSGENVME-ILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIIS 222
Cdd:PRK03695 161 MNSLDV-AQQAALDrLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLLA 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-221 |
3.15e-11 |
|
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: 63.05 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 1 MNIIEIKQLNRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNiigCLDTATGGSYKIDGKETieltndqLS 80
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLK---ALANRTEGNVSVEGDIH-------YN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQKFGFIFQRYnllSSLTAAENVALPAIYAGmpqnQRLERAKQLleklglgdkwqnKPNQ----LSGGQQQRVSIAR 156
Cdd:cd03233 71 GIPYKEFAEKYPGE---IIYVSEEDVHFPTLTVR----ETLDFALRC------------KGNEfvrgISGGERKRVSIAE 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTHD--KHIAASANRIIEIKDGEII 221
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMaDVLKTTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-228 |
4.15e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 26 ISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKeTIELTNDQLSdLRS--------QKFGFIFQrynlL 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK-PIDIRSPRDA-IRAgimlcpedRKAEGIIP----V 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLtaAENVALPA----IYAGMPQNQRLER--AKQLLEKLGLGDKWQNKP-NQLSGGQQQRVSIARALMNGGEIILADEP 170
Cdd:PRK11288 346 HSV--ADNINISArrhhLRAGCLINNRWEAenADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 171 TGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQKHQ 228
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-201 |
4.70e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGegeNRVHVlKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltnDQlSDLR 83
Cdd:NF033858 267 IEARGLTMRFG---DFTAV-DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-----DA-GDIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 S-QKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGG 162
Cdd:NF033858 337 TrRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQL-HEEGHTIIMVTH 201
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELsREDGVTIFISTH 456
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-220 |
6.07e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.12 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLRSQKfgFIFQRYNLLSSLT 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG---LNIAKIGLHDLRFKI--TIIPQDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGMPQNQRLERA--KQLLEKL--GLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEVWWALELAhlKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1040783748 178 SGENVMEILRQLHEEGhTIIMVTHDKHIAASANRIIEIKDGEI 220
Cdd:TIGR00957 1456 TDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-220 |
7.10e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLdTATGGSYKIDGKEtieLTNDQLSDLRSQKFGFIFQ---RYNLLS 98
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGAL-PRTSGYVTLDGHE---VVTRSPQDGLANGIVYISEdrkRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAENVALPAIYAGMPQNQRLERAKqllEKLGLGDKWQ----NKPNQ------LSGGQQQRVSIARALMNGGEIILAD 168
Cdd:PRK10762 344 GMSVKENMSLTALRYFSRAGGSLKHAD---EQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 169 EPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEI 220
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-207 |
8.25e-11 |
|
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: 64.96 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEgenRVhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDgkETIELTN-DQls 80
Cdd:TIGR03719 321 KVIEAENLTKAFGD---KL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYvDQ-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 dlrsqkfgfifQRYNLLSSLTAAENVA--LPAIYAG---MPQNQRLER-----AKQlleklglgdkwQNKPNQLSGGQQQ 150
Cdd:TIGR03719 393 -----------SRDALDPNKTVWEEISggLDIIKLGkreIPSRAYVGRfnfkgSDQ-----------QKKVGQLSGGERN 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDshsgenvMEILRQLhEEG-----HTIIMVTHDK--------HIAA 207
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLD-------VETLRAL-EEAllnfaGCAVVISHDRwfldriatHILA 512
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-221 |
8.50e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENrVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN------------IIGCLDTATGGS-----YKI 66
Cdd:PTZ00265 1166 IEIMDVNFRYISRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSllmrfydlkndhHIVFKNEHTNDMtneqdYQG 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 67 DGKETIELTN-DQLSDLRSQKFG---FIFQR-------------YNL-----LSSLTAAENVALP-AIYAGMP---QNQR 120
Cdd:PTZ00265 1245 DEEQNVGMKNvNEFSLTKEGGSGedsTVFKNsgkilldgvdicdYNLkdlrnLFSIVSQEPMLFNmSIYENIKfgkEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 121 LERAKQLLEKLGLGDKWQNKPNQ-----------LSGGQQQRVSIARALMNGGEIILADEPTGALDSHSgENVMEilrql 189
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIE----- 1398
|
250 260 270
....*....|....*....|....*....|....
gi 1040783748 190 heegHTIIMVTH--DKHIAASANRIIEIKDGEII 221
Cdd:PTZ00265 1399 ----KTIVDIKDkaDKTIITIAHRIASIKRSDKI 1428
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-273 |
9.38e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.95 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLdTATGGSYKIDGKETIELTndqLSDLR 83
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP---LQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSlTAAENVAlpaiyagmPQNQ-RLERAKQLLEKLGLGDKWQNKPNQ-----------LSGGQQQR 151
Cdd:cd03289 77 -KAFGVIPQKVFIFSG-TFRKNLD--------PYGKwSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 152 VSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHeEGHTIIMVTHDKHIAASANRIIEIKDGEIisdTQKHQVKS 231
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAF-ADCTVILSEHRIEAMLECQRFLVIEENKV---RQYDSIQK 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1040783748 232 AVKNPSVFKGrfGFSKDQLMEAFRMSVSAIVAHKMRSLLTML 273
Cdd:cd03289 223 LLNEKSHFKQ--AISPSDRLKLFPRRNSSKSKRKPRPQIQAL 262
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-219 |
1.37e-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: 62.57 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKST-LMNIIGCLDTATGgsyKIDGKETIELtndqlsdlrSQKFGFIFQ---RYNLL 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSlLMLILGELEPSEG---KIKHSGRISF---------SSQFSWIMPgtiKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKwqnkpnQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:cd03291 120 FGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1040783748 178 SGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGE 219
Cdd:cd03291 194 TEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-205 |
3.63e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.33 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 14 GEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTA--TGGSYKIDGKETIELTNDQLS------DLRSQ 85
Cdd:PLN03140 887 GVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQETFARISgyceqnDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 86 KFgfifqryNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKP--NQLSGGQQQRVSIARALMNGGE 163
Cdd:PLN03140 967 QV-------TVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPS 1039
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHI 205
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
68-218 |
4.85e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 62.92 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 68 GKETIELTNDQLSDLrsqkfgFIFqrynlLSSLTAAEnVALPAIYAGMpqNQRLerakQLLEKLGLGDKWQNKP-NQLSG 146
Cdd:PRK00635 418 GKTFAEFQQMSLQEL------FIF-----LSQLPSKS-LSIEEVLQGL--KSRL----SILIDLGLPYLTPERAlATLSG 479
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040783748 147 GQQQRVSIARALmnGGEII----LADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDG 218
Cdd:PRK00635 480 GEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
122-202 |
6.52e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 122 ER--AKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMV 199
Cdd:COG1245 189 ERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVV 268
|
...
gi 1040783748 200 THD 202
Cdd:COG1245 269 EHD 271
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-218 |
7.77e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKST-LMNIIGCLDTATGgsyKIDGKETIELtndqlsdlrSQKFGFIFQ---RYNLL 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSlLMMIMGELEPSEG---KIKHSGRISF---------SPQTSWIMPgtiKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVALPAIyagmpqnqrleRAKQLLEKLGLGDKWQNKP-----NQLSGGQQQRVSIARALMNGGEIILADEPTG 172
Cdd:TIGR01271 509 FGLSYDEYRYTSVI-----------KACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1040783748 173 ALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDG 218
Cdd:TIGR01271 578 HLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-220 |
8.41e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIgcldtaTGG---SYKID----GK-----ETIeltndqlSDLRsQKFGF 89
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGDhpqGYSNDltlfGRrrgsgETI-------WDIK-KHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 90 IFqrynllSSL-------TAAENVALPA------IYAGMPQNQRLeRAKQLLEKLGLGDKWQNKPNQ-LSGGQQQRVSIA 155
Cdd:PRK10938 341 VS------SSLhldyrvsTSVRNVILSGffdsigIYQAVSDRQQK-LAQQWLDILGIDKRTADAPFHsLSWGQQRLALIV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 156 RALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHT-IIMVTHDKHIAAS--ANRIIEIKDGEI 220
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAciTHRLEFVPDGDI 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-221 |
1.36e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLdTATGGSYKIDGKETI-------- 72
Cdd:PRK15064 318 NALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGEL-EPDSGTVKWSENANIgyyaqdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 73 -ELTNDQ-LSDLRSQkfgfifqrynllssltaaenvalpaiYAGMPQNQRLERAkQLLEKLGLGDKWQNKPNQLSGGQQQ 150
Cdd:PRK15064 393 yDFENDLtLFDWMSQ--------------------------WRQEGDDEQAVRG-TLGRLLFSQDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLheEGhTIIMVTHDKHIAAS-ANRIIEIKDGEII 221
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EG-TLIFVSHDREFVSSlATRIIEITPDGVV 514
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-201 |
1.71e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.18 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 26 ISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieLTNdqLSDLRsQKFGFIFQRYNLLSSLTAAEN 105
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTN--ISDVH-QNMGYCPQFDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 106 VALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEI 185
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170
....*....|....*.
gi 1040783748 186 LRQLHEEGHTIIMVTH 201
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSH 2128
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-221 |
2.08e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 60.80 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNII--GCLDT------ATGGSYK-IDGKETIE---------------- 73
Cdd:TIGR00630 620 RENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTlyPALANrlngakTVPGRYTsIEGLEHLDkvihidqspigrtprs 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 74 --LTN----DQLSDL-----RSQKFGFIFQRYNLLSSLTAAENVA-----------LPAIYAGMPQ-------NQRLE-- 122
Cdd:TIGR00630 700 npATYtgvfDEIRELfaetpEAKVRGYTPGRFSFNVKGGRCEACQgdgvikiemhfLPDVYVPCEVckgkrynRETLEvk 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 123 ----------------------------RAKQLLEKLGLG--DKWQNKPNqLSGGQQQRVSIARALM---NGGEIILADE 169
Cdd:TIGR00630 780 ykgkniadvldmtveeayeffeavpsisRKLQTLCDVGLGyiRLGQPATT-LSGGEAQRIKLAKELSkrsTGRTLYILDE 858
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 170 PTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEI------KDGEII 221
Cdd:TIGR00630 859 PTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVV 916
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-201 |
2.48e-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: 60.69 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLNRYFGEGENRVhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLdTATGGSYKIDGketIELTNDQLSDLR 83
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG---VSWNSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 sQKFGFIFQRYNLLSSlTAAENVALPAIYAGmpqnqrlERAKQLLEKLGLGDKWQNKPNQ-----------LSGGQQQRV 152
Cdd:TIGR01271 1292 -KAFGVIPQKVFIFSG-TFRKNLDPYEQWSD-------EEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLM 1362
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1040783748 153 SIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGhTIIMVTH 201
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC-TVILSEH 1410
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-203 |
2.77e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtieLTNDQLSdlRSQKFGFIFQRYNLLSSLT 101
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS---IKKDLCT--YQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAEN----VALPAIYAGMPQNQRLERAKQLLE-KLGLgdkwqnkpnqLSGGQQQRVSIARALMNGGEIILADEPTGALDS 176
Cdd:PRK13540 91 LRENclydIHFSPGAVGITELCRLFSLEHLIDyPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*..
gi 1040783748 177 HSGENVMEILRQLHEEGHTIIMVTHDK 203
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-202 |
3.99e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.80 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDF-----VAIMGQSGSGKSTLMNIIGcldtatgGSYKIDGKEtIELTNDQLSdLRSQKFGFIFQR--YN 95
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLA-------GVLKPDEGD-IEIELDTVS-YKPQYIKADYEGtvRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 96 LLSSLTAaenvalpaIYAGMPQNQrleraKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALD 175
Cdd:cd03237 81 LLSSITK--------DFYTHPYFK-----TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180
....*....|....*....|....*...
gi 1040783748 176 SHSGENVMEILRQLHEEGH-TIIMVTHD 202
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEkTAFVVEHD 175
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-219 |
4.40e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 4 IEIKQLnRYFGEGENRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNdqLSDLR 83
Cdd:PTZ00265 383 IQFKNV-RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDIN--LKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 84 SqKFGFIFQ-------------RYNLLS-----------------------------------------SLTAAENVALP 109
Cdd:PTZ00265 460 S-KIGVVSQdpllfsnsiknniKYSLYSlkdlealsnyynedgndsqenknkrnscrakcagdlndmsnTTDSNELIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 110 AIYAGMPQNQRLERAKQLLEK---LGLGDKWQ----NKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENV 182
Cdd:PTZ00265 539 KNYQTIKDSEVVDVSKKVLIHdfvSALPDKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270
....*....|....*....|....*....|....*...
gi 1040783748 183 MEILRQLH-EEGHTIIMVTHDKHIAASANRIIEIKDGE 219
Cdd:PTZ00265 619 QKTINNLKgNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-193 |
4.53e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEgenRVhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIdGkETIELTN-DQls 80
Cdd:PRK11819 323 KVIEAENLSKSFGD---RL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETVKLAYvDQ-- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 dlrsqkfgfifQRYNLLSSLTAAENVA--LPAIYAG---MPQnqrleRA-------KqlleklglGDKWQNKPNQLSGGQ 148
Cdd:PRK11819 395 -----------SRDALDPNKTVWEEISggLDIIKVGnreIPS-----RAyvgrfnfK--------GGDQQKKVGVLSGGE 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1040783748 149 QQRVSIARALMNGGEIILADEPTGALDshsgenvMEILRQLhEEG 193
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLD-------VETLRAL-EEA 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-226 |
5.16e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKEtIELTNDQlsDLRSQKFGFIFQRYNLLSS 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE-IDFKSSK--EALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 100 LTAAENVAL---PAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDS 176
Cdd:PRK10982 88 RSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 177 HSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIIsDTQK 226
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQWI-ATQP 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-218 |
7.26e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTL----MNIIgcldTATGGSYKIDGKetiELTNDQLSDLRSQkFGFIFQRYNLL 97
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLlltfMRMV----EVCGGEIRVNGR---EIGAYGLRELRRQ-FSMIPQDPVLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSlTAAENV-----ALPA-IYAGMPQNQRLERAKQllEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE-IILADEP 170
Cdd:PTZ00243 1397 DG-TVRQNVdpfleASSAeVWAALELVGLRERVAS--ESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEA 1473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1040783748 171 TG----ALDSHSGENVMEILrqlheEGHTIIMVTHDKHIAASANRIIEIKDG 218
Cdd:PTZ00243 1474 TAnidpALDRQIQATVMSAF-----SAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-233 |
7.79e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEgenrVHVLKDISLSIEKGDFVAIMGQSGSGKSTlmniiGCLDTATGGSYKIDGKETIELTNDQLSD 81
Cdd:NF000106 12 NAVEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**R-----GALPAHV*GPDAGRRPWRF*TWCANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNG 161
Cdd:NF000106 83 LRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040783748 162 GEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAAS-ANRIIEIKDGEIISDTQKHQVKSAV 233
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKV 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-202 |
1.13e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 30 IEKGDFVAIMGQSGSGKSTLMNII-GCLDTATGGSYKIDGKETI-------ELtNDQLSDLRSQKfgfifqrynllssLT 101
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsGELIPNLGDYEEEPSWDEVlkrfrgtEL-QNYFKKLYNGE-------------IK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENV----ALPAIYAGmPQNQRLERA------KQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPT 171
Cdd:PRK13409 162 VVHKPqyvdLIPKVFKG-KVRELLKKVdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|.
gi 1040783748 172 GALDSHSGENVMEILRQLhEEGHTIIMVTHD 202
Cdd:PRK13409 241 SYLDIRQRLNVARLIREL-AEGKYVLVVEHD 270
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
122-202 |
1.23e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 122 ERAKQ--LLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMV 199
Cdd:cd03236 116 ERGKLdeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVV 195
|
...
gi 1040783748 200 THD 202
Cdd:cd03236 196 EHD 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-253 |
1.44e-08 |
|
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: 57.53 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENRVHVlKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLDTATGGSYKIDGKETieltnDQLSD 81
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPV-----DIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 82 LRSQKFGFIF-----QRYNLLSSLTAAENVALPAI--YAGMpqnQRLERAKQL------LEKLGLGDKWQNKP-NQLSGG 147
Cdd:TIGR02633 331 AQAIRAGIAMvpedrKRHGIVPILGVGKNITLSVLksFCFK---MRIDAAAELqiigsaIQRLKVKTASPFLPiGRLSGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 148 QQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISDTQK 226
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGDFVN 487
|
250 260
....*....|....*....|....*..
gi 1040783748 227 HqvksavknpsvfkgrfGFSKDQLMEA 253
Cdd:TIGR02633 488 H----------------ALTQEQVLAA 498
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-220 |
2.20e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 14 GEGenrvhvLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQ--------LSDLRsQ 85
Cdd:PRK15439 276 GEG------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvyLPEDR-Q 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 86 KFGFIFQ---RYNLlSSLTaaenvalpaiYAGMPQNQRLERAKQLLEKL--GLGDKWqNKPNQ----LSGGQQQRVSIAR 156
Cdd:PRK15439 349 SSGLYLDaplAWNV-CALT----------HNRRGFWIKPARENAVLERYrrALNIKF-NHAEQaartLSGGNQQKVLIAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 157 ALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIKDGEI 220
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEeIEQMADRVLVMHQGEI 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
5-201 |
2.51e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 5 EIKQLNRYFGEGENRvHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIeltndqlsdlrs 84
Cdd:PRK13545 23 KLKDLFFRSKDGEYH-YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 qkfgfIFQRYNLLSSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGdKWQNKP-NQLSGGQQQRVSIARALMNGGE 163
Cdd:PRK13545 90 -----IAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIG-KFIYQPvKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1040783748 164 IILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTH 201
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISH 201
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-201 |
2.89e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 2 NIIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLD--TATGGSYKIDGKETIELTNDQl 79
Cdd:CHL00131 6 PILEIKNLHASVNENE----ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 80 sdlRSQKFGFIFQRY-------NLLSSLTAAENVALpaIYAGMPQNQRLERAKQLLEKLGLGDKWQ-----NKPNQLSGG 147
Cdd:CHL00131 81 ---RAHLGIFLAFQYpieipgvSNADFLRLAYNSKR--KFQGLPELDPLEFLEIINEKLKLVGMDPsflsrNVNEGFSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 148 QQQRVSIAR-ALMNGGEIILaDEPTGALDSHSGENVMEILRQLHEEGHTIIMVTH 201
Cdd:CHL00131 156 EKKRNEILQmALLDSELAIL-DETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
20-215 |
2.93e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.15 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN--IIGCLDTATGGSY----KIDG-----------------KETIELTN 76
Cdd:PRK00635 608 KHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtLVPAVEEFIEQGFcsnlSIQWgaisrlvhitrdlpgrsQRSIPLTY 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 77 ----DQLSDL-----RSQKFGFIFQRYNL------------LSSLTAAEN---VALPAIYAGMPQNQRLE---------- 122
Cdd:PRK00635 688 ikafDDLRELfaeqpRSKRLGLTKSHFSFntplgacaecqgLGSITTTDNrtsIPCPSCLGKRFLPQVLEvrykgkniad 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 123 -------RAKQLL-------EK------LGLGDKWQNKP-NQLSGGQQQRVSIARALMNGGE---IILADEPTGALDSHS 178
Cdd:PRK00635 768 ilemtayEAEKFFldepsihEKihalcsLGLDYLPLGRPlSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHD 847
|
250 260 270
....*....|....*....|....*....|....*..
gi 1040783748 179 GENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEI 215
Cdd:PRK00635 848 IKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-201 |
4.87e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 15 EGENRVhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNiigCLDTATGGSYKIDGketIELTNDQLSDLRSQK-FGFIFQR 93
Cdd:TIGR00956 772 KKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTTLLN---VLAERVTTGVITGG---DRLVNGRPLDSSFQRsIGYVQQQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 94 YNLLSSLTAAENVALPAiYAGMPQ-------NQRLERAKQLLEKLGLGDKWQNKPNQ-LSGGQQQRVSIARALM-NGGEI 164
Cdd:TIGR00956 845 DLHLPTSTVRESLRFSA-YLRQPKsvsksekMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVaKPKLL 923
|
170 180 190
....*....|....*....|....*....|....*..
gi 1040783748 165 ILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTH 201
Cdd:TIGR00956 924 LFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-202 |
7.50e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDF-----VAIMGQSGSGKSTLMNIIGCLDTATGG--------SYK-----IDGKETIEltnDQLSDLRS 84
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlkiSYKpqyisPDYDGTVE---EFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 QKFGfifqrynllSSLTAAEnvalpaiyagmpqnqrlerakqLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEI 164
Cdd:COG1245 428 DDFG---------SSYYKTE----------------------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190
....*....|....*....|....*....|....*....
gi 1040783748 165 ILADEPTGALDSHSGENVMEILRQLHEE-GHTIIMVTHD 202
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHD 515
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-201 |
7.77e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 18 NRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETielTNDQlsdlRSQKFGFIFQRYNLL 97
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGD----RSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVALPAIYAGmpqnqrlERAKQL----LEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGA 173
Cdd:PRK13543 95 ADLSTLENLHFLCGLHG-------RRAKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180
....*....|....*....|....*....
gi 1040783748 174 LDSHSGENVMEILR-QLHEEGHTIImVTH 201
Cdd:PRK13543 168 LDLEGITLVNRMISaHLRGGGAALV-TTH 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-216 |
1.00e-07 |
|
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: 51.98 E-value: 1.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040783748 143 QLSGGQQQRVSIARAL----MNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIK 216
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-202 |
1.53e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 18 NRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSdlrsqkfgfifqrynll 97
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLS----------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 98 SSLTAAENVALPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*
gi 1040783748 178 SGENVMEILRQLHEEGHTIIMVTHD 202
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHN 202
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
140-219 |
2.29e-07 |
|
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: 51.42 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 140 KPN--QLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGH-TIIMVTHDKHIAASANRIIEIK 216
Cdd:cd03222 66 KPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVF 145
|
...
gi 1040783748 217 DGE 219
Cdd:cd03222 146 EGE 148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-191 |
3.53e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 18 NRVHVLKDISLSIEKGDFVAIMGQSGSGKSTLmniigcLDTATGGSYKIDGKETIELTNDQLS--DLRSQKFG---FIFQ 92
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTL------LKTIASNTDGFHIGVEGVITYDGITpeEIKKHYRGdvvYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 93 RYNLLSSLTAAENVALPAIYAGmPQNQ-----RLERAKQL----LEKLGLGDKWQNKPNQ-----LSGGQQQRVSIARAL 158
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAARCKT-PQNRpdgvsREEYAKHIadvyMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEAS 224
|
170 180 190
....*....|....*....|....*....|...
gi 1040783748 159 MNGGEIILADEPTGALDSHSGenvMEILRQLHE 191
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATA---LEFIRALKT 254
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-220 |
3.56e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNII-GCLDTATGGSYkidgketieltndqlsdlRSQKFGF-IFQRYNLLS- 98
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIsGELQPSSGTVF------------------RSAKVRMaVFSQHHVDGl 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAENVALPAIYAGMPQnQRLeRAKqlLEKLGLGDKWQNKP-NQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:PLN03073 586 DLSSNPLLYMMRCFPGVPE-QKL-RAH--LGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1040783748 178 SGENVMEILrQLHEEGhtIIMVTHDKH-IAASANRIIEIKDGEI 220
Cdd:PLN03073 662 AVEALIQGL-VLFQGG--VLMVSHDEHlISGSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-202 |
5.27e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIE-----KGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSykIDGKETI-----ELTNDQlsDLRSQKFgfifq 92
Cdd:PRK13409 350 LGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPELKIsykpqYIKPDY--DGTVEDL----- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 93 rynlLSSLTAAenvalpaiYAGMPQNQrlerakQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTG 172
Cdd:PRK13409 421 ----LRSITDD--------LGSSYYKS------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190
....*....|....*....|....*....|.
gi 1040783748 173 ALDSHSGENVMEILRQLHEE-GHTIIMVTHD 202
Cdd:PRK13409 483 HLDVEQRLAVAKAIRRIAEErEATALVVDHD 513
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-216 |
5.29e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 20 VHVLKD-ISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLS 98
Cdd:PRK10636 13 VRVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAENVA---------------LPAIYAGMPQNqrleRAKQLLEKLGLGDKWQNKP-NQLSGGQQQRVSIARALMNGG 162
Cdd:PRK10636 93 QLEAQLHDAnerndghaiatihgkLDAIDAWTIRS----RAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 163 EIILADEPTGALDSHSgenVMEILRQLHEEGHTIIMVTHDKH-IAASANRIIEIK 216
Cdd:PRK10636 169 DLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILISHDRDfLDPIVDKIIHIE 220
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-221 |
1.04e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.68 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTL----MNIIGCLDtatgGSYKIDGketIELTNDQLSDLRSqKFGFIFQ----- 92
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDG---IDISKLPLHTLRS-RLSIILQdpilf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 93 ----RYNLLSSLTAAENVALPAIyagmpqnqRLERAKQLLEKL--GLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIIL 166
Cdd:cd03288 108 sgsiRFNLDPECKCTDDRLWEAL--------EIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1040783748 167 ADEPTGALDSHSgENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-221 |
1.05e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGketIELTNDQLSDLRsqKFGFIFQRYNLLSSLT 101
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVAKFGLTDLR--RVLSIIPQSPVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 AAENVALPAIYAGMPQNQRLERA--KQLLEK--LGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSH 177
Cdd:PLN03232 1326 VRFNIDPFSEHNDADLWEALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1040783748 178 SGENVMEILRQlHEEGHTIIMVTHDKHIAASANRIIEIKDGEII 221
Cdd:PLN03232 1406 TDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-222 |
1.36e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 35 FVAIMGQSGSGKSTlmnIIGCLDTATGG-----SYKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENValp 109
Cdd:cd03240 24 LTLIVGQNGAGKTT---IIEALKYALTGelppnSKGGAHDPKLIREGEVRAQVKLAFENANGKKYTITRSLAILENV--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 110 aIYagMPQNqrlERAKQLLEKLGlgdkwqnkpnQLSGGQQQ------RVSIARALMNGGEIILADEPTGALDSHSGENVM 183
Cdd:cd03240 98 -IF--CHQG---ESNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1040783748 184 -EILR-QLHEEGHTIIMVTHDKHIAASANRIIEI-KDGEIIS 222
Cdd:cd03240 162 aEIIEeRKSQKNFQLIVITHDEELVDAADHIYRVeKDGRQKS 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-204 |
1.37e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 40 GQSGSGKSTLMNIIGCLDTATGGSYKIDgketielTNDQLSDLRSQKFGFifQRYNLL---------------------S 98
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLD-------PNERLGKLRQDQFAF--EEFTVLdtvimghtelwevkqerdriyA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 99 SLTAAEN----VA-LPAIYAGMPQNQRLERAKQLLEKLGLGDKWQNKP-NQLSGGQQQRVSIARALMNGGEIILADEPTG 172
Cdd:PRK15064 105 LPEMSEEdgmkVAdLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1040783748 173 ALDSHS---GENVmeilrqLHEEGHTIIMVTHDKH 204
Cdd:PRK15064 185 NLDINTirwLEDV------LNERNSTMIIISHDRH 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-236 |
1.55e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN-IIGCLDTATGGSYKIDGKE-TIELTNDQLsdlrsqKFGFIF----- 91
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPvKIRNPQQAI------AQGIAMvpedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 92 QRYNLLSSLTAAENVALPAI--YAGMpqnQRLERAKQL------LEKLGLGDKWQNKP-NQLSGGQQQRVSIARALMNGG 162
Cdd:PRK13549 348 KRDGIVPVMGVGKNITLAALdrFTGG---SRIDDAAELktilesIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 163 EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHD-KHIAASANRIIEIKDGEIISD------TQKHQVKSAVKN 235
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGDlinhnlTQEQVMEAALRS 504
|
.
gi 1040783748 236 P 236
Cdd:PRK13549 505 E 505
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
142-215 |
2.66e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 50.87 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 142 NQLSGGQQ------QRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEI 215
Cdd:NF041034 778 NALSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEELKEISDYIISV 857
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-218 |
2.92e-06 |
|
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: 50.40 E-value: 2.92e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040783748 142 NQLSGGQQQRVSIARALMNG--GEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDG 218
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGPG 565
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-175 |
3.60e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 22 VLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETIELTndqLSDLRsQKFGFIFQRynllsslt 101
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQA-------- 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 102 aaenvalPAIYAGM------PQNQR--------LERA--KQLLEK--LGLGDKWQNKPNQLSGGQQQRVSIARALMNGGE 163
Cdd:PLN03130 1322 -------PVLFSGTvrfnldPFNEHndadlwesLERAhlKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170
....*....|..
gi 1040783748 164 IILADEPTGALD 175
Cdd:PLN03130 1395 ILVLDEATAAVD 1406
|
|
| FtsX |
COG2177 |
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning]; |
467-627 |
6.69e-06 |
|
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441780 [Multi-domain] Cd Length: 292 Bit Score: 48.29 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 467 SITVKISDDVNSTVAEksLTELLKSLHGKkDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIgVMNIMLVSVTE 546
Cdd:COG2177 120 SIEVKLKPEDPEDLEA--LAAALEALPGV-AEVDYDREWVERLFALLNLLRLVGLVLAALLLLAAVLL-IGNTIRLAIYS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 547 RTKEIGV-RMaIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFNS-------FITDFSMDFSTASIVTAVL-FS 617
Cdd:COG2177 196 RREEIEImKL-VGATDGFIRRPFLLEGALLGLLGGLLALLLLALLYLLLVSaladglaFLSLLSLGGLLLLLLLLLLlLG 274
|
170
....*....|
gi 1040783748 618 TLIGVLFGYM 627
Cdd:COG2177 275 ALLGALGSRL 284
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-219 |
9.61e-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: 45.83 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 32 KGDFVAIMGQSGSGKSTLMN-IIGCLDTATGGSYKIDGKETIELTNDQLSDLRSQKfgfifqrynllssltaaenvalpa 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 111 iyagmpqnqrlerakqlleklglgdkwqnKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILR--- 187
Cdd:smart00382 57 -----------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1040783748 188 ---QLHEEGHTIIMVTHDKHIAASAN------RIIEIKDGE 219
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALlrrrfdRRIVLLLIL 148
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-205 |
1.46e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGEnrvhVLKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLD--TATGGSYKIDGKETIELTNDQls 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 dlRSQKFGFI-FQ----------RYNLLSSLTAAENvalpaiYAGMPQNQRLERAKQLLEKLGLGDKWQNKPNQ-----L 144
Cdd:PRK09580 75 --RAGEGIFMaFQypveipgvsnQFFLQTALNAVRS------YRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRsvnvgF 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040783748 145 SGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHI 205
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRI 207
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
36-202 |
2.63e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.77 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 36 VAIMGQSGSGKSTLMNII-----GCLDTAT-----------------------GGSYKI---DGkETIELTNDQlSDLRS 84
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryalyGKARSRSklrsdlinvgseeasvelefehgGKRYRIerrQG-EFAEFLEAK-PSERK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 85 QKFGFIFQ--RYNLLSSLTAAENVALPAIYAGMPQNQRLERakQLLEKL-GLGDkwqnkPNQLSGGQQQRVSIARALmng 161
Cdd:COG0419 104 EALKRLLGleIYEELKERLKELEEALESALEELAELQKLKQ--EILAQLsGLDP-----IETLSGGERLRLALADLL--- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1040783748 162 gEIILaDepTGALDSHSGENVMEILRQLHeeghtiiMVTHD 202
Cdd:COG0419 174 -SLIL-D--FGSLDEERLERLLDALEELA-------IITHV 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
68-201 |
3.01e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 68 GKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVAlpAIYAGMPQNQRLERakqlleklglgdkwqNKPNQLSGG 147
Cdd:PLN03073 286 GKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAA--SILAGLSFTPEMQV---------------KATKTFSGG 348
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1040783748 148 QQQRVSIARALMNGGEIILADEPTGALDSHSgenVMEILRQLHEEGHTIIMVTH 201
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSH 399
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-51 |
4.42e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 4.42e-05
10 20
....*....|....*....|....*....
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMN 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-49 |
4.56e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 4.56e-05
10 20 30
....*....|....*....|....*....|.
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTL 49
Cdd:COG0178 12 REHNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
144-216 |
4.62e-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: 44.95 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 144 LSGGQQQRVSIARAL-------MNGG---EIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRII 213
Cdd:cd03279 124 LSGGETFLASLSLALalsevlqNRGGarlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRL 203
|
...
gi 1040783748 214 EIK 216
Cdd:cd03279 204 EVI 206
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-199 |
5.49e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 3 IIEIKQLNRYFGEGENRvHVLKDISLSIEKGDFVAIMGQSGSGKSTL-MNIIG-CLDTATGGSYKIDGKEtIELTNdqLS 80
Cdd:NF040905 257 VFEVKNWTVYHPLHPER-KVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrSYGRNISGTVFKDGKE-VDVST--VS 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 81 DLRSQKFGFIFQ---RYNLLSSLTAAENV---ALPAIYAGMPQNQRLER--AKQLLEKLGL--GDKWQNKPNqLSGGQQQ 150
Cdd:NF040905 333 DAIDAGLAYVTEdrkGYGLNLIDDIKRNItlaNLGKVSRRGVIDENEEIkvAEEYRKKMNIktPSVFQKVGN-LSGGNQQ 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1040783748 151 RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMV 199
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-51 |
5.95e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 5.95e-05
10 20 30
....*....|....*....|....*....|...
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTLMN 51
Cdd:COG0178 617 RENNLKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
144-221 |
6.31e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 144 LSGGQQQRVSIARALM---NGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEI----- 215
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLgpegg 906
|
....*..
gi 1040783748 216 -KDGEII 221
Cdd:COG0178 907 dGGGEIV 913
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-49 |
1.16e-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: 45.39 E-value: 1.16e-04
10 20 30
....*....|....*....|....*....|.
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTL 49
Cdd:TIGR00630 8 REHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-200 |
1.29e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 23 LKDISLSIEKGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSYKIDGKETieltnDQLSDLRSQKFGFifqrynllsSLTA 102
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI-----NNHNANEAINHGF---------ALVT 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 103 AENVAlPAIYAGMPQ--NQRLERAKQLLEKLGLGD--------KW------------QNKPNQLSGGQQQRVSIARALMN 160
Cdd:PRK10982 330 EERRS-TGIYAYLDIgfNSLISNIRNYKNKVGLLDnsrmksdtQWvidsmrvktpghRTQIGSLSGGNQQKVIIGRWLLT 408
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1040783748 161 GGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVT 200
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
19-49 |
2.57e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 2.57e-04
10 20 30
....*....|....*....|....*....|.
gi 1040783748 19 RVHVLKDISLSIEKGDFVAIMGQSGSGKSTL 49
Cdd:PRK00349 12 REHNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-218 |
1.30e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 119 QRLERAKQLLEKLGLG--DKWQNKpNQLSGGQQQRVSIARALMNGGE---IILADEPTGALDSHSGENVMEILRQLHEEG 193
Cdd:PRK00635 1674 KKIQKPLQALIDNGLGylPLGQNL-SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLG 1752
|
90 100
....*....|....*....|....*
gi 1040783748 194 HTIIMVTHDKHIAASANRIIEIKDG 218
Cdd:PRK00635 1753 HSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
32-62 |
1.94e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.45 E-value: 1.94e-03
10 20 30
....*....|....*....|....*....|..
gi 1040783748 32 KGDFVAIMGQSGSGKSTLMN-IIGCLDTATGG 62
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNaLLPELDLRTGE 136
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
142-216 |
2.45e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040783748 142 NQLSGGQQQ------RVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTI---IMVTHDKHIAASANRI 212
Cdd:PRK01156 800 DSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIpqvIMISHHRELLSVADVA 879
|
....
gi 1040783748 213 IEIK 216
Cdd:PRK01156 880 YEVK 883
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
144-215 |
8.64e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 8.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040783748 144 LSGGQQQRVSIARALMNG--GEI-ILaDEPTGALdsHSGEN--VMEILRQLHEEGHTIIMVTHDKHIAASANRIIEI 215
Cdd:COG0178 486 LSGGEAQRIRLATQIGSGlvGVLyVL-DEPSIGL--HQRDNdrLIETLKRLRDLGNTVIVVEHDEDTIRAADYIIDI 559
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
32-61 |
9.75e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 9.75e-03
10 20 30
....*....|....*....|....*....|.
gi 1040783748 32 KGDFVAIMGQSGSGKSTLMN-IIGCLDTATG 61
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNaLLPELVLATG 114
|
|
| |
