|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-647 |
0e+00 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 1208.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQIISDNNNHHSVPVKKAP-PA 239
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTePV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 240 IQTASYFHQVIGRFTQALNMAWRAMVVNKIRTLLTMLGIIIGIASVVTIIVIGDAAKDRVLADIKAIGANTIDIYPGKEL 319
Cdd:PRK10535 241 VNTASGWRQFVSGFREALTMAWRAMAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRAIGTNTIDIYPGKDF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 320 GSDSPEDKQSLTIQDVDALKQQSYIQSVTPQIYFSSRLRRGNQDAPATVSGVNEDYFSVYALKFAQGSTFTPDMIHRQAQ 399
Cdd:PRK10535 321 GDDDPQYQQALKYDDLIAIQKQPWVASATPAVSQSLRLRYGNIDVAASANGVSGDYFNVYGMTFSEGNTFNQEQLNGRAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 400 VVVIDENTRHRFFPNKQAVIGEQIIIRNIPSTIIGVVAEQKSTFGDNKSLRVWVPYSTLSSRIYNRSYLDNITVKVKEGY 479
Cdd:PRK10535 401 VVVLDSNTRRQLFPHKADVVGEVILVGNMPATVIGVAEEKQSMFGSSKVLRVWLPYSTMSGRVMGQSWLNSITVRVKEGY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 480 DASVAEQQILRLLTIRHGKKDIFTYNIDSFIKAAEKTTQTMQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMA 559
Cdd:PRK10535 481 DSAEAEQQLTRLLTLRHGKKDFFTWNMDSVLKTAEKTTRTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 560 VGARASDVMQQFLIESVLVCLVGGLLGISLSFAIAMFASMMLPNWHFVFQPTALISAFACSTAIGVIFGFLPARNAAKMN 639
Cdd:PRK10535 561 VGARASDVLQQFLIEAVLVCLVGGALGITLSLLIAFTLQLFLPGWEIGFSPLALLSAFLCSTVTGILFGWLPARNAARLD 640
|
....*...
gi 490367952 640 PIDALARE 647
Cdd:PRK10535 641 PVDALARE 648
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-224 |
4.21e-130 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 382.08 E-value: 4.21e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-221 |
6.54e-115 |
|
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: 342.55 E-value: 6.54e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALR 84
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| SalY |
COG0577 |
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms]; |
255-647 |
1.50e-94 |
|
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
Pssm-ID: 440342 [Multi-domain] Cd Length: 339 Bit Score: 294.88 E-value: 1.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 255 QALNMAWRAMVVNKIRTLLTMLGIIIGIASVVTIIVIGDAAKDRVLADIKAIGANTIDIYpgkelgSDSPEDKQSLTIQD 334
Cdd:COG0577 1 EYLRLALRSLRRNKLRSLLTVLGIAIGIALVIAILALGRGLRRSLLRDLDSLGFDLLTVS------RTPGGSRATLSYED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 335 V-DALKQQSYIQSVTPQIYFSSRLR-RGNQDAPATVSGVNEDYFSVYALKFAQGSTFTPDMIHRQAQVVVIDENTRHRFF 412
Cdd:COG0577 75 LrEALRALPGVESVAPSSSGSATVRyGGGEPPSVRVLGVDPDYFRVLGIPLLAGRFFTAADDLGAPPVVVIGEALARRLF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 413 PNKQAvIGEQIIIRNIPSTIIGVVaeqkstfgdnkslrvwvpystlssriynrsyldnitvkvkegydasvaEQQILRLL 492
Cdd:COG0577 155 GGEDP-VGKTIRLNGRPFTVVGVV------------------------------------------------EAELRALL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 493 TIRHGKKDIFTYNIDSFIKAAEKTTQTMQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVMQQFL 572
Cdd:COG0577 186 RRRDPGDDFEVQTLDEILAALYGVLRTLTLLLGAIAGLALLVACIGIMNLMLASVTERTREIGIRKALGASRRDILRQFL 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 573 IESVLVCLVGGLLGISLSFAIAMFASMMLPnWHFVFQPTALISAFACSTAIGVIFGFLPARNAAKMNPIDALARE 647
Cdd:COG0577 266 TEALLLALLGGLLGLLLALLLLRLLAALLG-LPVSLDPWVLLLALALSLLVGLLAGLYPARRAARLDPVEALRSE 339
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-224 |
1.23e-86 |
|
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: 270.46 E-value: 1.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLA 81
Cdd:COG4181 6 APIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALRREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSteQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-224 |
5.35e-83 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 260.37 E-value: 5.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALR 84
Cdd:COG2884 2 IRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:COG2884 79 R-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQIISD 224
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLeLVDRMPKRVLELEDGRLVRD 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-224 |
7.75e-73 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 234.95 E-value: 7.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAA 82
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 LRREhFGFIFQRYHLMAHLTAEQNV------EIPAIYA--GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVS 154
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRSllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHDPLIAQQ-ADRIIEIKDGQIISD 224
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRyADRIIGLRDGRVVFD 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-222 |
4.18e-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: 4.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDqLAAL 83
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD-INKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREhFGFIFQRYHLMAHLTAEQNVEIPAIYA-GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNG 162
Cdd:COG1126 76 RRK-VGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 163 GEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-216 |
9.00e-71 |
|
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: 227.88 E-value: 9.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 7 LNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRRE 86
Cdd:TIGR03608 1 LKNISKKF----GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 87 HFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVI 166
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490367952 167 LADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEI 216
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-214 |
9.36e-71 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 229.98 E-value: 9.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDql 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aalrrehFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:COG1116 82 -------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 161 NGGEVILADEPTGALDSQSgKEVMA--ILKQLNQQGHTVIIVTHDP-----LiaqqADRII 214
Cdd:COG1116 155 NDPEVLLMDEPFGALDALT-RERLQdeLLRLWQETGKTVLFVTHDVdeavfL----ADRVV 210
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-221 |
1.52e-67 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 219.98 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-214 |
2.19e-66 |
|
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: 216.95 E-value: 2.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesdqlaalR 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 165 VILADEPTGALDSQSgKEVM--AILKQLNQQGHTVIIVTHDplIAQQ---ADRII 214
Cdd:cd03293 152 VLLLDEPFSALDALT-REQLqeELLDIWRETGKTVLLVTHD--IDEAvflADRVV 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-221 |
2.62e-66 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 217.38 E-value: 2.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLA 81
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALRREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLN-QQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-220 |
6.67e-66 |
|
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: 215.58 E-value: 6.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVA---ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:TIGR02673 78 RR-RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQ 220
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLsLVDRVAHRVIILDDGR 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-222 |
1.38e-65 |
|
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: 215.14 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEmEVVKRICDRVAVMEKGEVV 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-222 |
4.83e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 217.64 E-value: 4.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALR 84
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:COG1135 82 R-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-221 |
2.89e-64 |
|
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: 210.85 E-value: 2.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmESDQLAALR 84
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNVEIPAIYA-GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQI 221
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-224 |
3.93e-63 |
|
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: 208.96 E-value: 3.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT---DINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 --REHFGFIFQRYHLMAHLTAEQNVEIPAI--------YAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVS 154
Cdd:cd03256 75 qlRRQIGMIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQIISD 224
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREyADRIVGLKDGRIVFD 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-221 |
7.82e-63 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 207.71 E-value: 7.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-224 |
3.02e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 206.45 E-value: 3.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE---DVARDPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 RehFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:COG1131 74 R--IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQIISD 224
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVAD 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-220 |
1.96e-61 |
|
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: 203.47 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYTNGEEdtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalrR 85
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 EHFGFIFQ--RYHLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:cd03225 75 RKVGLVFQnpDDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQ 220
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-224 |
7.36e-61 |
|
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: 202.56 E-value: 7.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK---DITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRY-HLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:COG1122 75 R-KVGLVFQNPdDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQIISD 224
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLdLVAELADRVIVLDDGRIVAD 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-226 |
1.06e-60 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 202.63 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlAAL 83
Cdd:PRK09493 1 MIEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHfGFIFQRYHLMAHLTAEQNVEI-PAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNG 162
Cdd:PRK09493 76 RQEA-GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 163 GEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQIISDNN 226
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGD 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-222 |
6.19e-58 |
|
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: 194.28 E-value: 6.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMesdqlaALR 84
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------PPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALAlADRIAVMNEGRIV 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-224 |
6.71e-58 |
|
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: 195.21 E-value: 6.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RReHFGFIFQRYHLMAHLTAEQNVEIPAIYA--------GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSI 155
Cdd:TIGR02315 78 RR-RIGMIFQHYNLIERLTVLENVLHGRLGYkptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQIISD 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKyADRIVGLKAGEIVFD 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-222 |
3.54e-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: 201.67 E-value: 3.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTV-VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAA 82
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 LRReHFGFIFQR-YH-LMAHLTAEQNV-EIPAIYAGKSTEQRKERARALLTRLGL-AERIHYRPSQLSGGQQQRVSIARA 158
Cdd:COG1123 340 LRR-RVQMVFQDpYSsLNPRMTVGDIIaEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDlAVVRYIADRVAVMYDGRIV 484
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
8.26e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 196.09 E-value: 8.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesdqL 80
Cdd:COG3842 2 AMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:COG3842 73 PPEKR-NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 161 NGGEVILADEPTGALDSQS----GKEVMAILKQLnqqGHTVIIVTHDpliaQQ-----ADRIIEIKDGQII 222
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLreemREELRRLQREL---GITFIYVTHD----QEealalADRIAVMNDGRIE 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-221 |
1.79e-56 |
|
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: 190.31 E-value: 1.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALR 84
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03292 78 R-KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQI 221
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-222 |
5.38e-56 |
|
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: 189.64 E-value: 5.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMeSDQLAAL 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGFIFQRYH--LMAHLTAEQNVEIPAIYAGKST--EQRKERARALLTRLGLAERI-HYRPSQLSGGQQQRVSIARA 158
Cdd:cd03257 80 RRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDlGVVAKIADRVAVMYAGKIV 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
1.67e-54 |
|
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: 185.95 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:COG1127 2 SEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRReHFGFIFQRYHLMAHLTAEQNVEIPAI-YAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARAL 159
Cdd:COG1127 78 YELRR-RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKII 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-229 |
6.79e-54 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 184.45 E-value: 6.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSalLELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcVADMESD-- 78
Cdd:PRK11124 1 MS--IQLNGINCFYGA----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN-HFDFSKTps 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 --QLAALRREhFGFIFQRYHLMAHLTAEQN-VEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSI 155
Cdd:PRK11124 74 dkAIRELRRN-VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQIISDNNNHH 229
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASC 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-222 |
8.80e-54 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 184.06 E-value: 8.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSalLELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCV---ADMES 77
Cdd:COG4161 1 MS--IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 78 DQLAALRREhFGFIFQRYHLMAHLTAEQN-VEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:COG4161 75 KAIRLLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-222 |
7.89e-53 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 184.97 E-value: 7.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSalLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDqL 80
Cdd:COG1118 1 MS--IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFTN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:COG1118 71 PPRER-RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALElADRVVVMNQGRIE 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-220 |
9.12e-53 |
|
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: 179.31 E-value: 9.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMEsDQLAALR 84
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNVEIPaiyagksteqrkeraralltrlglaerihyrpsqLSGGQQQRVSIARALMNGGE 164
Cdd:cd03229 76 R-RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQ 220
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-222 |
8.23e-52 |
|
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: 178.46 E-value: 8.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALR 84
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGK-STEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAiADRIAVLYDGKIV 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-222 |
2.42e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 180.77 E-value: 2.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRR 85
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 eHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEV 165
Cdd:PRK11153 83 -QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 166 ILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEmDVVKRICDRVAVIDAGRLV 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-221 |
4.87e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 176.82 E-value: 4.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGcLDKPSSGEYKVAGQCVADmesdq 79
Cdd:COG1121 3 MMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG-LLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 80 laalRREHFGFIFQRYHLMAH--LTAEQNVEIPAIYA----GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRV 153
Cdd:COG1121 73 ----ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQI 221
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLgAVREYFDRVLLLNRGLV 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-221 |
6.77e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.39 E-value: 6.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMesdQLAALR 84
Cdd:COG4619 1 LELEGLSFRVGG----KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REhFGFIFQRYHLMAHlTAEQNVEIPAIYAGKSTEQrkERARALLTRLGLAERIHYRP-SQLSGGQQQRVSIARALMNGG 163
Cdd:COG4619 74 RQ-VAYVPQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHDP-LIAQQADRIIEIKDGQI 221
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
23-203 |
2.08e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 175.76 E-value: 2.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCV------------ADMesDQLAALRREhFGF 90
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpADR--RQLQRIRTR-LGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 91 IFQRYHLMAHLTAEQNV-EIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILAD 169
Cdd:COG4598 100 VFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFD 179
|
170 180 190
....*....|....*....|....*....|....
gi 490367952 170 EPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD 203
Cdd:COG4598 180 EPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHE 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-224 |
7.56e-50 |
|
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: 181.25 E-value: 7.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEEDtvVLDQISLTINAGEMVAIIGASGSGKSTL-MNILGCLDKPS--SGEYKVAGQCVADMEs 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGGriSGEVLLDGRDLLELS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 78 dqlAALRREHFGFIFQRYhlMAHL---TAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVS 154
Cdd:COG1123 78 ---EALRGRRIGMVFQDP--MTQLnpvTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDP-LIAQQADRIIEIKDGQIISD 224
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLgVVAEIADRVVVMDDGRIVED 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-221 |
2.04e-49 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 176.03 E-value: 2.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesdqLAA 82
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-----LPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 LRReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNG 162
Cdd:COG3839 73 KDR-NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 163 GEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQI 221
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTlADRIAVMNDGRI 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
22-222 |
2.91e-49 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 172.24 E-value: 2.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVaGQCVADME---SDQLAALR--REHFGFIFQRYH 96
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTArslSQQKGLIRqlRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 97 LMAHLTAEQNV-EIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGAL 175
Cdd:PRK11264 96 LFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490367952 176 DSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIV 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-224 |
6.73e-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: 171.14 E-value: 6.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESdqlAAL 83
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR---KAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RReHFGFIFQRYHLMAH--LTAEQNVEIPAIYAGKSteQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARALM 160
Cdd:COG1124 78 RR-RVQMVFQDPYASLHprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDP-LIAQQADRIIEIKDGQIISD 224
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLaVVAHLCDRVAVMQNGRIVEE 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-222 |
2.66e-47 |
|
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: 175.33 E-value: 2.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalr 84
Cdd:COG4988 337 IELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMaHLTAEQNVeipAIYAGKSTEQRKERA------RALLTRL--GLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:COG4988 410 RRQIAWVPQNPYLF-AGTIRENL---RLGRPDASDEELEAAleaaglDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-224 |
4.40e-47 |
|
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: 166.37 E-value: 4.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RrehfGFIFQRYHLMAHLTAEQNVE---IPAIYA-GKSTEQRKERARALLTRLGLAERIHyRP-SQLSGGQQQRVSIARA 158
Cdd:COG1120 77 I----AYVPQEPPAPFGLTVRELVAlgrYPHLGLfGRPSAEDREAVEEALERTGLEHLAD-RPvDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHDP-LIAQQADRIIEIKDGQIISD 224
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-221 |
7.79e-47 |
|
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: 165.10 E-value: 7.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesdqLAALR 84
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03300 72 R-PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDpliaQQ-----ADRIIEIKDGQI 221
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHD----QEealtmSDRIAVMNKGKI 209
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-222 |
1.83e-46 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 166.42 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalRR 85
Cdd:COG1125 3 EFENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 eHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIhYR---PSQLSGGQQQRVSIARALMNG 162
Cdd:COG1125 77 -RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEE-YRdryPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 163 GEVILADEPTGALD----SQSGKEVMAILKQLnqqGHTVIIVTHD-----PLiaqqADRIIEIKDGQII 222
Cdd:COG1125 155 PPILLMDEPFGALDpitrEQLQDELLRLQREL---GKTIVFVTHDidealKL----GDRIAVMREGRIV 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-222 |
2.08e-46 |
|
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: 165.12 E-value: 2.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 21 TVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRREHFGFIFQRYHLMAH 100
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 LTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSG 180
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490367952 181 KEVMAILKQLN-QQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:cd03294 197 REMQDELLRLQaELQKTIVFITHDLDEALRlGDRIAIMKDGRLV 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-218 |
5.03e-46 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 161.88 E-value: 5.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDqlaa 82
Cdd:COG4133 1 MMLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 lRREHFGFIFQRYHLMAHLTAEQNVeipAIYAG-KSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:COG4133 73 -YRRRLAYLGHADGLKPELTVRENL---RFWAAlYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLiAQQADRIIEIKD 218
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPL-ELAAARVLDLGD 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-214 |
2.60e-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: 163.69 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDKP--SSGEYKVAGQCVADMESDQL 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQryHLMAHLT-----AEQNVEIPAIYAGKSTEQRKERARALLTRLGL---AERIHYRPSQLSGGQQQR 152
Cdd:COG0444 81 RKIRGREIQMIFQ--DPMTSLNpvmtvGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 153 VSIARALMNGGEVILADEPTGALD--SQsgKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRII 214
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDvtIQ--AQILNLLKDLQRElGLAILFITHDlGVVAEIADRVA 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-222 |
4.63e-45 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 160.54 E-value: 4.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEedtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalr 84
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLaERIHYR---PSQLSGGQQQRVSIARALMN 161
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGL-DPAEFAdryPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIA-QQADRIIEIKDGQII 222
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAfRLADRIAIMKNGEIV 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-221 |
7.30e-45 |
|
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: 157.56 E-value: 7.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAAlr 84
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---DIKKEPEEV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEipaiyagksteqrkeraralltrlglaerihyrpsqLSGGQQQRVSIARALMNGGE 164
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQI 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-224 |
1.73e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 158.76 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngEEDTVvldQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlaalr 84
Cdd:COG3840 2 LRLDDLTYRY---GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REhFGFIFQRYHLMAHLTAEQNVEIpAIYAG-KSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:COG3840 71 RP-VSMLFQENNLFPHLTVAQNIGL-GLRPGlKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHDPL-IAQQADRIIEIKDGQIISD 224
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEdAARIADRVLLVADGRIAAD 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-220 |
2.32e-44 |
|
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: 156.00 E-value: 2.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSrlYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalr 84
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMaHLTAEQNVeipaiyagksteqrkeraralltrlglaerihyrpsqLSGGQQQRVSIARALMNGGE 164
Cdd:cd03228 75 RKNIAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQ 220
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
2.87e-44 |
|
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: 166.87 E-value: 2.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGEEDtvVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDkPSSGEYKVAGQCVADMESDQL 80
Cdd:COG4987 331 GPSLELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLD-PQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aalrREHFGFIFQRYHLMAHlTAEQNVeipAIYAGKSTEqrkERARALLTRLGLAERIHYRP-----------SQLSGGQ 149
Cdd:COG4987 408 ----RRRIAVVPQRPHLFDT-TLRENL---RLARPDATD---EELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 150 QQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
3.12e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 158.87 E-value: 3.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALlELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQl 80
Cdd:COG4525 1 MSML-TVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aalrrehfGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:COG4525 79 --------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490367952 161 NGGEVILADEPTGALDSQSgKEVMA--ILKQLNQQGHTVIIVTHD 203
Cdd:COG4525 151 ADPRFLLMDEPFGALDALT-REQMQelLLDVWQRTGKGVFLITHS 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-224 |
8.31e-44 |
|
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: 156.83 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtnGEedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALr 84
Cdd:cd03219 1 LEVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 rehfGFI--FQRYHLMAHLTAEQNVEIPAIYAGKST----------EQRKERARALLTRLGLAERIHYRPSQLSGGQQQR 152
Cdd:cd03219 76 ----GIGrtFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 153 VSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISD 224
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDmDVVMSLADRVTVLDQGRVIAE 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-222 |
1.17e-43 |
|
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: 156.19 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLmniLGCLDK--------PSSGEYKVAGQCVADME 76
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTL---LRLLNRlndlipgaPDEGEVLLDGKDIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 77 SDQLAaLRREhFGFIFQRyHLMAHLTAEQNVEIPAIYAG-KSTEQRKERARALLTRLGLAERIHYR--PSQLSGGQQQRV 153
Cdd:cd03260 74 VDVLE-LRRR-VGMVFQK-PNPFPGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARvADRTAFLLNGRLV 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-221 |
1.48e-43 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 155.80 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREhFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:PRK10908 78 RRQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDiGLISRRSYRMLTLSDGHL 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-217 |
2.39e-43 |
|
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: 155.00 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLdKPSSGEYKVAGQCVADMesdqlaalr 84
Cdd:cd03235 1 EVEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFGKPLEKE--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAH--LTAEQNVEIPAIYA----GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARA 158
Cdd:cd03235 67 RKRIGYVPQRRSIDRDfpISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIK 217
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLLLN 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-221 |
6.99e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 157.94 E-value: 6.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSalLELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESdql 80
Cdd:PRK10851 1 MS--IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aalRREHFGFIFQRYHLMAHLTAEQNVEIpaiyaGKSTEQRKERA-----RALLTRL-------GLAERIhyrPSQLSGG 148
Cdd:PRK10851 72 ---RDRKVGFVFQHYALFRHMTVFDNIAF-----GLTVLPRRERPnaaaiKAKVTQLlemvqlaHLADRY---PAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 149 QQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQI 221
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-222 |
7.19e-43 |
|
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: 154.42 E-value: 7.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMEsdqlaaLR 84
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNV----EIPAIYAGKSTEQRKERARALL--TRL-GLAERIhyrPSQLSGGQQQRVSIAR 157
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVafglRVKPRSERPPEAEIRAKVHELLklVQLdWLADRY---PAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 158 ALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEvADRVVVMNKGRIE 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-224 |
1.01e-42 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 151.82 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAalrr 85
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 EHFGFIFQryhlmahltaeqnveipaiyagksteqrkeraraLLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEV 165
Cdd:cd03214 73 RKIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 166 ILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDP-LIAQQADRIIEIKDGQIISD 224
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLnLAARYADRVILLKDGRIVAQ 179
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-228 |
2.67e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 153.09 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDqlaal 83
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:COG4555 72 ARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQIISDNNNH 228
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMqEVEALCDRVVILHKGKVVAQGSLD 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-220 |
3.36e-42 |
|
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: 152.20 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVS---RLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLM-----NILgcldkPSSGE--YKVAGQ 70
Cdd:COG4778 1 MTTLLEVENLSktfTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLkciygNYL-----PDSGSilVRHDGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 71 CV--ADMESDQLAALRREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERI-HYRPSQLSG 147
Cdd:COG4778 76 WVdlAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 148 GQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQ 220
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEeVREAVADRVVDVTPFS 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-172 |
6.60e-42 |
|
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: 148.56 E-value: 6.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALRReHFGFIFQRYHLMAHLTA 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ---DLTDDERKSLRK-EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 104 EQNVEIPAIYAGKSTEQRKERARALLTRLGL----AERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPT 172
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
8.78e-42 |
|
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: 152.12 E-value: 8.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSR----LytngeedtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADME 76
Cdd:COG0411 1 SDPLLEVRGLTKrfggL--------VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 77 SDQLAAL---RrehfgfIFQRYHLMAHLTAEQNVEIPAIYAGKST---------------EQRKERARALLTRLGLAERI 138
Cdd:COG0411 73 PHRIARLgiaR------TFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 139 HYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHD-PLIAQQADRIIEI 216
Cdd:COG0411 147 DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDmDLVMGLADRIVVL 226
|
....*...
gi 490367952 217 KDGQIISD 224
Cdd:COG0411 227 DFGRVIAE 234
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-221 |
1.59e-41 |
|
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: 154.42 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesdqL 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR-----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREhFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:TIGR03265 72 PPQKRD-YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIA-QQADRIIEIKDGQI 221
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEAlSMADRIVVMNHGVI 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-220 |
2.12e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 147.39 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalrR 85
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 EHFGFIFQryhlmahltaeqnveipaiyagksteqrkeraralltrlglaerihyrpsqLSGGQQQRVSIARALMNGGEV 165
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 166 ILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQ 220
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-221 |
3.64e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 150.50 E-value: 3.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQ---CVAD-------MESDQLAALRrEHFGFIF 92
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinLVRDkdgqlkvADKNQLRLLR-TRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 93 QRYHLMAHLTAEQNV-EIPAIYAGKSTEQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARALMNGGEVILADE 170
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490367952 171 PTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQI 221
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKI 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-224 |
6.56e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 149.50 E-value: 6.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSrlYTNGeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNIL-GCLdKPSSGEYKVAGQCVADMESDQLAA 82
Cdd:COG4559 1 MLEAENLS--VRLG--GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 LRrehfGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTR---LGLAERiHYRpsQLSGGQQQRVSIARAL 159
Cdd:COG4559 76 RR----AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALvglAHLAGR-SYQ--TLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 160 ------MNGGE-VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISD 224
Cdd:COG4559 149 aqlwepVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDlNLAAQYADRILLLHQGRLVAQ 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-224 |
7.88e-41 |
|
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: 158.84 E-value: 7.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSrlYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI---DLRQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMaHLTAEQNVeipAIYAGKSTEqrkERARALLTRLGLAERIHYRP-----------SQLSGGQQQRV 153
Cdd:COG2274 549 R-QIGVVLQDVFLF-SGTIRENI---TLGDPDATD---EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNqQGHTVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-224 |
8.53e-41 |
|
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: 149.50 E-value: 8.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSrlYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmeSDQLAALR 84
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQR--YHLMAhLTAEQNVeipaiyA------GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:TIGR04520 77 K-KVGMVFQNpdNQFVG-ATVEDDV------AfglenlGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 157 RAL-MNgGEVILADEPTGALDSQSGKEVMAILKQLN-QQGHTVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:TIGR04520 149 GVLaMR-PDIIILDEATSMLDPKGRKEVLETIRKLNkEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-229 |
9.45e-41 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 149.39 E-value: 9.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCL---DKPSSGEYKVAG---QCVAD 74
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGrtvQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 75 MESDQLAAlrREHFGFIFQRYHLMAHLTAEQNVEIPAIyaGKS----------TEQRKERARALLTRLGLAERIHYRPSQ 144
Cdd:PRK09984 77 LARDIRKS--RANTGYIFQQFNLVNRLSVLENVLIGAL--GSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 145 LSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIA-QQADRIIEIKDGQII 222
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAlRYCERIVALRQGHVF 232
|
....*..
gi 490367952 223 SDNNNHH 229
Cdd:PRK09984 233 YDGSSQQ 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-224 |
2.64e-40 |
|
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: 146.67 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 26 QISLTINaGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRREHFGFIFQRYHLMAHLTAEQ 105
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 106 NVEIpaIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMA 185
Cdd:cd03297 95 NLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490367952 186 ILKQLNQQGH-TVIIVTHDPLIAQQ-ADRIIEIKDGQIISD 224
Cdd:cd03297 173 ELKQIKKNLNiPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-221 |
3.15e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 151.25 E-value: 3.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQla 81
Cdd:PRK09452 12 SPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 alrrEHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:PRK09452 86 ----RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDpliaQQ-----ADRIIEIKDGQI 221
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD----QEealtmSDRIVVMRDGRI 223
|
|
| MacB_PCD |
pfam12704 |
MacB-like periplasmic core domain; This family represents the periplasmic core domain found in ... |
271-491 |
2.42e-39 |
|
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: 143.82 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 271 TLLTMLGIIIGIASVVTIIVIGDAAKDRVLADIKAIGaNTIDIYPGKELGSDSPedkQSLTIQDVDALKQQSYIQSVTPQ 350
Cdd:pfam12704 1 TALTVLGIAIGVAAVIAILSLGDGLLSAVPEQISDSD-NLVVVQPGAAGGGGTR---PPLSDPDAEALRRAVPVEAVAPV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 351 IyFSSRLRRGNQDAPATVSGVNEDYFSVYALKFAQGSTFTPDMIHRQAQVVVIDENTRHRFFPNkQAVIGEQIIIRNIPS 430
Cdd:pfam12704 77 V-STVRYGNSTTERLVTVVGVDPDFFKVFGLPLAEGRFFTEADVLGGPNVVVLGESLAEKLFGG-DDPVGKTIRLNGQPF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 431 TIIGVVAEQKSTFGDNksLRVWVPYSTLSSRIynRSYLDNITVKVKEGYDASVAEQQILRL 491
Cdd:pfam12704 155 TVVGVLPDFPGSDGGG--DLVYVPLTTLQRRL--GDSVSTILVRLKDGADLAAAAAELRAL 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-224 |
9.87e-39 |
|
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: 142.25 E-value: 9.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 28 SLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADME-SDQLAALrrehfgfIFQRYHLMAHLTAEQN 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpADRPVSM-------LFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 107 VEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAI 186
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490367952 187 LKQLN-QQGHTVIIVTHDPL-IAQQADRIIEIKDGQIISD 224
Cdd:cd03298 171 VLDLHaETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQ 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-222 |
1.02e-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: 150.22 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKS-TLMNILGCLDKPS---SGEYKVAGQCVADME 76
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 77 SDQLAALRREHFGFIFQRyhlmaHLTA--------EQNVEIPAIYAGKSTEQRKERARALLTRLGLAE---RIHYRPSQL 145
Cdd:COG4172 83 ERELRRIRGNRIAMIFQE-----PMTSlnplhtigKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 146 SGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDlGVVRRFADRVAVMRQGEIV 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-224 |
6.13e-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: 143.40 E-value: 6.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 39 IIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmesdQLAALRReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKST 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLR-HINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 119 EQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALD----SQSGKEVMAILKQLnqqG 194
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---G 151
|
170 180 190
....*....|....*....|....*....|.
gi 490367952 195 HTVIIVTHDPLIA-QQADRIIEIKDGQIISD 224
Cdd:TIGR01187 152 ITFVFVTHDQEEAmTMSDRIAIMRKGKIAQI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-214 |
1.26e-37 |
|
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: 147.05 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalr 84
Cdd:TIGR02857 322 LEFSGVSVAYPGR---RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEqNVEIPAIYAGKSTEQRKERARALLT-----RLGLAERIHYRPSQLSGGQQQRVSIARAL 159
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTIAE-NIRLARPDASDAEIREALERAGLDEfvaalPQGLDTPIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRII 214
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIV 527
|
|
| LolE |
COG4591 |
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ... |
431-647 |
1.30e-37 |
|
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: 141.21 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 431 TIIGVVAEQKSTFGDNkslRVWVPYSTLSSRIYNRSYLDNITVKVKEGYDASVAEQQILRLLtirhgkKDIFTYNIDSFI 510
Cdd:COG4591 69 TVVGIFESGGYELDGS---LVYVPLETAQELLGLGDQVSGILVKLKDGADAEAVAAALEAAL------PGLEVKTWRELN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 511 KAAEKTTQTMQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVMQQFLIESVLVCLVGGLLGISLS 590
Cdd:COG4591 140 AALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLERTREIGILKALGASRRQIRRIFLLEGLLLGLIGGLLGLLLG 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 591 FAIAMFASMMLPNW-------HFVFQPTALISAFACSTAIGVIFGFLPARNAAKMNPIDALARE 647
Cdd:COG4591 220 LLLALLLNALLGILlpfifalPVSLSPSDVLLALLLALLISLLASLYPARRAARLDPVEALRGE 283
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-224 |
1.52e-37 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 139.83 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSG-EYKVAGQcvaDMESDQL 80
Cdd:COG1119 1 DPLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE---RRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRReHFGF----IFQRYHlmAHLTAEqNVEIPAIYA-----GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQ 151
Cdd:COG1119 74 WELRK-RIGLvspaLQLRFP--RDETVL-DVVLSGFFDsiglyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 152 RVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVII-VTHD-----PLIaqqaDRIIEIKDGQIISD 224
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHHveeipPGI----THVLLLKDGRVVAA 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-221 |
2.35e-37 |
|
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: 138.16 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesdqLAALR 84
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD-----LPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REhFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03301 72 RD-IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQI 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-222 |
3.05e-37 |
|
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: 138.02 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAAlr 84
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY---SIRTDRKAA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-224 |
3.31e-37 |
|
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: 138.11 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNgeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGqcvadMESDQL-AAL 83
Cdd:cd03245 3 IEFRNVSFSYPN--QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG-----TDIRQLdPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGFIFQRYHLMAHlTAEQNVEIPAIYAgksTEQRKERA--RALLTRL------GLAERIHYRPSQLSGGQQQRVSI 155
Cdd:cd03245 76 LRRNIGYVPQDVTLFYG-TLRDNITLGAPLA---DDERILRAaeLAGVTDFvnkhpnGLDLQIGERGRGLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-221 |
3.53e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 139.43 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYkVAGqcvadmeSDQLAALR 84
Cdd:PRK11247 13 LLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-------TAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 rEHFGFIFQRYHLMAHLTAEQNVEIpaiyaGKSTEQRkERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:PRK11247 81 -EDTRLMFQDARLLPWKKVIDNVGL-----GLKGQWR-DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIA-QQADRIIEIKDGQI 221
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-222 |
5.60e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.69 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalr 84
Cdd:COG1132 340 IEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMaHLTAEQNVeipAIYAGKSTEQRKERAralLTRLGLAERIHYRP-----------SQLSGGQQQRV 153
Cdd:COG1132 413 RRQIGVVPQDTFLF-SGTIRENI---RYGRPDATDEEVEEA---AKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRI 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-222 |
7.42e-37 |
|
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: 136.58 E-value: 7.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDqlaalr 84
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKsteqRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHdpL---IAQQADRIIEIKDGQII 222
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH--LlseIQKVADRIGIINKGKLI 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-222 |
1.06e-36 |
|
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: 140.62 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 26 QISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQ-LAALRReHFGFIFQRYHLMAHLTAE 104
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIfLPPHRR-RIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 105 QNVEipaiYAGK--STEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKE 182
Cdd:COG4148 96 GNLL----YGRKraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490367952 183 VMAILKQLNQQGHT-VIIVTHDPL-IAQQADRIIEIKDGQII 222
Cdd:COG4148 172 ILPYLERLRDELDIpILYVSHSLDeVARLADHVVLLEQGRVV 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-224 |
1.46e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 137.60 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSrlYTNGeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNIL-GCLdKPSSGEYKVAGQCVADMESDQLA 81
Cdd:PRK13548 1 AMLEARNLS--VRLG--GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALR---REHF--GFIFqryhlmahlTAEQNVEIPAIYAGKSTEQRKERARALLTR---LGLAERiHYRpsQLSGGQQQRV 153
Cdd:PRK13548 76 RRRavlPQHSslSFPF---------TVEEVVAMGRAPHGLSRAEDDALVAAALAQvdlAHLAGR-DYP--QLSGGEQQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 154 SIARALM------NGGEVILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISD 224
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDlNLAARYADRIVLLHQGRLVAD 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-222 |
2.73e-36 |
|
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: 136.21 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtnGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMEsdqLAALR 84
Cdd:cd03251 1 VEFKNVTFRY--PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMaHLTAEQNVEipaiYA--GKSTEQRKERARA-----LLTRL--GLAERIHYRPSQLSGGQQQRVSI 155
Cdd:cd03251 76 R-QIGLVSQDVFLF-NDTVAENIA----YGrpGATREEVEEAARAanaheFIMELpeGYDTVIGERGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-222 |
5.27e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 136.88 E-value: 5.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSalLELNNVSRLYTNGEE-DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAG-QCVADMESD 78
Cdd:PRK13641 1 MS--IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyHITPETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 QLAALRREhFGFIFQ--RYHLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAER-IHYRPSQLSGGQQQRVSI 155
Cdd:PRK13641 79 NLKKLRKK-VSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLI 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-228 |
5.30e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 137.52 E-value: 5.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEY----------KVAGQCVADMESDQLAALR-------- 84
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKLVIQKTRfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 --REHFGFIFQ--RYHLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARAL 159
Cdd:PRK13651 102 eiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRsPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISDNNNH 228
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-216 |
1.26e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 133.38 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSrLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDKP--SSGEYKVAGQcvadmESDQLA 81
Cdd:COG4136 2 LSLENLT-ITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGR-----RLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALRReHFGFIFQRYHLMAHLTAEQNVEIpAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:COG4136 73 AEQR-RIGILFQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMA-ILKQLNQQGHTVIIVTHDPLIAQQADRIIEI 216
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-222 |
1.99e-35 |
|
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: 133.26 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmESDQLaalrREHFGFIFQRYHLMA 99
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREV----RRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 100 HLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQS 179
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490367952 180 GKEVMAILKQLNQ-QGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:cd03265 167 RAHVWEYIEKLKEeFGMTILLTTHYMEEAEQlCDRVAIIDHGRII 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-222 |
3.94e-35 |
|
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: 132.00 E-value: 3.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 10 VSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGqcvadmeSDQLAALRREHFG 89
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-------KPIKAKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 90 FIFQ--RYHLMahltaEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVIL 167
Cdd:cd03226 75 YVMQdvDYQLF-----TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 168 ADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQII 222
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYeFLAKVCDRVLLLANGAIV 205
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-222 |
7.40e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 133.04 E-value: 7.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTN-----GEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADM 75
Cdd:COG4167 1 MSALLEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 76 ESDQlaalRREHFGFIFQ--RYHLMAHLTAEQNVEIPAIYAGK-STEQRKERARALLTRLGL-AERIHYRPSQLSGGQQQ 151
Cdd:COG4167 81 DYKY----RCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDlTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 152 RVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHDP-LIAQQADRIIEIKDGQII 222
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEkLGISYIYVSQHLgIVKHISDKVLVMHQGEVV 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-221 |
8.83e-35 |
|
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: 131.14 E-value: 8.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 28 SLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmesdQLAALRREhFGFIFQRYHLMAHLTAEQNV 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT-----GLAPYQRP-VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 108 EIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAIL 187
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 490367952 188 KQL-NQQGHTVIIVTHDPL-IAQQADRIIEIKDGQI 221
Cdd:TIGR01277 172 KQLcSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-219 |
1.16e-34 |
|
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: 131.43 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAalrrehfgfIFQRYHLMAHLTA 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 EQNV--EIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGK 181
Cdd:TIGR01184 72 RENIalAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490367952 182 EVMAILKQLNQQGH-TVIIVTHDPLIAQ-QADRIIEIKDG 219
Cdd:TIGR01184 152 NLQEELMQIWEEHRvTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-222 |
1.25e-34 |
|
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: 131.26 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYtnGeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGcLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:COG0410 1 MPMLEVENLHAGY--G--GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AAL--------RRehfgfIFqryhlmAHLTAEQNVEIPAiYAGKSTEQRKERARALLT---RLglAERIHYRPSQLSGGQ 149
Cdd:COG0410 76 ARLgigyvpegRR-----IF------PSLTVEENLLLGA-YARRDRAEVRADLERVYElfpRL--KERRRQRAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 150 QQRVSIARALMNGGEVILADEPTgaldsqSG------KEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPS------LGlaplivEEIFEIIRRLNREGVTILLVEQNARFALEiADRAYVLERGRIV 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
1.42e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.45 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEEDTvvLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVadmeSDQL 80
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYA--LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL----SEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQRY-HLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARAL 159
Cdd:PRK13635 76 VWDVRRQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHDPLIAQQADRIIEIKDGQIIS 223
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-222 |
6.74e-34 |
|
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: 128.71 E-value: 6.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGcLDKPSSGEYKVAGQCVADMESDQLAal 83
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMG-LLPPRSGSIRFDGRDITGLPPHERA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rREHFGFIFQRYHLMAHLTAEQNVEIpAIYAGKSTEQRKERAR--ALLTRlgLAERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:cd03224 74 -RAGIGYVPEGRRIFPELTVEENLLL-GAYARRRAKRKARLERvyELFPR--LKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNaRFALEIADRAYVLERGRVV 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-203 |
8.44e-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: 8.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRReHFGFIFQ--------Ry 95
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRR-RMQMVFQdpyaslnpR- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 96 hlmahLTAEQNVEIPAIYAG-KSTEQRKERARALLTRLGLAERiHYR--PSQLSGGQQQRVSIARALMNGGEVILADEPT 172
Cdd:COG4608 112 -----MTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPE-HADryPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 490367952 173 GALD----SQsgkeVMAILKQLNQQ-GHTVIIVTHD 203
Cdd:COG4608 186 SALDvsiqAQ----VLNLLEDLQDElGLTYLFISHD 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-222 |
8.77e-34 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 128.99 E-value: 8.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEedtvvLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDqlaalr 84
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPL-IAQQADRIIEIKDGQII 222
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEeAWALADKVAIMLNGKLI 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-224 |
1.08e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.15 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmeSDQL 80
Cdd:COG1129 1 AEPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF--RSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRRehfG--FIFQRYHLMAHLTAEQNveipaIYAGKstEQRK----------ERARALLTRLGLAERIHYRPSQLSGG 148
Cdd:COG1129 75 DAQAA---GiaIIHQELNLVPNLSVAEN-----IFLGR--EPRRgglidwramrRRARELLARLGLDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 149 QQQRVSIARALMNGGEVILADEPTGALdsqSGKEV---MAILKQLNQQGHTVIIVTHDpL--IAQQADRIIEIKDGQIIS 223
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASL---TEREVerlFRIIRRLKAQGVAIIYISHR-LdeVFEIADRVTVLRDGRLVG 220
|
.
gi 490367952 224 D 224
Cdd:COG1129 221 T 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-222 |
1.18e-33 |
|
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: 127.69 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGeedtVVLDQISLTINAGeMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVadmeSDQLAALR 84
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03264 72 R-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNqQGHTVIIVTH---DplIAQQADRIIEIKDGQII 222
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHiveD--VESLCNQVAVLNKGKLV 208
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-222 |
1.30e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 129.05 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAA--- 82
Cdd:COG4604 3 EIKNVSKRYG----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 -LRrehfgfifQRYHLMAHLTAEQNVEI---PaiYA-GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIAR 157
Cdd:COG4604 79 iLR--------QENHINSRLTVRELVAFgrfP--YSkGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 158 ALMNGGEVILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHDplI---AQQADRIIEIKDGQII 222
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHD--InfaSCYADHIVAMKDGRVV 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-222 |
2.39e-33 |
|
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: 125.23 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmesdqlaalr 84
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 rehfgfifqryhlmahltaeqnveipaiyagksteqRKERARALltRLGLAeRIHyrpsQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03216 66 ------------------------------------FASPRDAR--RAGIA-MVY----QLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-203 |
3.60e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 127.89 E-value: 3.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYtNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlaal 83
Cdd:PRK11248 1 MLQISHLYADY-GGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rrehfGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHD 203
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQeTGKQVLLITHD 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
3.83e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 128.27 E-value: 3.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAl 83
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rREHFGFIFQRY--HLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:PRK13639 77 -RKTVGIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIIS 223
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvDLVPVYADKVYVMSDGKIIK 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
5-224 |
3.84e-33 |
|
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: 135.38 E-value: 3.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNgeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGqcvadMESDQL--AA 82
Cdd:TIGR03375 464 IEFRNVSFAYPG--QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG-----VDIRQIdpAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 LRReHFGFIFQrYHLMAHLTAEQNVEIPAIYAgksTEQRKERA--RALLTRL------GLAERIHYRPSQLSGGQQQRVS 154
Cdd:TIGR03375 537 LRR-NIGYVPQ-DPRLFYGTLRDNIALGAPYA---DDEEILRAaeLAGVTEFvrrhpdGLDMQIGERGRSLSGGQRQAVA 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-224 |
1.23e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 126.74 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNG-EEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlaal 83
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGFIFQRyHLM---AHLTAEQNVEIpAIYAGKS-------TEQRKERARALLTRL--GLAERIHYRPSQLSGGQQQ 151
Cdd:COG1101 78 RAKYIGRVFQD-PMMgtaPSMTIEENLAL-AYRRGKRrglrrglTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 152 RVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHDpliAQQA----DRIIEIKDGQIISD 224
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHN---MEQAldygNRLIMMHEGRIILD 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-221 |
1.33e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 129.08 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 27 ISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRREHFGFIFQRYHLMAHLTAEQN 106
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 107 VEipaiYAGKST--EQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVM 184
Cdd:TIGR02142 96 LR----YGMKRArpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 490367952 185 AILKQLNQQ-GHTVIIVTHDPL-IAQQADRIIEIKDGQI 221
Cdd:TIGR02142 172 PYLERLHAEfGIPILYVSHSLQeVLRLADRVVVLEDGRV 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-221 |
3.22e-32 |
|
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: 122.71 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEdtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalr 84
Cdd:cd03246 1 LEVENVSFRYPGAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFifqryhLMahltaeQNVEipaIYAGKsteqrkeraralltrlgLAERIhyrpsqLSGGQQQRVSIARALMNGGE 164
Cdd:cd03246 75 GDHVGY------LP------QDDE---LFSGS-----------------IAENI------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-222 |
3.38e-32 |
|
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: 130.96 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYT-------NGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTL-MNILGCLdkPSSGEYKVAGQCVADM 75
Cdd:COG4172 275 LLEARDLKVWFPikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 76 ESDQLAALRReHFGFIFQ--------RyhlmahLTAEQNVEIP-AIYA-GKSTEQRKERARALLTRLGLAERIHYR-PSQ 144
Cdd:COG4172 353 SRRALRPLRR-RMQVVFQdpfgslspR------MTVGQIIAEGlRVHGpGLSAAERRARVAEALEEVGLDPAARHRyPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 145 LSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDlAVVRALAHRVMVMKDGKVV 505
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-230 |
4.03e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 131.49 E-value: 4.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGEEDtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLa 81
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 alrREHFGFIFQRYHLMAHlTAEQNVeipAIYAGKSTEqrkERARALLTRLGLAERIHYRPS----------QLSGGQQQ 151
Cdd:PRK11160 413 ---RQAISVVSQRVHLFSA-TLRDNL---LLAAPNASD---EALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 152 RVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQIIsDNNNHHS 230
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQFDRICVMDNGQII-EQGTHQE 559
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-224 |
4.11e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.59 E-value: 4.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEEDT--VVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESd 78
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 qLAALRREHfGFIFQR--YHLMAHLTAE------QNVEIPAiyagkstEQRKERARALLTRLGLAERIHYRPSQLSGGQQ 150
Cdd:PRK13633 80 -LWDIRNKA-GMVFQNpdNQIVATIVEEdvafgpENLGIPP-------EEIRERVDESLKKVGMYEYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 151 QRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-222 |
8.54e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.13 E-value: 8.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 27 ISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVaGQCV--ADMESDQLAALRReHFGFIFQ-RYHLMAHLTA 103
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNKKLKPLRK-KVGIVFQfPEHQLFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 EQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKE 182
Cdd:PRK13634 104 EKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490367952 183 VMAILKQLNQ-QGHTVIIVTH---DplIAQQADRIIEIKDGQII 222
Cdd:PRK13634 184 MMEMFYKLHKeKGLTTVLVTHsmeD--AARYADQIVVMHKGTVF 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-223 |
8.91e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 129.80 E-value: 8.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 7 LNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCvadmesdQLAALRRE 86
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 87 HFGF------------------IFQRYHLMAHLTAEQNVEIPAIyaGKSTEQRKE--------RARALLTRLGLAERIHY 140
Cdd:COG0488 70 PPLDddltvldtvldgdaelraLEAELEELEAKLAEPDEDLERL--AELQEEFEAlggweaeaRAEEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 141 RP-SQLSGGQQQRVSIARALMNGGEVILADEPTGALDsqsgkeVMAIL---KQLNQQGHTVIIVTHD-PLIAQQADRIIE 215
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIEwleEFLKNYPGTVLVVSHDrYFLDRVATRILE 221
|
....*...
gi 490367952 216 IKDGQIIS 223
Cdd:COG0488 222 LDRGKLTL 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-224 |
1.87e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 123.26 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNG-----EEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESD 78
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 QLAALRREhFGFIFQ--------RYHL-------MAHLTaeqnveipaiyaGKSTEQRKERARALLTRLGLAERI-HYRP 142
Cdd:PRK10419 83 QRKAFRRD-IQMVFQdsisavnpRKTVreiirepLRHLL------------SLDKAERLARASEMLRAVDLDDSVlDKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 143 SQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTV-IIVTHD-PLIAQQADRIIEIKDGQ 220
Cdd:PRK10419 150 PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDlRLVERFCQRVMVMDNGQ 229
|
....
gi 490367952 221 IISD 224
Cdd:PRK10419 230 IVET 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-222 |
2.28e-31 |
|
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: 120.73 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMNIL-GCLDKPS-SGEYKVAGQcvaDMESDQLaalrREHFGFIFQRYHLMAH 100
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGR---PLDKRSF----RKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 LTAEQNVEipaiYAgksteqrkerarALLtrlglaerihyrpSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSG 180
Cdd:cd03213 97 LTVRETLM----FA------------AKL-------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490367952 181 KEVMAILKQLNQQGHTVIIVTHDP--LIAQQADRIIEIKDGQII 222
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQPssEIFELFDKLLLLSQGRVI 191
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-203 |
2.43e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 126.10 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYtNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQl 80
Cdd:PRK11607 16 LTPLLEIRNLTKSF-DGQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aalrrEHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:PRK11607 91 -----RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490367952 161 NGGEVILADEPTGALDSQSGK----EVMAILKQLnqqGHTVIIVTHD 203
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHD 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-226 |
3.36e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 123.35 E-value: 3.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEE-DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGFIFQ--RYHLMahltaEQNVEIPAIYAGKS----TEQRKERARALLTRLGLAERI-HYRPSQLSGGQQQRVSIA 156
Cdd:PRK13646 83 VRKRIGMVFQfpESQLF-----EDTVEREIIFGPKNfkmnLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQLN-QQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISDNN 226
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQTS 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-214 |
3.57e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.03 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 17 GEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmesdqlaalrrehfGFIFQRYH 96
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV---------------AYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 97 LMAHL--TAEQNVEI----PAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADE 170
Cdd:NF040873 66 VPDSLplTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490367952 171 PTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRII 214
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-222 |
3.73e-31 |
|
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: 119.73 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSrlYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMEsdqlaALR 84
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-----KAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMahltaeqnveipaiyagksteqrkerARALLTRLGLaerihyrpsQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03247 74 SSLISVLNQRPYLF--------------------------DTTLRNNLGR---------RFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 165 VILADEPTGALDSQSGKEVMA-ILKQLnqQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSlIFEVL--KDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
7.22e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.77 E-value: 7.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aalrREHFGFIFQRY--HLMAhLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARA 158
Cdd:PRK13647 78 ----RSKVGLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIIS 223
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGRVLA 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-224 |
1.30e-30 |
|
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: 119.39 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGqcvADMESDQLAAL 83
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RRehFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:cd03266 78 RR--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHdplIAQQA----DRIIEIKDGQIISD 224
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTH---IMQEVerlcDRVVVLHRGRVVYE 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-228 |
1.83e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 125.97 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKS-TLMNILGCLDKPS----SGEYKVAGQCVADME 76
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 77 SDQLAALRREHFGFIFQRyhLMA-----HLTAEQNVEIPAIYAGksteQRKERARA----LLTRLGL---AERIHYRPSQ 144
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQE--PMVslnplHTLEKQLYEVLSLHRG----MRREAARGeilnCLDRVGIrqaAKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 145 LSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
....*.
gi 490367952 223 SDNNNH 228
Cdd:PRK15134 237 EQNRAA 242
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-222 |
3.09e-30 |
|
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: 125.60 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYtnGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMesdQLAAL 83
Cdd:TIGR02203 330 DVEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RReHFGFIFQRYHLMAHLTAEqNVEIPAIYAGKSTEQRKERARALLTR------LGLAERIHYRPSQLSGGQQQRVSIAR 157
Cdd:TIGR02203 405 RR-QVALVSQDVVLFNDTIAN-NIAYGRTEQADRAEIERALAAAYAQDfvdklpLGLDTPIGENGVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 158 ALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-213 |
3.68e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.37 E-value: 3.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTL------MN--ILGCLdkpSSGEYKVAGQCV 72
Cdd:COG1117 8 LEPKIEVRNLNVYYG----DKQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNdlIPGAR---VEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 73 ADMESDqLAALRReHFGFIFQR--------YhlmahltaeQNVEIPAIYAG-KSTEQRKERARALLTRLGL----AERIH 139
Cdd:COG1117 81 YDPDVD-VVELRR-RVGMVFQKpnpfpksiY---------DNVAYGLRLHGiKSKSELDEIVEESLRKAALwdevKDRLK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 140 YRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDPliaQQADRI 213
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNM---QQAARV 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
4.69e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 4.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGEedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLa 81
Cdd:PRK13632 5 SVMIKVENVSFSYPNSE--NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 alrREHFGFIFQRY-HLMAHLTAE-------QNVEIPaiyagksTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRV 153
Cdd:PRK13632 82 ---RKKIGIIFQNPdNQFIGATVEddiafglENKKVP-------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-213 |
5.51e-30 |
|
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: 118.55 E-value: 5.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGeYKVAGQCVADMES--DQ-- 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKE----ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPG-VRIEGKVLFDGQDiyDKki 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 80 -LAALRReHFGFIFQRYHLMAhLTAEQNVEI-PAIYAGKSTEQRKERARALLTRLGLAE----RIHYRPSQLSGGQQQRV 153
Cdd:TIGR00972 76 dVVELRR-RVGMVFQKPNPFP-MSIYDNIAYgPRLHGIKDKKELDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDpliAQQADRI 213
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHN---MQQAARI 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-224 |
5.64e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.15 E-value: 5.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNgeedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlaal 83
Cdd:PRK10771 1 MLKLTDITWLYHH------LPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rrEHFGFIFQRYHLMAHLTAEQNVEI---PAIyagKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:PRK10771 71 --RPVSMLFQENNLFSHLTVAQNIGLglnPGL---KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTH---DPliAQQADRIIEIKDGQIISD 224
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHsleDA--ARIAPRSLVVADGRIAWD 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-229 |
2.61e-29 |
|
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: 116.17 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalrR 85
Cdd:cd03254 4 EFENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 EHFGFIFQRYHL----------MAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGlaERIHYrpsqLSGGQQQRVSI 155
Cdd:cd03254 77 SMIGVVLQDTFLfsgtimenirLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLG--ENGGN----LSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNqQGHTVIIVTHDPLIAQQADRIIEIKDGQIISDNNNHH 229
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-224 |
2.89e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.65 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAalr 84
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 rEHFGFIFQRyhlmaHLTAEqNVEIPAIYA-GKS------------TEQRKERARALLTRLGLAERihyRPSQLSGGQQQ 151
Cdd:PRK11231 76 -RRLALLPQH-----HLTPE-GITVRELVAyGRSpwlslwgrlsaeDNARVNQAMEQTRINHLADR---RLTDLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 152 RVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDpliAQQA----DRIIEIKDGQIISD 224
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD---LNQAsrycDHLVVLANGHVMAQ 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-222 |
4.10e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.67 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVaDMESDQl 80
Cdd:COG3845 2 MPPALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRReHFGFIFQRYHLMAHLTAEQNVEI---PAIYAGKSTEQRKERARALLTRLGLA----ERIHyrpsQLSGGQQQRV 153
Cdd:COG3845 76 DAIAL-GIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDvdpdAKVE----DLSVGEQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDpL--IAQQADRIIEIKDGQII 222
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHK-LreVMAIADRVTVLRRGKVV 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-222 |
4.27e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 122.26 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLdkPSSGEYKVAGQCVADMESDQLaalrREHFGFIFQRYHL 97
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELDPESW----RKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 MaHLTAEQNVEIPAIYAGKST-EQRKERARAL----LTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPT 172
Cdd:PRK11174 435 P-HGTLRDNVLLGNPDASDEQlQQALENAWVSeflpLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490367952 173 GALDSQSGKEVMAILKQlNQQGHTVIIVTH--DPLiaQQADRIIEIKDGQII 222
Cdd:PRK11174 514 ASLDAHSEQLVMQALNA-ASRRQTTLMVTHqlEDL--AQWDQIWVMQDGQIV 562
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-203 |
5.39e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 117.76 E-value: 5.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYT-----NGEEDTV-VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAD 74
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrglFKPERLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 75 MESDQLAALRREhFGFIFQR-Y-HLMAHLTAEQNVEIP-AIYAGKSTEQRKERARALLTRLGL-AEriHYR--PSQLSGG 148
Cdd:PRK11308 82 ADPEAQKLLRQK-IQIVFQNpYgSLNPRKKVGQILEEPlLINTSLSAAERREKALAMMAKVGLrPE--HYDryPHMFSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 149 QQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHT--VIIvTHD 203
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFI-SHD 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-222 |
7.34e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 118.28 E-value: 7.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesdqlAALR 84
Cdd:PRK11432 7 VVLKNITKRFGS----NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKER---ARALLTRLGLAERIhyrPSQLSGGQQQRVSIARALMN 161
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRvkeALELVDLAGFEDRY---VDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIA-QQADRIIEIKDGQII 222
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAfAVSDTVIVMNKGKIM 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-222 |
1.21e-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: 114.25 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:cd03253 1 IEFENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ---DIREVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMaHLTAEQNVEipaiYA--GKSTEQRKERARA-----LLTRL--GLAERIHYRPSQLSGGQQQRVSI 155
Cdd:cd03253 75 R-AIGVVPQDTVLF-NDTIGYNIR----YGrpDATDEEVIEAAKAaqihdKIMRFpdGYDTIVGERGLKLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNqQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-222 |
1.56e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.53 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLElnNVSRLYTNGEE-DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmESDQ 79
Cdd:PRK13637 1 MSIKIE--NLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 80 LAALRREhFGFIFQ--RYHLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLA-ERIHYR-PSQLSGGQQQRVSI 155
Cdd:PRK13637 78 LSDIRKK-VGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKsPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTH---DplIAQQADRIIEIKDGQII 222
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHsmeD--VAKLADRIIVMNKGKCE 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-203 |
2.04e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 112.52 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 18 EEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAalRREHFGFIFQR--Y 95
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLE--RRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 96 HLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGAL 175
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180
....*....|....*....|....*...
gi 490367952 176 DSQSGKEVMAILKQLNQQGHTVIIVTHD 203
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-222 |
3.10e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.46 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGE--EDTVVLDqISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAA 82
Cdd:PRK13649 3 INLQNVSYTYQAGTpfEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 LRREHFGFIFQ--RYHLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARAL 159
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTH---DplIAQQADRIIEIKDGQII 222
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlmdD--VANYADFVYVLEKGKLV 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-222 |
3.90e-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: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLD---KPSSGEYKVAGQcvadmESDqlA 81
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ-----PRK--P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALRREHFGFIFQRYHLMAHLTAEQNVEIPAIYAG---KSTEQRKER-ARALLTRLGLAERIHYRPSQLSGGQQQRVSIAR 157
Cdd:cd03234 77 DQFQKCVAYVRQDDILLPGLTVRETLTYTAILRLprkSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 158 ALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPL--IAQQADRIIEIKDGQII 222
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-222 |
4.59e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.93 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMEsdQLAAL 83
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RReHFGFIFQRYHL-MAHLTAEQNVEI-PAIYAGKSTEQRKERARALlTRLGLAERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:PRK13644 76 RK-LVGIVFQNPETqFVGRTVEEDLAFgPENLCLPPIEIRKRVDRAL-AEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 162 GGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-222 |
5.05e-28 |
|
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: 112.63 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalrREHFGFIFQRYHLMA 99
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 100 HLTAEQnveipaIYAGKSTEQRKERARA--------LLTRL--GLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILAD 169
Cdd:cd03249 91 GTIAEN------IRYGKPDATDEEVEEAakkanihdFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490367952 170 EPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:cd03249 165 EATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-222 |
5.79e-28 |
|
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: 111.60 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvadmesdQLAALR 84
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK--------PLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-221 |
9.19e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 115.13 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 7 LNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlaalrRE 86
Cdd:PRK11000 6 LRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 87 hFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVI 166
Cdd:PRK11000 77 -VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 167 LADEPTGALDS----QSGKEVMAILKQLnqqGHTVIIVTHDPLIAQQ-ADRIIEIKDGQI 221
Cdd:PRK11000 156 LLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTlADKIVVLDAGRV 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-204 |
1.10e-27 |
|
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: 117.46 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTL-MNILGCLDkPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLlATLAGLLD-PLQGEVTLDGVPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rrehFGFIFQRYHLMAHlTAEQNVeipAIYAGKSTEqrkERARALLTRLGLAERIHYRP-----------SQLSGGQQQR 152
Cdd:TIGR02868 411 ----VSVCAQDAHLFDT-TVRENL---RLARPDATD---EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490367952 153 VSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNqQGHTVIIVTHDP 204
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHHL 530
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-222 |
2.18e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 111.56 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGeedtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGE--YKVAG---QCVADM 75
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMRDgqlRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 76 ESDQLAALRREHFGFIFQ--RYHLMAHLTAEQNVEIPAIYAGksteQR---KERARAL--LTRLGL-AERIHYRPSQLSG 147
Cdd:PRK11701 79 SEAERRRLLRTEWGFVHQhpRDGLRMQVSAGGNIGERLMAVG----ARhygDIRATAGdwLERVEIdAARIDDLPTTFSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 148 GQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVV 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-222 |
2.23e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.75 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 28 SLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRREHFGFIFQRYHLMAHLTAEQNV 107
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 108 EIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAIL 187
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190
....*....|....*....|....*....|....*..
gi 490367952 188 KQLN-QQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:PRK10070 208 VKLQaKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
355-644 |
2.42e-27 |
|
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: 118.00 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 355 SRLRRGNQDAPATVSGVNEDYFSVYALKFAQGSTFTPDMIHRQAQVVVIDENTRHRFFPNKQAvIGEQIIIRNIPS---T 431
Cdd:TIGR03434 516 RPPPPPGEEPLADYRRVSPGYFETMGIPLLRGRDFTERDTAGSPPVAIVNEAFARRYFPGEDP-IGKRIRLGGDDGpwfE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 432 IIGVVAEQKST-FGDNKSLRVWVPYStlssriynRSYLDNITVKVKEGYDASVAEQQILRllTIRHGKKDIFTYNIDSFI 510
Cdd:TIGR03434 595 IVGVVGDVRYAgLDEPPRPEVYLPYA--------QSPDRGMTLVVRTAGDPAALAAAVRR--AVRAIDPNLPVYDVRTME 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 511 KAAEKTTQTMQLFLTLV---AVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVMQQFLIESVLVCLVGGLLGI 587
Cdd:TIGR03434 665 EQVDRSLAQERFLALLLglfAALALLLAAIGLYGVLAYSVAQRTREIGIRMALGAQRGDVLRLVLRQGLRLAAAGLAIGL 744
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 588 SLSFAIAMFASMMLpnwhF---VFQPTALISAFACSTAIGVIFGFLPARNAAKMNPIDAL 644
Cdd:TIGR03434 745 AAALALARLLASLL----FgvsPTDPLTFAAVAALLLAVALLACYLPARRAARVDPMIAL 800
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-221 |
3.75e-27 |
|
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: 115.91 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEDTvvLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAalr 84
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 rEHFGFIFQRYHLMAHLTAE------QNVEIPAIYAGKSTEQRKEraraLLTRL--GLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:TIGR01842 392 -KHIGYLPQDVELFPGTVAEniarfgENADPEKIIEAAKLAGVHE----LILRLpdGYDTVIGPGGATLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-226 |
5.69e-27 |
|
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: 109.55 E-value: 5.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALr 84
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 reHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03218 76 --GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTH---DPLiaQQADRIIEIKDGQIISDNN 226
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHnvrETL--SITDRAYIIYEGKVLAEGT 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
6.22e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.87 E-value: 6.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLY-TNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKV----AGQCVADMESD 78
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 QLAALR--------REHFGFIFQ--RYHLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYR-PSQLSG 147
Cdd:PRK13631 101 TNPYSKkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERsPFGLSG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 148 GQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHdpliaqQADRIIEIKDGQIISD 224
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITH------TMEHVLEVADEVIVMD 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-221 |
8.62e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 112.24 E-value: 8.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADME-SDQLA 81
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEpADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALrrehfgfIFQRYHLMAHLTAEQNVEipaiY----AGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIAR 157
Cdd:PRK11650 79 AM-------VFQNYALYPHMSVRENMA----YglkiRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 158 ALMNGGEVILADEPTGALDS----QsgkevMAI-LKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQI 221
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAklrvQ-----MRLeIQRLHRRlKTTSLYVTHDQVEAMTlADRVVVMNGGVA 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-213 |
8.76e-27 |
|
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: 107.83 E-value: 8.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 21 TVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvadmESDQLAALRREHFGFIFQRYHLMAH 100
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-----PLAEQRDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 LTAEQNVEIPAIYAGksTEQRKerARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSG 180
Cdd:TIGR01189 88 LSALENLHFWAAIHG--GAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|...
gi 490367952 181 KEVMAILKQLNQQGHTVIIVTHDPLIAQQADRI 213
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQDLGLVEAREL 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-232 |
9.05e-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: 9.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSgeyKVAGQCVAD---MESDQLaalrREHFGFIFQRYHLMAH 100
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV---KGSGSVLLNgmpIDAKEM----RAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 LTAEQNVEIPA---IYAGKSTEQRKERARALLTRLGLAERIHYR---PSQ---LSGGQQQRVSIARALMNGGEVILADEP 171
Cdd:TIGR00955 114 LTVREHLMFQAhlrMPRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 172 TGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPL--IAQQADRIIEIKDGQIISDNNNHHSVP 232
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
9.26e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 109.20 E-value: 9.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMesdQL 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQ----ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKST-EQRKERARALLTRLglAERIHYRPSQLSGGQQQRVSIARAL 159
Cdd:PRK11614 75 AKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIA-QQADRIIEIKDGQII 222
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQAlKLADRGYVLENGHVV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-224 |
9.51e-27 |
|
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: 108.96 E-value: 9.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALRRehFGFIF-QRYHL 97
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPWKRRKKFLRR--IGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 MAHLTAEQNVE-IPAIYaGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALD 176
Cdd:cd03267 107 WWDLPVIDSFYlLAAIY-DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490367952 177 SQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQIISD 224
Cdd:cd03267 186 VVAQENIRNFLKEYNRErGTTVLLTSHYmKDIEALARRVLVIDKGRLLYD 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
1.35e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.20 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLM-NILGCLDkPSSGEYKVAGQcvadmesdQLAAL 83
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGILA-PDSGEVLWDGE--------PLDPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGF------IFQRYHLMAHLtaeqnveipaIY----AGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRV 153
Cdd:COG4152 69 DRRRIGYlpeergLYPKMKVGEQL----------VYlarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVEELCDRIVIINKGRKV 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-224 |
1.40e-26 |
|
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: 108.00 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMEsdqLAAlrrehfGFifqryhlMAHLT 102
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG---LGG------GF-------NPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 103 AEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKE 182
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490367952 183 VMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQIISD 224
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPsSIKRLCDRALVLEKGKIRFD 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
2.01e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.07 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTvvLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaal 83
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rREHFGFIFQ-----------RYHLMAHLtaeQNVEIPaiyagksTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQR 152
Cdd:PRK13648 82 -RKHIGIVFQnpdnqfvgsivKYDVAFGL---ENHAVP-------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 153 VSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-222 |
5.75e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 109.06 E-value: 5.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKS-TLMNILGCLDKP---SSGEYKVAGQCVADMESD 78
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 QLAALRREHFGFIFQryHLMAHLT-----AEQNVEIPAIYAGKSTEQRKERARALLTRLGL---AERIHYRPSQLSGGQQ 150
Cdd:PRK11022 82 ERRNLVGAEVAMIFQ--DPMTSLNpcytvGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 151 QRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDlALVAEAAHKIIVMYAGQVV 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-221 |
6.28e-26 |
|
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: 112.53 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSrlYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNIL-GCLdKPSSGEYKVAGQCVADMESDQLAal 83
Cdd:COG4618 331 LSVENLT--VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELG-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rrEHFGFIFQRYHLMAHlTAEQNVeipAIYAGKSTEQRKERARA-----LLTRL--GLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:COG4618 406 --RHIGYLPQDVELFDG-TIAENI---ARFGDADPEKVVAAAKLagvheMILRLpdGYDTRIGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-220 |
9.27e-26 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 103.30 E-value: 9.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAgqcvadmesdqlaalr 84
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 rehfgfifqryhlmahltaeQNVEIPaiyagksteqrkeraralltrlglaeriHYrpSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03221 61 --------------------STVKIG----------------------------YF--EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 165 VILADEPTGALDSQSgkeVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQ 220
Cdd:cd03221 91 LLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHDRyFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-222 |
1.03e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVaGQCVadmesdqlaal 83
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rreHFGFIFQRyhlMAHLTAEQNVeIPAIYAGKSTEQRKErARALLTRLGLA-ERIHYRPSQLSGGQQQRVSIARALMNG 162
Cdd:COG0488 379 ---KIGYFDQH---QEELDPDKTV-LDELRDGAPGGTEQE-VRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 163 GEVILADEPTGALDSQSgKEVMAILkqLNQ-QGhTVIIVTHDP-LIAQQADRIIEIKDGQII 222
Cdd:COG0488 451 PNVLLLDEPTNHLDIET-LEALEEA--LDDfPG-TVLLVSHDRyFLDRVATRILEFEDGGVR 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-226 |
1.06e-25 |
|
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: 111.43 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLD--KPSSGE--YKVA------------ 68
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRiiYHVAlcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 69 --GQ----CVADME---------SDQLAALRREHFGFIFQR-YHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRL 132
Cdd:TIGR03269 77 kvGEpcpvCGGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 133 GLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVM-AILKQLNQQGHTVIIVTHDP-LIAQQA 210
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHWPeVIEDLS 236
|
250
....*....|....*.
gi 490367952 211 DRIIEIKDGQIISDNN 226
Cdd:TIGR03269 237 DKAIWLENGEIKEEGT 252
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-222 |
1.59e-25 |
|
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: 106.07 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYTNGeedtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAA 82
Cdd:TIGR02323 2 PLLQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 -----LRREHFGFIFQ--RYHLMAHLTAEQNV-EIPAIYAGKSTEQRKERARALLTRLGL-AERIHYRPSQLSGGQQQRV 153
Cdd:TIGR02323 78 aerrrLMRTEWGFVHQnpRDGLRMRVSAGANIgERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHDPLIAQ-QADRIIEIKDGQII 222
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGlAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-214 |
2.16e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.80 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSrlYTNGeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLa 81
Cdd:PRK10247 5 SPLLQLQNVG--YLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 alrREHFGFIFQRYHLMAHlTAEQNVEIPAIYAGKSTEQRKerARALLTRLGLAERIHYRP-SQLSGGQQQRVSIARALM 160
Cdd:PRK10247 80 ---RQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAI--FLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLN-QQGHTVIIVTHDPLIAQQADRII 214
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEINHADKVI 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
2.30e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYtNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQL 80
Cdd:PRK13650 1 MSNIIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRReHFGFIFQRY-HLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARAL 159
Cdd:PRK13650 77 WDIRH-KIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQADRIIEIKDGQIIS 223
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-222 |
2.50e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 110.00 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMES-DQ 79
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 80 LAAlrreHFGFIFQRYHLMAHLTAEQNV---EIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:PRK11288 77 LAA----GVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTH--DPlIAQQADRIIEIKDGQII 222
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHrmEE-IFALCDAITVFKDGRYV 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-224 |
2.60e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.10 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNIL-GCLdKPSSGEYKVAGQCvadmESDQLAALRReHFGFIF-QRYHLMAHL 101
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEVRVLGYV----PFKRRKEFAR-RIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 102 TAEQNVEI-PAIYaGKSTEQRKERARALLTRLGLAERIHyRP-SQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQS 179
Cdd:COG4586 112 PAIDSFRLlKAIY-RIPDAEYKKRLDELVELLDLGELLD-TPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490367952 180 GKEVMAILKQLNQQ-GHTVIIVTHDpL--IAQQADRIIEIKDGQIISD 224
Cdd:COG4586 190 KEAIREFLKEYNRErGTTILLTSHD-MddIEALCDRVIVIDHGRIIYD 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-221 |
2.73e-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: 103.28 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALRREHFGFIfqryhlmahlt 102
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK---PVTRRSPRDAIRAGIAYV----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 103 aeqnveipaiyagksTEQRKERAraLLTRLGLAERIHYrPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKE 182
Cdd:cd03215 81 ---------------PEDRKREG--LVLDLSVAENIAL-SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490367952 183 VMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:cd03215 143 IYRLIRELADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-224 |
3.19e-25 |
|
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: 104.49 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtnGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:cd03252 1 ITFEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGH---DLALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REhFGFIFQRYHLMAHLTAEQnveIPAIYAGKSTEQRKERARA-------LLTRLGLAERIHYRPSQLSGGQQQRVSIAR 157
Cdd:cd03252 76 RQ-VGVVLQENVLFNRSIRDN---IALADPGMSMERVIEAAKLagahdfiSELPEGYDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 158 ALMNGGEVILADEPTGALDSQSGKEVMAILKQLNqQGHTVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-254 |
3.77e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.13 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 9 NVSRLYTNgEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCV---ADMESDQLAALRR 85
Cdd:PRK14246 12 NISRLYLY-INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 EhFGFIFQRYHLMAHLTAEQNVEIPAIYAG-KSTEQRKERARALLTRLGLAERIHYR----PSQLSGGQQQRVSIARALM 160
Cdd:PRK14246 91 E-VGMVFQQPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDP-LIAQQADRIIEIKDGQIISDNNNHHsvpVKKAPPA 239
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPqQVARVADYVAFLYNGELVEWGSSNE---IFTSPKN 245
|
250
....*....|....*
gi 490367952 240 IQTASYfhqVIGRFT 254
Cdd:PRK14246 246 ELTEKY---VIGRIS 257
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-229 |
4.37e-25 |
|
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: 109.89 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEDTV-VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesDQLAAL 83
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rREHFGFIFQRYHLMAHLTAEQNVEIPaiyagksteqrkERARALLTRLGLAERIHYR-----PSQLSGGQQQRVSIARA 158
Cdd:COG4615 405 -RQLFSAVFSDFHLFDRLLGLDGEADP------------ARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVA 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 159 LMNGGEVILADE------PTgaldsqsGKEV--MAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQIISDNNNHH 229
Cdd:COG4615 472 LLEDRPILVFDEwaadqdPE-------FRRVfyTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAA 543
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
5.97e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVaDMESDQLA 81
Cdd:PRK13636 3 DYILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALRrEHFGFIFQRY-HLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:PRK13636 79 KLR-ESVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDiDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-222 |
7.81e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 109.34 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTngEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:PRK11176 342 IEFRNVTFTYP--GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 rEHFGFIFQRYHLMAHlTAEQNVEIPA--IYAGKSTEQRKERARAL--LTRL--GLAERIHYRPSQLSGGQQQRVSIARA 158
Cdd:PRK11176 417 -NQVALVSQNVHLFND-TIANNIAYARteQYSREQIEEAARMAYAMdfINKMdnGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-213 |
1.36e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.30 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMesdqlAALR 84
Cdd:PRK13536 42 IDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-----ARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHdplIAQQADRI 213
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH---FMEEAERL 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
1.44e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 107.97 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTV-VLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKV-AGQCVADMeSDQLA 81
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDM-TKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALR---REHFGFIFQRYHLMAH------LTAEQNVEIP-------AIYAGKSTEQRKERARALLTRLglaerihyrPSQL 145
Cdd:TIGR03269 358 DGRgraKRYIGILHQEYDLYPHrtvldnLTEAIGLELPdelarmkAVITLKMVGFDEEKAEEILDKY---------PDEL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 146 SGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVM-AILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIV 507
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-205 |
1.62e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 101.42 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNV--SRlytngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESD--- 78
Cdd:PRK13538 1 MLEARNLacER------DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 ------QLAALRREhfgfifqryhlmahLTAEQNVeipAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQR 152
Cdd:PRK13538 75 dllylgHQPGIKTE--------------LTALENL---RFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490367952 153 VSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPL 205
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDL 190
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-221 |
1.83e-24 |
|
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: 102.16 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNgEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaal 83
Cdd:cd03248 11 IVKFQNVTFAYPT-RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rREHFGFIFQRYHLMAHLTAEQnveIPAIYAGKSTEQRKERARA-------LLTRLGLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:cd03248 87 -HSKVSLVGQEPVLFARSLQDN---IAYGLQSCSFECVKEAAQKahahsfiSELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-223 |
2.44e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 102.23 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVS---RLYTngeedtvvldqISLTINAGEMVAIIGASGSGKSTLMNIL-GCLdkPSSGEYKVAGQCVADMESDQL 80
Cdd:COG4138 1 LQLNDVAvagRLGP-----------ISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAEL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRrehfgfifqryhlmAHLTaeQNVEIPAI-----Y------AGKSTEQRKERARALLTRLGLAERIHyRP-SQLSGG 148
Cdd:COG4138 68 ARHR--------------AYLS--QQQSPPFAmpvfqYlalhqpAGASSEAVEQLLAQLAEALGLEDKLS-RPlTQLSGG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 149 QQQRVSIARALMN-------GGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQ 220
Cdd:COG4138 131 EWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGK 210
|
...
gi 490367952 221 IIS 223
Cdd:COG4138 211 LVA 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-220 |
2.89e-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: 101.01 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 15 TNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDKpSSGEYKVAGQC--VAdmesdQLAALR----REH 87
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGSIayVS-----QEPWIQngtiREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 88 --FG--FIFQRYHLMAHLTA-EQNVEIPAiyAGKSTEqrkeraralltrlglaerIHYRPSQLSGGQQQRVSIARALMNG 162
Cdd:cd03250 86 ilFGkpFDEERYEKVIKACAlEPDLEILP--DGDLTE------------------IGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 163 GEVILADEPTGALDSQSGKEVM--AILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQ 220
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFenCILGLL-LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-223 |
5.35e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.39 E-value: 5.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 7 LNNVSRLYTNGEE-DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCV-ADMES-DQLAAL 83
Cdd:PRK13645 9 LDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREhFGFIFQ--RYHLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARALM 160
Cdd:PRK13645 89 RKE-IGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHD-PLIAQQADRIIEIKDGQIIS 223
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNmDQVLRIADEVIVMHEGKVIS 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-228 |
8.91e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 8.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmesdQL 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYG----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-----SR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALM 160
Cdd:PRK13537 75 ARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQ-ADRIIEIKDGQIISDNNNH 228
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPH 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-213 |
1.38e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.30 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCL-----DKPSSGEYKVAGQCVADM 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 76 ESDQLAAlrREHFGFIFQRYHLMAHLTAEQNVEIPAIYAG--KSTEQRKERARALLTRLGLAERIHYR----PSQLSGGQ 149
Cdd:PRK14267 77 DVDPIEV--RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 150 QQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDPliaQQADRI 213
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSP---AQAARV 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-223 |
2.05e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 102.26 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 26 QISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESD-QLAALRReHFGFIFQRYHLMAHLTAE 104
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLPPEKR-RIGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 105 QNVEipaiYAGKstEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVM 184
Cdd:PRK11144 95 GNLR----YGMA--KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490367952 185 AILKQLNQQGHTVII-VTH--DPLIaQQADRIIEIKDGQIIS 223
Cdd:PRK11144 169 PYLERLAREINIPILyVSHslDEIL-RLADRVVVLEQGKVKA 209
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-223 |
2.29e-23 |
|
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: 99.14 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtnGEedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAalr 84
Cdd:TIGR03410 1 LEVSNLNVYY--GQ--SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLglAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHDPLIAQQ-ADRIIEIKDGQIIS 223
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARElADRYYVMERGRVVA 212
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-221 |
2.77e-23 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 104.28 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADmesDQLAALR 84
Cdd:PRK10522 323 LELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHLTAEQNveipaiyagksTEQRKERARALLTRLGLAERIHYRPS-----QLSGGQQQRVSIARAL 159
Cdd:PRK10522 397 K-LFSAVFTDFHLFDQLLGPEG-----------KPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEV-MAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-224 |
2.79e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVS---RLYTNGE---------------EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSS 62
Cdd:COG1134 1 MSSMIEVENVSksyRLYHEPSrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 63 GEYKVAGQCVADMEsdqlaalrrehFGFIFQryhlmAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHyRP 142
Cdd:COG1134 81 GRVEVNGRVSALLE-----------LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID-QP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 143 -SQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQ 220
Cdd:COG1134 144 vKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMgAVRRLCDRAIWLEKGR 223
|
....
gi 490367952 221 IISD 224
Cdd:COG1134 224 LVMD 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-203 |
3.18e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.95 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKS-TLMNILGCLDKPS--SGEYKVAGQCVADMES 77
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 78 DQLAALRREHFGFIFQryHLMAHLT-----AEQNVEIPAIYAGKSTEQRKERARALLTRLGLAE---RIHYRPSQLSGGQ 149
Cdd:PRK09473 89 KELNKLRAEQISMIFQ--DPMTSLNpymrvGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 150 QQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVII-VTHD 203
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHD 221
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
366-644 |
3.51e-23 |
|
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: 104.90 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 366 ATVSGvneDYFSVYALKFAQGSTFTPDMIHRQA-QVVVIDENTRHRFFPNKQAVIGEQIIIRNIPSTIIGVVAEQkstFG 444
Cdd:TIGR03434 113 AFVSA---NFFPVLGVQPALGRLFTPEDDRPGApPVVVLSYALWQRRFGGDPAVVGRTIRLNGRPYTVVGVMPPG---FT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 445 D-NKSLRVWVP---YSTLSSRIYNRSYLDNITVKVKEGYDASVAEQQ---ILRLLTIRHGKKdiftyNIDSFIK----AA 513
Cdd:TIGR03434 187 FpGRDPDVWVPlamDPALAGSANRGSRWLRVIGRLKPGVTLAQAQAEldaIAARLAAAYPDT-----NAGRGLAvtplRE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 514 EKTTQTMQLFLTLVAVISLV--VGGIGVMNIMLVSVTERTREIGIRMAVGARASDVMQQFLIESVLVCLVGGLLGISLSF 591
Cdd:TIGR03434 262 SLVGDVRPPLLVLLGAVGLVllIACANVANLLLARAAARQREIAVRLALGAGRGRLVRQLLTESLLLALAGGALGLLLAY 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 592 -AIAMFASMMLPNWHFVFQ----PTALISAFACSTAIGVIFGFLPARNAAKMNPIDAL 644
Cdd:TIGR03434 342 wGLRLLLALLPASLPRLLEisldGRVLLFALALSLLTGLLFGLAPALQATRSDLAEAL 399
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-220 |
3.71e-23 |
|
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: 97.56 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmesdqlaalrrEHFGFIFQRYHLMAH- 100
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD------------FQRDSIARGLLYLGHa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 ------LTAEQNVEIpaIYAGKSTEQRKERaralLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGA 174
Cdd:cd03231 82 pgikttLSVLENLRF--WHADHSDEQVEEA----LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490367952 175 LDSQSGKEVMAILKQLNQQGHTVIIVTHDPLiAQQADRIIEIKDGQ 220
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQDL-GLSEAGARELDLGF 200
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-224 |
4.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNgEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQL 80
Cdd:PRK13642 1 MNKILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREhFGFIFQRY-HLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARAL 159
Cdd:PRK13642 77 WNLRRK-IGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 160 MNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHDPLIAQQADRIIEIKDGQIISD 224
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-222 |
4.56e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.83 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCL-----DKPSSGEYKVAGQCVADMESDQLaalrREHFGFIFQR 94
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL----RRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 95 YHLMAHLTAEQNVEI-PAI-YAGKSTEQRKERARALLTRLGLAERIHYR----PSQLSGGQQQRVSIARALMNGGEVILA 168
Cdd:PRK14247 91 PNPIPNLSIFENVALgLKLnRLVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 169 DEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDPliaQQADRIIE----IKDGQII 222
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFP---QQAARISDyvafLYKGQIV 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-221 |
5.06e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.21 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmesdQL 80
Cdd:PRK15439 8 APPLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-----RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFG--FIFQRYHLMAHLTAEQNVeipaIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARA 158
Cdd:PRK15439 79 TPAKAHQLGiyLVPQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-223 |
9.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.04 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRREHFGFIFQ--RYHLMAHl 101
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 102 TAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSG 180
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490367952 181 KEVMAILKQLNQQGHTVIIVTH--DPlIAQQADRIIEIKDGQIIS 223
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHlmDD-VADYADYVYLLEKGHIIS 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-224 |
1.81e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.98 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 25 DQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALrrehfGFI--FQRYHLMAHLT 102
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-----GVVrtFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 103 AEQNVEIP-------AIYAG--------KSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVIL 167
Cdd:PRK11300 97 VIENLLVAqhqqlktGLFSGllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 168 ADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISD 224
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDmKLVMGISDRIYVVNQGTPLAN 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-214 |
1.93e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.01 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 25 DQISLTINAGEMVAIIGASGSGKSTLMN-ILGcLDKPSSGEYKVAGQCVADMESDQLAALRREhFGFIFQryHLMAHLTA 103
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQ--DPLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 EQNV-EIPA----IYAGK-STEQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARALMNGGEVILADEPTGALD 176
Cdd:PRK15079 114 RMTIgEIIAeplrTYHPKlSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490367952 177 SQSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRII 214
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVL 233
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
252-647 |
2.23e-22 |
|
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: 102.19 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 252 RFTQALNMAWRAMVVNKIRTLLtmLGIIIGIASVVTIIVIGDAAKDRVLADIKAI-GAntiDIypgkELGSDSPEDKQsl 330
Cdd:COG3127 3 SLRLALRLAWRDLRAGELRLLL--LALVLGVAAVAAVGSFSDRLQAGLARQARELlGG---DL----VLRSDQPLPAA-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 331 TIQDVDALKQQsyiqsVTPQIYFSSRLRRGNQDAPATVSGVNEDYFSVYALKFAQGSTFTPDMIHRQAQ-VVVIDENTRH 409
Cdd:COG3127 72 WLAQARALGLR-----VSRTVEFRSMARAGDGSQLVEVKAVDGAYPLYGELELAPAPPLADALAGGPAPgEVWVDPRLLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 410 RFfpnkQAVIGEQIIIRNIPSTIIGVVAEQ--KSTFGDNKSLRVWVPYSTL--------SSRIYNRsYLdnitVKVKEGY 479
Cdd:COG3127 147 RL----GLKVGDTIRLGDATFTIAGVLTREpdRGGGGFSLAPRVLINLADLeatgliqpGSRVRYR-YL----VAGPDAD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 480 DASV---AEQQI---LRLLTIRHGKKDIftynidsfikaaEKTTQTMQLFLTLVAVISLVVGGIGVMNIMLVSVTERTRE 553
Cdd:COG3127 218 LEALrawLEPALpagQRVRTVEDARPEL------------GRALDRAEQFLLLVALLALLLAGVAVANAARRYVARRLDT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 554 IGIRMAVGARASDVMQQFLIESVLVCLVGGLLGISLSFAIAMFASMMLPNW-----HFVFQPTALISAFACSTAIGVIFG 628
Cdd:COG3127 286 IALLRCLGASRRQIFRIYLLQLLLLGLLGSLLGLLLGALLQALLAALLADLlpvplEPALSPLPLLLGLLVGLLVLLLFA 365
|
410
....*....|....*....
gi 490367952 629 FLPARNAAKMNPIDALARE 647
Cdd:COG3127 366 LPPLLRLRRVPPLRVLRRD 384
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
4.46e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.41 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaal 83
Cdd:PRK13652 3 LIETRDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rREHFGFIFQRYH-LMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNG 162
Cdd:PRK13652 77 -RKFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 163 GEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQIIS 223
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQlDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-222 |
6.69e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.04 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMesdQLA 81
Cdd:PRK13657 332 KGAVEFDDVSFSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALRReHFGFIFQRYHLMAHlTAEQNVEIpaiyaGKST----EQRK--ERARAL---LTR-LGLAERIHYRPSQLSGGQQQ 151
Cdd:PRK13657 406 SLRR-NIAVVFQDAGLFNR-SIEDNIRV-----GRPDatdeEMRAaaERAQAHdfiERKpDGYDTVVGERGRQLSGGERQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 152 RVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-222 |
9.10e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 95.15 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVsRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKStlMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:PRK10418 1 MPQQIELRNI-ALQA----AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQR-------YHLMAHltaeQNVEIPAIYAGKSTEQRkerARALLTRLGLAER---IHYRPSQLSGGQQ 150
Cdd:PRK10418 74 CALRGRKIATIMQNprsafnpLHTMHT----HARETCLALGKPADDAT---LTAALEAVGLENAarvLKLYPFEMSGGML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 151 QRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDmGVVARLADDVAVMSHGRIV 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-223 |
1.44e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEdtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALR 84
Cdd:PRK13640 6 VEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 rEHFGFIFQRY-HLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:PRK13640 84 -EKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQL-NQQGHTVIIVTHDPLIAQQADRIIEIKDGQIIS 223
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLLA 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-203 |
1.54e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKST----LMNILgcldkPSSGEYKVAGQCVADMESDQLAALRREhFGFIFQ--RY 95
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 96 HLMAHLTAEQNVE--IPAIYAGKSTEQRKERARALLTRLGL-AERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPT 172
Cdd:PRK15134 374 SLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190
....*....|....*....|....*....|...
gi 490367952 173 GALDSQSGKEVMAILKQLnQQGHTV--IIVTHD 203
Cdd:PRK15134 454 SSLDKTVQAQILALLKSL-QQKHQLayLFISHD 485
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-253 |
1.68e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.46 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSrLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLM---NILGCLDkPS---SGEYKVAGQCVAD 74
Cdd:PRK14239 2 TEPILQVSDLS-VYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLN-PEvtiTGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 75 MESDQLAaLRREhFGFIFQRYHLMAhLTAEQNVeipaIYaGKSTEQRKERAR---ALLTRLGLA-------ERIHYRPSQ 144
Cdd:PRK14239 77 PRTDTVD-LRKE-IGMVFQQPNPFP-MSIYENV----VY-GLRLKGIKDKQVldeAVEKSLKGAsiwdevkDRLHDSALG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 145 LSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDpliAQQADRIIE----IKDGQ 220
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRS---MQQASRISDrtgfFLDGD 224
|
250 260 270
....*....|....*....|....*....|....*
gi 490367952 221 IISDNNNHHSV--PVKKappaiQTASYfhqVIGRF 253
Cdd:PRK14239 225 LIEYNDTKQMFmnPKHK-----ETEDY---ISGKF 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-223 |
2.48e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.08 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAalrREhFGFIFQRYHLMAHL 101
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA---RK-VAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 102 TAEQNVEI---PAIYA-GKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDS 177
Cdd:PRK10575 101 TVRELVAIgryPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490367952 178 QSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQIIS 223
Cdd:PRK10575 181 AHQVDVLALVHRLSQErGLTVIAVLHDiNMAARYCDYLVALRGGEMIA 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-223 |
3.99e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.31 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILgCLDKPSsGEYKvaGQCVADMESDQL 80
Cdd:PRK13549 2 MEYLLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPH-GTYE--GEIIFEGEELQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALR-REHFG--FIFQRYHLMAHLTAEQNV----EI--------PAIYAgksteqrkeRARALLTRLGLAERIHYRPSQL 145
Cdd:PRK13549 74 SNIRdTERAGiaIIHQELALVKELSVLENIflgnEItpggimdyDAMYL---------RAQKLLAQLKLDINPATPVGNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 146 SGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDpL--IAQQADRIIEIKDGQIIS 223
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHK-LneVKAISDTICVIRDGRHIG 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-222 |
5.37e-21 |
|
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: 91.79 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEDtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV---DISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQRYHLMAHlTAEQNVEIpaiyAGKSTEQRKERA--RALLTRL------GLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:cd03244 78 S-RISIIPQDPVLFSG-TIRSNLDP----FGEYSDEELWQAleRVGLKEFveslpgGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQlNQQGHTVIIVTH--DPLIaqQADRIIEIKDGQII 222
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHrlDTII--DSDRILVLDKGRVV 216
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-224 |
6.38e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 91.84 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 29 LTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCvadmesdqlAALRREHFGFIFQRYhlmahltaEQNVE 108
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---------PGKGWRHIGYVPQRH--------EFAWD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 109 IP-----AIYAGKSTE----QRKERA-----RALLTRLGLAErIHYRP-SQLSGGQQQRVSIARALMNGGEVILADEPTG 173
Cdd:TIGR03771 64 FPisvahTVMSGRTGHigwlRRPCVAdfaavRDALRRVGLTE-LADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490367952 174 ALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIeIKDGQIISD 224
Cdd:TIGR03771 143 GLDMPTQELLTELFIELAGAGTAILMTTHDlAQAMATCDRVV-LLNGRVIAD 193
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-219 |
6.45e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.39 E-value: 6.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALrreHFGFIFQRYHLMAHLTA 103
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 EQNveipaIYAGKSTEQR------------KERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEP 171
Cdd:PRK09700 98 LEN-----LYIGRHLTKKvcgvniidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490367952 172 TGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDG 219
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-221 |
1.17e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 96.71 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNgEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPN-RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aalrREHFGFIFQRYHLMAHlTAEQNVeipaIYAGKSTEQRKERARALLTRL---------GLAERIHYRPSQLSGGQQQ 151
Cdd:TIGR00958 554 ----HRQVALVGQEPVLFSG-SVRENI----AYGLTDTPDEEIMAAAKAANAhdfimefpnGYDTEVGEKGSQLSGGQKQ 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 152 RVSIARALMNGGEVILADEPTGALDSQsgkeVMAILKQL-NQQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAE----CEQLLQESrSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-220 |
1.56e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 93.05 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLD---KPSSGEYKVAGQCVADMESDQLAALRREHFGFIFQryHLM 98
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQ--EPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 99 AHLTAEQNVE------IPAIYAG----KSTEQRKERARALLTRLGLAERIHYR---PSQLSGGQQQRVSIARALMNGGEV 165
Cdd:COG4170 100 SCLDPSAKIGdqlieaIPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 166 ILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVTHDPL-IAQQADRIIEIKDGQ 220
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLEsISQWADTITVLYCGQ 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-213 |
1.79e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.77 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLM---NILGCLDKPSSGEYKVA--GQCVADME 76
Cdd:PRK14243 8 ETVLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVTfhGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 77 SDQLAALRRehFGFIFQRYHLMAHLTAEQNVEIPAI--YAGKSTE--QRKERARALLTRLglAERIHYRPSQLSGGQQQR 152
Cdd:PRK14243 84 VDPVEVRRR--IGMVFQKPNPFPKSIYDNIAYGARIngYKGDMDElvERSLRQAALWDEV--KDKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 153 VSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDpliAQQADRI 213
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHN---MQQAARV 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-256 |
2.66e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.31 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 15 TNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGeYKVAGQCVADMES-----DQLAALRRehFG 89
Cdd:PRK14271 28 TLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSifnyrDVLEFRRR--VG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 90 FIFQRYHLMAhLTAEQNVeIPAIYAGKSTEQRKER--ARALLTRLGL----AERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNV-LAGVRAHKLVPRKEFRgvAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQgHTVIIVTHDplIAQQA---DRIIEIKDGQIISDNNNHHsvpVKKAPPAI 240
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHN--LAQAArisDRAALFFDGRLVEEGPTEQ---LFSSPKHA 256
|
250
....*....|....*.
gi 490367952 241 QTASYFHQVIGRFTQA 256
Cdd:PRK14271 257 ETARYVAGLSGDVKDA 272
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-205 |
4.24e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvadmesdqlaalrREHFGFIFQRYHLMAH- 100
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG--------------DIDDPDVAEACHYLGHr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 ------LTAEQNVEIPAIYAGksteQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGA 174
Cdd:PRK13539 82 namkpaLTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|...
gi 490367952 175 LDSqSGKEVMA--ILKQLNQQGhTVIIVTHDPL 205
Cdd:PRK13539 158 LDA-AAVALFAelIRAHLAQGG-IVIAATHIPL 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-222 |
7.75e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.14 E-value: 7.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVA--DMESD 78
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 QLAALrrehfGFIFQRYHLMAHLTAEQNV----EIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVS 154
Cdd:PRK10762 77 QEAGI-----GIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRlKEIFEICDDVTVFRDGQFI 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-222 |
7.84e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYtngeedtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmESDQLAAL 83
Cdd:COG1129 256 VLEVEGLSVGG--------VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RRehfGFIF-----QRYHLMAHLTAEQNVEIPAI--YAGK---STEQRKERARALLTRLGL-AERIHYRPSQLSGGQQQR 152
Cdd:COG1129 326 RA---GIAYvpedrKGEGLVLDLSIRENITLASLdrLSRGgllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQK 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 153 VSIARALMNGGEVILADEPT-----GAldsqsgK-EVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTrgidvGA------KaEIYRLIRELAAEGKAVIVISSElPELLGLSDRILVMREGRIV 473
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-222 |
8.72e-20 |
|
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: 93.35 E-value: 8.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMesdQLAALR 84
Cdd:COG5265 358 VRFENVSFGY---DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV---TQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 ReHFGFIFQ---------RYhlmahltaeqNVeipaIYA--GKSTEQRKERARA-----LLTRL--GLAERIHYRPSQLS 146
Cdd:COG5265 432 A-AIGIVPQdtvlfndtiAY----------NI----AYGrpDASEEEVEAAARAaqihdFIESLpdGYDTRVGERGLKLS 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490367952 147 GGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-223 |
8.84e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.68 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTL-MNILGCLdKPSSGEYKVAGQCVaDMESDQLAALRREhFGFIFQRYHL 97
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKPL-DYSKRGLLALRQQ-VATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 MAHLT-AEQNVEIPAIYAGKSTEQRKERARALLTrLGLAERIHYRPSQ-LSGGQQQRVSIARALMNGGEVILADEPTGAL 175
Cdd:PRK13638 89 QIFYTdIDSDIAFSLRNLGVPEAEITRRVDEALT-LVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490367952 176 DSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIIS 223
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDiDLIYEISDAVYVLRQGQILT 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-223 |
9.95e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.93 E-value: 9.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILgcldkpsSGEY---KVAGQCVADMESDQLAALR-REHFGF--IFQRYHL 97
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGVYphgSYEGEILFDGEVCRFKDIRdSEALGIviIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 MAHLTAEQNveipaIYAGksTEQRK----------ERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALmnGGEV-- 165
Cdd:NF040905 90 IPYLSIAEN-----IFLG--NERAKrgvidwnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL--SKDVkl 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 166 -ILaDEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDpL--IAQQADRIIEIKDGQIIS 223
Cdd:NF040905 161 lIL-DEPTAALNEEDSAALLDLLLELKAQGITSIIISHK-LneIRRVADSITVLRDGRTIE 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
23-222 |
1.44e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.16 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGcLDKPSSGEYKVAGQCVADmesdqLAALRREHFGF--------IFQ 93
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYmIVG-LVKPDSGRIFLDGEDITH-----LPMHKRARLGIgylpqeasIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 94 RyhlmahLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTG 173
Cdd:COG1137 92 K------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490367952 174 ALDSQSGKEVMAILKQLNQQGHTVIIVTHDpliAQQADRIIE----IKDGQII 222
Cdd:COG1137 166 GVDPIAVADIQKIIRHLKERGIGVLITDHN---VRETLGICDrayiISEGKVL 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
5-223 |
4.31e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.30 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVS---RLYTngeedtvvldqISLTINAGEMVAIIGASGSGKSTLMN-ILGCLdkPSSGEYKVAGQCVADMESDQL 80
Cdd:PRK03695 1 MQLNDVAvstRLGP-----------LSAEVRAGEILHLVGPNGAGKSTLLArMAGLL--PGSGSIQFAGQPLEAWSAAEL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aALRREHFG------FIFQRYH-LMAHLtaeqnveipaiYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRV 153
Cdd:PRK03695 68 -ARHRAYLSqqqtppFAMPVFQyLTLHQ-----------PDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRV 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 154 SIA-------RALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDpL--IAQQADRIIEIKDGQIIS 223
Cdd:PRK03695 136 RLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHD-LnhTLRHADRVWLLKQGKLLA 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-221 |
8.39e-19 |
|
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: 91.61 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAAlrREHFGFIFQRYHLMAHLTA 103
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK---DIETNLDAV--RQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 EQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEV 183
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|....*....
gi 490367952 184 MAILKQLnQQGHTVIIVTHDPLIAQ-QADRIIEIKDGQI 221
Cdd:TIGR01257 1101 WDLLLKY-RSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-223 |
2.25e-18 |
|
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: 88.73 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILgCLDKPS---SGEYKVAGQcvaDMESDQL 80
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYPHgtwDGEIYWSGS---PLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQRYHLMAHLTAEQNV----EIPAIYAGKSTEQRKERARALLTRLGLAERIHYRP-SQLSGGQQQRVSI 155
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIIS 223
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQHVA 221
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
505-647 |
2.43e-18 |
|
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: 89.47 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 505 NIDSFIKAAEKTTQTMQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVMQQFLIESVLVCLVGGL 584
Cdd:COG3127 688 DVDAILDQVRDILDQVSLAVEFLAGFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGL 767
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 585 LGISLSFAIAMFASMMLPNWHFVFQPTALISAFACSTAIGVIFGFLPARNAAKMNPIDALARE 647
Cdd:COG3127 768 LAALLAELAGWALARFVFDLPFSPPWWLWLAGLLGGALLVLLAGLLGARRVLRQPPLEVLREE 830
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-221 |
2.60e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALRREhFGFIFQRYHLMA 99
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD---DVEALSARAASRR-VASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 100 HLTAEQNVEI---PAI--YAGKSTEQRKERARALlTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGA 174
Cdd:PRK09536 91 EFDVRQVVEMgrtPHRsrFDTWTETDRAAVERAM-ERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490367952 175 LDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGKTAVAAIHDlDLAARYCDELVLLADGRV 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-224 |
2.89e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 85.26 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNIL-GCLDKPS-------SGEYKVAGQCVADMESDQLAALR-------RE 86
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 87 HFGFIFQRYHLMAHLTAeqnveipAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARAL------- 159
Cdd:PRK13547 95 AFAFSAREIVLLGRYPH-------ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 160 --MNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHT-VIIVTHDP-LIAQQADRIIEIKDGQIISD 224
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPnLAARHADRIAMLADGAIVAH 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-203 |
2.97e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNGEedtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AAL--RREHFGFIFQ----------RYHLMAHLTaeqnveipaiyagKSTEQRKERARALLTRLGLAERIHYRPSQLSGG 148
Cdd:PRK15056 80 VAYvpQSEEVDWSFPvlvedvvmmgRYGHMGWLR-------------RAKKRDRQIVTAALARVDMVEFRHRQIGELSGG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 149 QQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD 203
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-262 |
4.98e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRL--YTNG---EEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQ--CVA 73
Cdd:PRK15112 1 VETLLEVRNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 74 DMesdqlaALRREHFGFIFQ--RYHLMAHLTAEQNVEIPAIYAGK-STEQRKERARALLTRLGL-AERIHYRPSQLSGGQ 149
Cdd:PRK15112 81 DY------SYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 150 QQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQ-QGHTVIIVT-HDPLIAQQADRIIEIKDGQIisdnnn 227
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTqHLGMMKHISDQVLVMHQGEV------ 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490367952 228 hhsvpVKKAPPAIQTASYFHQVIGR-----FTQALNM-AWR 262
Cdd:PRK15112 229 -----VERGSTADVLASPLHELTKRliaghFGEALTAdAWR 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-223 |
6.15e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.43 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSrlYTNGeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAAL 83
Cdd:PRK11831 7 LVDMRGVS--FTRG--NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREhFGFIFQRYHLMAHLTAEQNV--------EIPAIYAgKSTEQRKeraralLTRLGLAERIHYRPSQLSGGQQQRVSI 155
Cdd:PRK11831 83 RKR-MSMLFQSGALFTDMNVFDNVayplrehtQLPAPLL-HSTVMMK------LEAVGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQIIS 223
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDvPEVLSIADHAYIVADKKIVA 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-220 |
8.01e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSrLYT-NGEedtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKV-AGQCVAdmesdqlaa 82
Cdd:COG4178 363 LALEDLT-LRTpDGR---PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL--------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 lrrehfgFIFQR-YhlmahltaeqnveIPA-------IYAGKSTEQRKERARALLTRLGL---AERIHYR---PSQLSGG 148
Cdd:COG4178 430 -------FLPQRpY-------------LPLgtlrealLYPATAEAFSDAELREALEAVGLghlAERLDEEadwDQVLSLG 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 149 QQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGhTVIIVTHDPLIAQQADRIIEIKDGQ 220
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-214 |
1.13e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.31 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCL-DKPSSGEYKVAgqcvaDMESDQLAALrrehfgfifqryhlmah 100
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGALkGTPVAGCVDVP-----DNQFGREASL----------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 ltaeqnveIPAIYAGKSTEQRKEraraLLTRLGLAERIHYR--PSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQ 178
Cdd:COG2401 103 --------IDAIGRKGDFKDAVE----LLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 490367952 179 SGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQ--QADRII 214
Cdd:COG2401 171 TAKRVARNLQKLARRaGITLVVATHHYDVIDdlQPDLLI 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-251 |
1.16e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 10 VSRL----YTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAalRR 85
Cdd:PRK10253 5 VARLrgeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 ehFGFIFQRYHLMAHLTAEQNVEipaiyAGKSTEQ------RKERARALLTRL---GLAERIHYRPSQLSGGQQQRVSIA 156
Cdd:PRK10253 83 --IGLLAQNATTPGDITVQELVA-----RGRYPHQplftrwRKEDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 157 RALMNGGEVILADEPTGALDSQSGKEVMAILKQLN-QQGHTVIIVTHDPLIA-QQADRIIEIKDGQIISDNnnhhsvpvk 234
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQG--------- 226
|
250
....*....|....*..
gi 490367952 235 kAPPAIQTASYFHQVIG 251
Cdd:PRK10253 227 -APKEIVTAELIERIYG 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-218 |
1.41e-17 |
|
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: 80.28 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSrLYTngEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNIL--------GCLDKPssgeykvagqcvadme 76
Cdd:cd03223 1 IELENLS-LAT--PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgsGRIGMP---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 77 sdqlaalRREHFGFIFQRyhlmahltaeqnveiPAIYAGKsteqrkeraralltrlgLAERIHYrPSQ--LSGGQQQRVS 154
Cdd:cd03223 62 -------EGEDLLFLPQR---------------PYLPLGT-----------------LREQLIY-PWDdvLSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSGKEVMAILKQLnqqGHTVIIVTHDPLIAQQADRIIEIKD 218
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-203 |
2.35e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKST-LMNILGCLDKPssgeykvAGQCVADMESDQLA 81
Cdd:PRK10895 2 ATLTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGIVPRD-------AGNIIIDDEDISLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 82 ALR---REHFGFIFQRYHLMAHLTAEQNV-EIPAIYAGKSTEQRKERARALLTRLGLAeriHYRPS---QLSGGQQQRVS 154
Cdd:PRK10895 71 PLHaraRRGIGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIE---HLRDSmgqSLSGGERRRVE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD 203
Cdd:PRK10895 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-222 |
2.72e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 83.31 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMnilgcldKPSSGEYKVAGQCVAD-MESDQLAA 82
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIA-------KAICGVTKDNWRVTADrMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 L------RREHFG----FIFQRYHlmAHLTAEQNVE------IPA-IYAGKSTEQ---RKERARALLTRLGLAER---IH 139
Cdd:PRK15093 76 LrlspreRRKLVGhnvsMIFQEPQ--SCLDPSERVGrqlmqnIPGwTYKGRWWQRfgwRKRRAIELLHRVGIKDHkdaMR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 140 YRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVI-IVTHD-PLIAQQADRIIEIK 217
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDlQMLSQWADKINVLY 233
|
....*
gi 490367952 218 DGQII 222
Cdd:PRK15093 234 CGQTV 238
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-211 |
6.03e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 79.61 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVadmesDQLAALRREHFGFIFQRYHLM 98
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-----KKDLCTYQKQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 99 AHLTAEQNVeipaiYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQ 178
Cdd:PRK13540 87 PYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180 190
....*....|....*....|....*....|...
gi 490367952 179 SGKEVMAILKQLNQQGHTVIIVTHDPLIAQQAD 211
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-219 |
1.07e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.30 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLM-NILGCLDKpSSGEYKVAGQCVADMESDQLAALRREHFGFIFQRYHLM 98
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 99 aHLTAEQNVEIPAIYagksteqRKERARALLTRLGLAERIHYRPS-----------QLSGGQQQRVSIARALMNGGEVIL 167
Cdd:cd03290 92 -NATVEENITFGSPF-------NKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490367952 168 ADEPTGALDSQSGKEVM--AILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDG 219
Cdd:cd03290 164 LDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-222 |
1.15e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.73 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDK--PSSGEYKVAGQCVADMESDQLAalrREHFGFIFQ--- 93
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERA---RAGIFLAFQypv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 94 -------RYHLMAHLTAEQNVEIPAIyagksteQRKERARALLTRLGLAERIHYRP--SQLSGGQQQRVSIARALMNGGE 164
Cdd:COG0396 88 eipgvsvSNFLRTALNARRGEELSAR-------EFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQ--QADRIIEIKDGQII 222
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDyiKPDFVHVLVDGRIV 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-222 |
1.44e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCV----------A 73
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 74 DMESDQLAALRREHFGFIFQRyhLMAHLT-----AEQNVEIPAIYAGKSTEQRKERARALL--TRLGLAERIHYR-PSQL 145
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQE--PMTSLNpvftvGEQIAESIRLHQGASREEAMVEAKRMLdqVRIPEAQTILSRyPHQL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 146 SGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDmGVVAEIADRVLVMYQGEAV 248
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-222 |
1.52e-16 |
|
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: 78.46 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 2 SALLELNNVSRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGcldKPSSGEYKVAGQCVAD-MESDQL 80
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEGDIHYNgIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHFGFIFQRYHLMAHLTAEQNVEIPAiyagksteqrKERARALLtrlglaerihyrpSQLSGGQQQRVSIARALM 160
Cdd:cd03233 78 AEKYPGEIIYVSEEDVHFPTLTVRETLDFAL----------RCKGNEFV-------------RGISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVT---HDPLIAQQADRIIEIKDGQII 222
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqASDEIYDLFDKVLVLYEGRQI 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-222 |
2.14e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSrlyTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESdqlAAL 83
Cdd:COG3845 257 VLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP---RER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 RREHFGFI---FQRYHLMAHLTAEQNVEIPAIYAGK-------STEQRKERARALLTRLGL-AERIHYRPSQLSGGQQQR 152
Cdd:COG3845 331 RRLGVAYIpedRLGRGLVPDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490367952 153 VSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDpL--IAQQADRIIEIKDGQII 222
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISED-LdeILALSDRIAVMYEGRIV 481
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-222 |
4.46e-16 |
|
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: 77.18 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLD-KPSSGEYKVAGQCVADMESDQLAalrREHFGFIFQRyh 96
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 97 lmahltaeqNVEIPAIyagksteqrkeraralltrlGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALD 176
Cdd:cd03217 86 ---------PPEIPGV--------------------KNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490367952 177 SQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQ--QADRIIEIKDGQII 222
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-222 |
4.69e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLAALRREhFGFIFQRYHlmAHLTA 103
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDPY--ASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 EQNV-----EIPAIYAGKSTEQRKERARALLTRLGLAERIHYR-PSQLSGGQQQRVSIARALMNGGEVILADEPTGALDS 177
Cdd:PRK10261 417 RQTVgdsimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490367952 178 QSGKEVMAILKQLNQQ-GHTVIIVTHDPLIAQQ-ADRIIEIKDGQII 222
Cdd:PRK10261 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIV 543
|
|
| FtsX |
pfam02687 |
FtsX-like permease family; This is a family of predicted permeases and hypothetical ... |
526-640 |
7.10e-16 |
|
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: 74.21 E-value: 7.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 526 LVAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVMQQFLIESVLVCLVGGLLGISLSFAIAMF----ASMML 601
Cdd:pfam02687 2 LFSLLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVIGLLLGLLLAKLiailLYSSG 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 490367952 602 PNWHFVFQPTALISAFACSTAIGVIFGFLPARNAAKMNP 640
Cdd:pfam02687 82 ISLPILVPPLSILIALLLALLIALLASLLPALRIRKINP 120
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-213 |
7.88e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNIL-GCLDkPSSGEYKVAGQCVA--DMESdqlaalrREHFGFIFQRYH 96
Cdd:NF033858 278 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLP-ASEGEAWLFGQPVDagDIAT-------RRRVGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 97 LMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTgald 176
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT---- 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490367952 177 sqSGKEVMA------ILKQLN-QQGHTVIIVTHDPLIAQQADRI 213
Cdd:NF033858 426 --SGVDPVArdmfwrLLIELSrEDGVTIFISTHFMNEAERCDRI 467
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-223 |
1.15e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.38 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILG---CLDkpsSGEYKVAGQC-VADMESD 78
Cdd:PRK11147 2 SLISIHGAWLSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRIIYEQDLiVARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 79 QLAALRREHFGFI----------FQRYHLMAHLTA----EQNV----EIPAIYAGKSTEQRKERARALLTRLGLAEriHY 140
Cdd:PRK11147 75 PPRNVEGTVYDFVaegieeqaeyLKRYHDISHLVEtdpsEKNLnelaKLQEQLDHHNLWQLENRINEVLAQLGLDP--DA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 141 RPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDsqsgkeVMAI--LKQ--LNQQGhTVIIVTHD-PLIAQQADRIIE 215
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD------IETIewLEGflKTFQG-SIIFISHDrSFIRNMATRIVD 225
|
....*...
gi 490367952 216 IKDGQIIS 223
Cdd:PRK11147 226 LDRGKLVS 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-222 |
1.32e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.14 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalrREHFGFIFQRYHLMA 99
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 100 HlTAEQNVeipAIYAGKSTEQRKERARAL------LTRL--GLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEP 171
Cdd:PRK10789 403 D-TVANNI---ALGRPDATQQEIEHVARLasvhddILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490367952 172 TGALDSQSGKEVMAILKQLNqQGHTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-203 |
6.92e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 7 LNNVSRLYTNGEEdtvVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGE------YKV------------- 67
Cdd:TIGR03719 7 MNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgIKVgylpqepqldptk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 68 -AGQCVADMESDQLAALRRehFGFIFQRYHL----MAHLTAEQNVEIPAIYAGK--STEQRKERA-RALltRLglaerih 139
Cdd:TIGR03719 84 tVRENVEEGVAEIKDALDR--FNEISAKYAEpdadFDKLAAEQAELQEIIDAADawDLDSQLEIAmDAL--RC------- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 140 yrP------SQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSgkevMAILKQ-LNQQGHTVIIVTHD 203
Cdd:TIGR03719 153 --PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERhLQEYPGTVVAVTHD 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-219 |
9.41e-15 |
|
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: 73.05 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGcLDKPS---SGEYKVAGQCVADmesdqlaALRREhFGFIFQRYHLMAH 100
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLA-GRKTAgviTGEILINGRPLDK-------NFQRS-TGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 LTAEQNVEIPAIYAGKSTEQRKeraralltrlglaerihyrpsqlsggqqqRVSIARALMNGGEVILADEPTGALDSQSG 180
Cdd:cd03232 94 LTVREALRFSALLRGLSVEQRK-----------------------------RLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490367952 181 KEVMAILKQLNQQGHTVIIVTHDP--LIAQQADRIIEIKDG 219
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTIHQPsaSIFEKFDRLLLLKRG 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-203 |
1.15e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYTNgeedTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvadmesdql 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aaLRrehFGFIFQRYHLMAH--LTAEQNVEI-PAIyagksteqRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIAR 157
Cdd:PRK09544 67 --LR---IGYVPQKLYLDTTlpLTVNRFLRLrPGT--------KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490367952 158 ALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQ-GHTVIIVTHD 203
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-203 |
1.33e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.90 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVaGQCVadmesdqlaalr 84
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 reHFGFIFQ-RYHLMAHLTAEQ------------NVEIPA-IYAG----KSTEQRKeraralltrlglaerihyRPSQLS 146
Cdd:TIGR03719 386 --KLAYVDQsRDALDPNKTVWEeisggldiiklgKREIPSrAYVGrfnfKGSDQQK------------------KVGQLS 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 147 GGQQQRVSIARALMNGGEVILADEPTGALDSqsgkEVMAILKQ--LNQQGHTVIIvTHD 203
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEalLNFAGCAVVI-SHD 499
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-223 |
1.55e-14 |
|
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: 72.83 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtnGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALR 84
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI---DISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REhFGFIFQRYHLMAHlTAEQNVEIPAIYagkSTEQRKEraralltrlglAERIHYRPSQLSGGQQQRVSIARALMNGGE 164
Cdd:cd03369 82 SS-LTIIPQDPTLFSG-TIRSNLDPFDEY---SDEEIYG-----------ALRVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 165 VILADEPTGALDSQSGKEVMAILKQLnQQGHTVIIVTHDPLIAQQADRIIEIKDGQIIS 223
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-221 |
2.66e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 27 ISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGqcvADME-SDQLAAL----------RREHfGFifqry 95
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG---KDISpRSPLDAVkkgmayitesRRDN-GF----- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 96 hlMAHLTAEQNVEI-PAIYAGK----------STEQR-KERARALLTrLGLAErIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:PRK09700 353 --FPNFSIAQNMAIsRSLKDGGykgamglfheVDEQRtAENQRELLA-LKCHS-VNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-220 |
4.96e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSgeykVAGQCVADMESDQLAALRREhfGFIFQRYHLM 98
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILKRT--GFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 99 AHLTAEQNVEIPAIYAGKSTEQRKER---ARALLTRLGLA--ERIHYRPS---QLSGGQQQRVSIARALMNGGEVILADE 170
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKilvAESVISELGLTkcENTIIGNSfirGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490367952 171 PTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP--LIAQQADRIIEIKDGQ 220
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPssRVYQMFDSVLVLSEGR 284
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-211 |
5.43e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALL---ELNNVSRLYTNGEedtvVLDQISLTINAGEMVAIIGASGSGKSTLmniLGCLDKPSS--GEYKVAG------ 69
Cdd:PRK14258 1 MSKLIpaiKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTF---LKCLNRMNEleSEVRVEGrveffn 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 70 QCVADMESDqLAALRREhFGFIFQRYHLMAhLTAEQNV-------------EIPAIY--AGKSTEQRKEraralltrlgL 134
Cdd:PRK14258 74 QNIYERRVN-LNRLRRQ-VSMVHPKPNLFP-MSVYDNVaygvkivgwrpklEIDDIVesALKDADLWDE----------I 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 135 AERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHD-PLIAQQAD 211
Cdd:PRK14258 141 KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNlHQVSRLSD 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-221 |
5.58e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 27 ISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVAdmESDQLAALR---------REHFGFIfqryhl 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID--IRSPRDAIRagimlcpedRKAEGII------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 mAHLTAEQNVEIPA----IYAGKSTEQRKER--ARALLTRLGLAERIHYRP-SQLSGGQQQRVSIARALMNGGEVILADE 170
Cdd:PRK11288 344 -PVHSVADNINISArrhhLRAGCLINNRWEAenADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490367952 171 PTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRI 474
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-221 |
6.16e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDKPSSGEYKVAGQcVADME--SDQLAALRREH--FGFIFQ--RYH 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-VAYVPqvSWIFNATVRDNilFGSPFDpeRYE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 97 LMAHLTAEQNvEIPAIYAGKSTEqrkeraralltrlglaerIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALD 176
Cdd:PLN03130 712 RAIDVTALQH-DLDLLPGGDLTE------------------IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490367952 177 SQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:PLN03130 773 AHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-221 |
1.36e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNIL-GCLDKpSSGEYKVAGQ-CVADMESDQLAAlrrehfGFIF-----QRYH 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHeVVTRSPQDGLAN------GIVYisedrKRDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 97 LMAHLTAEQNVEIPAI-YAGKSTEQ-RKERARALLTRLGLAERIHyRPSQ------LSGGQQQRVSIARALMNGGEVILA 168
Cdd:PRK10762 341 LVLGMSVKENMSLTALrYFSRAGGSlKHADEQQAVSDFIRLFNIK-TPSMeqaiglLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490367952 169 DEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-222 |
1.62e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.39 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVA-----GQCVADMESDq 79
Cdd:PRK15064 320 LEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenaniGYYAQDHAYD- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 80 laalrrehFGFIFQRYHLMAHLTAEqnveipaiyagKSTEQrkeRARALLTRLGL-AERIHYRPSQLSGGQQQRVSIARA 158
Cdd:PRK15064 395 --------FENDLTLFDWMSQWRQE-----------GDDEQ---AVRGTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEVMAILKqlNQQGhTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEG-TLIFVSHDrEFVSSLATRIIEITPDGVV 514
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-222 |
2.11e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.21 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYtngEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:PRK10790 337 QSGRIDIDNVSFAY---RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 aalrREHFGFIFQRYHLMA-----HLTAEQNVEIPAIYAGKSTEQRKERARALLTrlGLAERIHYRPSQLSGGQQQRVSI 155
Cdd:PRK10790 414 ----RQGVAMVQQDPVVLAdtflaNVTLGRDISEEQVWQALETVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 156 ARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGhTVIIVTHDPLIAQQADRIIEIKDGQII 222
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT-TLVVIAHRLSTIVEADTILVLHRGQAV 553
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-220 |
2.43e-13 |
|
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: 68.50 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLmnILGCLDKPSSGEYKVAGQCVADMES---DQLAALRREHFGFifqryhlmah 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLISFLPKFSRNKLifiDQLQFLIDVGLGY---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 LTAEQNVeipaiyagksteqrkeraralltrlglaerihyrpSQLSGGQQQRVSIARALMNG--GEVILADEPTGALDSQ 178
Cdd:cd03238 79 LTLGQKL-----------------------------------STLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQ 123
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490367952 179 SGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQ 220
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-221 |
2.81e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGclDKPSS--------GEYKVAGQCVA 73
Cdd:PRK10938 259 PRIVLNNGVVSY----NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlITG--DHPQGysndltlfGRRRGSGETIW 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 74 DMesdqlaalrREHFGFIFQRYHLMAHL-TAEQNVEIP------AIYAGKSTEQRKeRARALLTRLGLAERIHYRPSQ-L 145
Cdd:PRK10938 333 DI---------KKHIGYVSSSLHLDYRVsTSVRNVILSgffdsiGIYQAVSDRQQK-LAQQWLDILGIDKRTADAPFHsL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 146 SGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHT-VIIVTHdpliaQQAD-------RIIEIK 217
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH-----HAEDapacithRLEFVP 477
|
....
gi 490367952 218 DGQI 221
Cdd:PRK10938 478 DGDI 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-221 |
3.71e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.06 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 14 YTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDKpSSGEYKVAGQCV-----ADMESDQLaalrREH 87
Cdd:TIGR00957 644 FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGSVAyvpqqAWIQNDSL----REN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 88 FGFifqryhlmahltaeqnveipaiyaGKSTEQRKER----ARALLTRL-----GLAERIHYRPSQLSGGQQQRVSIARA 158
Cdd:TIGR00957 719 ILF------------------------GKALNEKYYQqvleACALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARA 774
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 159 LMNGGEVILADEPTGALDSQSGKEV-------MAILKqlnqqGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVDAHVGKHIfehvigpEGVLK-----NKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-217 |
5.42e-13 |
|
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: 67.00 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNILGcldkpssgeykvagqcvadmesdqlaalrrehFGFIFQRYHLMAHL 101
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG--------------------------------LALGGAQSATRRRS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 102 TAEQNVEIPAIYAgksteqrkeraralltrlglaeRIHYRPSQLSGGQQQRVSIARAL----MNGGEVILADEPTGALDS 177
Cdd:cd03227 57 GVKAGCIVAAVSA----------------------ELIFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490367952 178 QSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIK 217
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-203 |
6.72e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 27 ISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEykvagqcVADMESDQLAALRREHFGFIFQRYH---LMAHLTA 103
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGN-------VSLDPNERLGKLRQDQFAFEEFTVLdtvIMGHTEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 -EQNVEIPAIYA-----------------------GKSTEQRkerARALLTRLGLAERIHYRP-SQLSGGQQQRVSIARA 158
Cdd:PRK15064 93 wEVKQERDRIYAlpemseedgmkvadlevkfaemdGYTAEAR---AGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490367952 159 LMNGGEVILADEPTGALDSQSgkevMAILKQ-LNQQGHTVIIVTHD 203
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLDINT----IRWLEDvLNERNSTMIIISHD 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-226 |
9.51e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDKPSSGEYKVAGQCV-ADMESDQLAALRREH--FGFIFQ--RYHL 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAyVPQVSWIFNATVRENilFGSDFEseRYWR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 MAHLTAEQNVEipAIYAGKSteqrkeraralLTRLGlaerihYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDS 177
Cdd:PLN03232 713 AIDVTALQHDL--DLLPGRD-----------LTEIG------ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490367952 178 QSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDGQIISDNN 226
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-176 |
1.18e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVaGQCVadmesdQLAALR 84
Cdd:PRK11819 325 IEAENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHfgfifqryhlmAHLTAEQNV----------------EIPA-IYAG----KSTEQRKeraralltRLGlaerihyrps 143
Cdd:PRK11819 394 QSR-----------DALDPNKTVweeisggldiikvgnrEIPSrAYVGrfnfKGGDQQK--------KVG---------- 444
|
170 180 190
....*....|....*....|....*....|...
gi 490367952 144 QLSGGQQQRVSIARALMNGGEVILADEPTGALD 176
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-219 |
1.99e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 70.71 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 8 NNVSRLYTNGEED----------TVVLDQISLTINAGEMVAIIGASGSGKST-LMNILGCLDkPSSGEYKVAGQ-CVADM 75
Cdd:TIGR01271 416 NNKARKQPNGDDGlffsnfslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSlLMMIMGELE-PSEGKIKHSGRiSFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 76 ESDQLAALRREH--FGFIFQRYHLMAHLTAEQNVEIPAIYAgksteqrkERARALLTRLGLAerihyrpsqLSGGQQQRV 153
Cdd:TIGR01271 495 TSWIMPGTIKDNiiFGLSYDEYRYTSVIKACQLEEDIALFP--------EKDKTVLGEGGIT---------LSGGQRARI 557
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVM--AILKQLNQQghTVIIVTHDPLIAQQADRIIEIKDG 219
Cdd:TIGR01271 558 SLARAVYKDADLYLLDSPFTHLDVVTEKEIFesCLCKLMSNK--TRILVTSKLEHLKKADKILLLHEG 623
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-203 |
2.94e-12 |
|
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: 69.43 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 34 GEMVAIIGASGSGKSTLMNILGCLDKPSSGEYkvagqcvaDMESDQLAALRRehfgfiFQRYHLMAHLTA---------- 103
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKR------FRGTELQDYFKKlangeikvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 -EQNVE-IPAIYAG------KSTEQRKeRARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGAL 175
Cdd:COG1245 165 kPQYVDlIPKVFKGtvrellEKVDERG-KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*...
gi 490367952 176 DSQSGKEVMAILKQLNQQGHTVIIVTHD 203
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-216 |
4.24e-12 |
|
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: 66.13 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLM---------------------NILGCLDKPSSGeyKVAGQCVAdMESDQLAA 82
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVD--SIEGLSPA-IAIDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 LR--REHFGFIFQRYHLMAHLTAeqNVEIpaiyagksteqrKERARaLLTRLGLAERIHYRPSQ-LSGGQQQRVSIARAL 159
Cdd:cd03270 88 SRnpRSTVGTVTEIYDYLRLLFA--RVGI------------RERLG-FLVDVGLGYLTLSRSAPtLSGGEAQRIRLATQI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 160 MNG--GEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEI 216
Cdd:cd03270 153 GSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-220 |
4.24e-12 |
|
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: 67.19 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKST-LMNILGCLDkPSSGEYKVAGQCVAdmeSDQLAALR----REH--FGFIFQRY 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSlLMLILGELE-PSEGKIKHSGRISF---SSQFSWIMpgtiKENiiFGVSYDEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 96 HLMAHLTAEQNVEIPAIYAgksteqrkERARALLTRLGLAerihyrpsqLSGGQQQRVSIARALMNGGEVILADEPTGAL 175
Cdd:cd03291 128 RYKSVVKACQLEEDITKFP--------EKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490367952 176 DSQSGKEVM--AILKQLNQQghTVIIVTHDPLIAQQADRIIEIKDGQ 220
Cdd:cd03291 191 DVFTEKEIFesCVCKLMANK--TRILVTSKMEHLKKADKILILHEGS 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-203 |
9.97e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 7 LNNVSRLYtngEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGE------YKV------------- 67
Cdd:PRK11819 9 MNRVSKVV---PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKVgylpqepqldpek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 68 -AGQCVADMESDQLAALRRehFGFIFQRY--------HLMAHLTAEQNvEIPAIyAGKSTEQRKERA-RALltRLglaer 137
Cdd:PRK11819 86 tVRENVEEGVAEVKAALDR--FNEIYAAYaepdadfdALAAEQGELQE-IIDAA-DAWDLDSQLEIAmDAL--RC----- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367952 138 ihyrP------SQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSgkevMAILKQ-LNQQGHTVIIVTHD 203
Cdd:PRK11819 155 ----PpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQfLHDYPGTVVAVTHD 219
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-248 |
1.00e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.89 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNILG--------------------------CLDKPSSgEYKVAGqcvaDM 75
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKneisadggsytfpgnwqlawvnqetpALPQPAL-EYVIDG----DR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 76 ESDQLAAlrREHFGFIFQRYHLMAHLTAEqnveIPAIYAGKSteqrKERARALLTRLGLAERIHYRP-SQLSGGQQQRVS 154
Cdd:PRK10636 90 EYRQLEA--QLHDANERNDGHAIATIHGK----LDAIDAWTI----RSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSgkeVMAILKQLNQQGHTVIIVTH-----DPLIaqqaDRIIEIKDGQIISDNNNHH 229
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILISHdrdflDPIV----DKIIHIEQQSLFEYTGNYS 232
|
250 260
....*....|....*....|
gi 490367952 230 SVPVKKAPP-AIQTASYFHQ 248
Cdd:PRK10636 233 SFEVQRATRlAQQQAMYESQ 252
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-202 |
1.01e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.50 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTNGEEDTVvlDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlaal 83
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAV--DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV---- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rREHFGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGG 163
Cdd:TIGR01257 2011 -HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190
....*....|....*....|....*....|....*....
gi 490367952 164 EVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTH 202
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-221 |
1.04e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.27 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILgcldkpsSGEYKVagqcvadmESDQLAALRRehFGFIFQRYHLM 98
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL-------LSQFEI--------SEGRVWAERS--IAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 99 aHLTAEQNV-----EIPAIYAGKSTEQRKERARALLTRlGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTG 173
Cdd:PTZ00243 734 -NATVRGNIlffdeEDAARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490367952 174 ALDSQSGKEVM--AILKQLnqQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:PTZ00243 812 ALDAHVGERVVeeCFLGAL--AGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-200 |
1.10e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.35 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVSRLYtngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQL 80
Cdd:PRK10938 1 MSSLQISQGTFRLS-----DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREhfgfIFQRYHLMAHLTAEQNVeipaiyaGKSTEQ-------RKERARALLTRLGLAERIHYRPSQLSGGQQQRV 153
Cdd:PRK10938 76 QKLVSD----EWQRNNTDMLSPGEDDT-------GRTTAEiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKT 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIV 200
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-203 |
3.92e-11 |
|
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: 63.92 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 34 GEMVAIIGASGSGKSTLMNILGCLDKPSSGEYkvagqcvaDMESDQLAALRreHF-GFIFQRYhLMAHLTAE-------Q 105
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEILD--EFrGSELQNY-FTKLLEGDvkvivkpQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 106 NV-EIPAIYAGKSTE---QRKERAR--ALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQS 179
Cdd:cd03236 95 YVdLIPKAVKGKVGEllkKKDERGKldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....
gi 490367952 180 GKEVMAILKQLNQQGHTVIIVTHD 203
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHD 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-172 |
3.95e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYtnGeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGqcvADMESdqlAALRR 85
Cdd:NF033858 3 RLEGVSHRY--G--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG---GDMAD---ARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 86 EhfgfIFQR--Y-------HLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAeRIHYRPS-QLSGGQQQRVSI 155
Cdd:NF033858 73 A----VCPRiaYmpqglgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLA-PFADRPAgKLSGGMKQKLGL 147
|
170
....*....|....*..
gi 490367952 156 ARALMNGGEVILADEPT 172
Cdd:NF033858 148 CCALIHDPDLLILDEPT 164
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-202 |
5.13e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMEsdqlaalRREHFGFIFQRYHLMA 99
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 100 HLTAEQNVEIPAIYAGKSTEQRKERAralLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQS 179
Cdd:PRK13543 96 DLSTLENLHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180
....*....|....*....|...
gi 490367952 180 GKEVMAILKQLNQQGHTVIIVTH 202
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTH 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-219 |
9.40e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvaDMESDQLAALRREhFGFIFQRYHLMAHl 101
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR---EIGAYGLRELRRQ-FSMIPQDPVLFDG- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 102 TAEQNVEiPAIyagkstEQRKERARALLTRLGLAERIHYRP-----------SQLSGGQQQRVSIARALMNGGE-VILAD 169
Cdd:PTZ00243 1399 TVRQNVD-PFL------EASSAEVWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARALLKKGSgFILMD 1471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490367952 170 EPTG----ALDSQSGKEVMAILkqlnqQGHTVIIVTHDPLIAQQADRIIEIKDG 219
Cdd:PTZ00243 1472 EATAnidpALDRQIQATVMSAF-----SAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-221 |
2.13e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 27 ISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlaalrREHFGFIF-----QRYHLmaHL 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGL--YL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 102 TAEQNVEIPAI-YAGKSTEQRKERARALLTRLGLAERIHYRPSQ-----LSGGQQQRVSIARALMNGGEVILADEPTGAL 175
Cdd:PRK15439 355 DAPLAWNVCALtHNRRGFWIKPARENAVLERYRRALNIKFNHAEqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490367952 176 DSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-222 |
2.15e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.58 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGclDKPS----SGEYKVAGQCVADMESDQlaalrREHFGfIFqry 95
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPAykilEGDILFKGESILDLEPEE-----RAHLG-IF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 96 hlmahLTAEQNVEIP---------AIYAGKSTEQRKERARAL---------LTRLGLAERIHYRPSQ--LSGGQQQRVSI 155
Cdd:CHL00131 88 -----LAFQYPIEIPgvsnadflrLAYNSKRKFQGLPELDPLefleiinekLKLVGMDPSFLSRNVNegFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 156 AR-ALMNGGEVILaDEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP--LIAQQADRIIEIKDGQII 222
Cdd:CHL00131 163 LQmALLDSELAIL-DETDSGLDIDALKIIAEGINKLMTSENSIILITHYQrlLDYIKPDYVHVMQNGKII 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-214 |
3.04e-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: 63.26 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 30 TINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGE--------YKvaGQCV-ADMESDQLAALRREHFGFIFQRYHlmah 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedlkisYK--PQYIsPDYDGTVEEFLRSANTDDFGSSYY---- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 101 ltaeqNVEIpaiyagksteqrkeraralLTRLGLaERIHYRP-SQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQS 179
Cdd:COG1245 436 -----KTEI-------------------IKPLGL-EKLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*..
gi 490367952 180 GKEVMAILKQL-NQQGHTVIIVTHD-PLIAQQADRII 214
Cdd:COG1245 491 RLAVAKAIRRFaENRGKTAMVVDHDiYLIDYISDRLM 527
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-219 |
5.06e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 62.92 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 127 ALLTRLGLAERIHYRP-SQLSGGQQQRVSIARALmnGGEVI----LADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVT 201
Cdd:PRK00635 458 SILIDLGLPYLTPERAlATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVE 535
|
90
....*....|....*...
gi 490367952 202 HDPLIAQQADRIIEIKDG 219
Cdd:PRK00635 536 HDEQMISLADRIIDIGPG 553
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-229 |
5.75e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDKPSSGEYKVAGQCV-----ADMESDQLAALRREHfgfifQRYH 96
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVkirnpQQAIAQGIAMVPEDR-----KRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 97 LMAHLTAEQNVEIPAI--YAGKST--EQRKER-ARALLTRLGL-AERIHYRPSQLSGGQQQRVSIARALMNGGEVILADE 170
Cdd:PRK13549 352 IVPVMGVGKNITLAALdrFTGGSRidDAAELKtILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 171 PTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISDNNNHH 229
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGDLINHN 491
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-221 |
6.94e-10 |
|
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: 60.25 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDkpSSGEYKVAGQCVADMESDQLaal 83
Cdd:cd03289 3 MTVKDLTAKYTEG--GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVPLQKW--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 84 rREHFGFIFQRYHLMAHlTAEQNVEiPaiYAGKSTEQRKERARalltRLGLAERIHYRPSQ-----------LSGGQQQR 152
Cdd:cd03289 76 -RKAFGVIPQKVFIFSG-TFRKNLD-P--YGKWSDEEIWKVAE----EVGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 153 VSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQlNQQGHTVIIVTH--DPLIAQQadRIIEIKDGQI 221
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHriEAMLECQ--RFLVIEENKV 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-203 |
7.22e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 34 GEMVAIIGASGSGKSTLMNILGCLDKPSSGEYkvagqcvaDMESDQLAALrrEHF-GFIFQRYhlMAHLTAE-------- 104
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDY--------EEEPSWDEVL--KRFrGTELQNY--FKKLYNGeikvvhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 105 QNVE-IPAIYAG------KSTEQRKeRARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDS 177
Cdd:PRK13409 167 QYVDlIPKVFKGkvrellKKVDERG-KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*.
gi 490367952 178 QSGKEVMAILKQLnQQGHTVIIVTHD 203
Cdd:PRK13409 246 RQRLNVARLIREL-AEGKYVLVVEHD 270
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-215 |
1.23e-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: 61.85 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTngEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLdKPSSGEYKVAGqcvADMESDQLAALR 84
Cdd:TIGR01271 1218 MDVQGLTAKYT--EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG---VSWNSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REhFGFIFQRYHLMAHlTAEQNVEIPAIYAGKSTEQRKEraralltRLGLAERIHYRPSQ-----------LSGGQQQRV 153
Cdd:TIGR01271 1292 KA-FGVIPQKVFIFSG-TFRKNLDPYEQWSDEEIWKVAE-------EVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLM 1362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQlNQQGHTVIIVTH--DPLIAQQADRIIE 215
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHrvEALLECQQFLVIE 1425
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-220 |
1.52e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.96 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 30 TINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVA----DMESDQLAALRRehfgfiFQRYHLMAHLTAEQ 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD------LLSSITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 106 -NVEIpaiyagksteqrkeraralLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVM 184
Cdd:cd03237 95 fKTEI-------------------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 490367952 185 AILKQ--LNQQgHTVIIVTHDPLIAQQ-ADRIIeIKDGQ 220
Cdd:cd03237 156 KVIRRfaENNE-KTAFVVEHDIIMIDYlADRLI-VFEGE 192
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-222 |
6.61e-09 |
|
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: 57.24 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMN-ILG-CLDKPSSGEYKVAGQC-----------VADMESDQLAALRREH--- 87
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYpALARRLHLKKEQPGNHdrieglehidkVIVIDQSPIGRTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 88 ----FGFIFQ---------RYHlmahltaEQNVEIpaIYAGKST----EQRKERARALLTRL-GLAERIH--------Y- 140
Cdd:cd03271 91 ytgvFDEIRElfcevckgkRYN-------RETLEV--RYKGKSIadvlDMTVEEALEFFENIpKIARKLQtlcdvglgYi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 141 ---RPS-QLSGGQQQRVSIARALMN---GGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRI 213
Cdd:cd03271 162 klgQPAtTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWI 241
|
250
....*....|....*
gi 490367952 214 IEI------KDGQII 222
Cdd:cd03271 242 IDLgpeggdGGGQVV 256
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-202 |
8.86e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQcvadmesdqlAALrrehfgfIFQRYHLMAHLTA 103
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AAL-------IAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 104 EQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEV 183
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170
....*....|....*....
gi 490367952 184 MAILKQLNQQGHTVIIVTH 202
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISH 201
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-251 |
9.13e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNilgCLDKPSSGEYKVAGQCVADMESDQLAALRRehFGFIFQR-YHL 97
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLN---VLAERVTTGVITGGDRLVNGRPLDSSFQRS--IGYVQQQdLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 mAHLTAEQNVEIPAIYAGKSTEQRKERAR------ALLTRLGLAERIHYRPSQ-LSGGQQQRVSIARALM-NGGEVILAD 169
Cdd:TIGR00956 849 -PTSTVRESLRFSAYLRQPKSVSKSEKMEyveeviKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVaKPKLLLFLD 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 170 EPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDP--LIAQQADRIIEI-KDGQIIS----DNNNH--------HSVPvk 234
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPsaILFEEFDRLLLLqKGGQTVYfgdlGENSHtiinyfekHGAP-- 1005
|
250
....*....|....*..
gi 490367952 235 KAPPAIQTASYFHQVIG 251
Cdd:TIGR00956 1006 KCPEDANPAEWMLEVIG 1022
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-216 |
1.03e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 58.69 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 123 ERARALLTrLGLAERIHYRP-SQLSGGQQQRVSIARALMNGGE---VILADEPTGALDSQSGKEVMAILKQLNQQGHTVI 198
Cdd:PRK00635 788 EKIHALCS-LGLDYLPLGRPlSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVV 866
|
90
....*....|....*...
gi 490367952 199 IVTHDPLIAQQADRIIEI 216
Cdd:PRK00635 867 IIEHNMHVVKVADYVLEL 884
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-228 |
1.54e-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: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMN-ILGCLDKPSSGEYKVAGQCVADMESDQlaALRRehfGFIF-----QRYHL 97
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQ--AIRA---GIAMvpedrKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 MAHLTAEQNVEIPAI--YAGKS---TEQRKERARALLTRLGLAERIHYRP-SQLSGGQQQRVSIARALMNGGEVILADEP 171
Cdd:TIGR02633 351 VPILGVGKNITLSVLksFCFKMridAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 172 TGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISDNNNH 228
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGDFVNH 488
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-221 |
1.76e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.03 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVSRLYTNGEEdtVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQLaalr 84
Cdd:TIGR00957 1285 VEFRNYCLRYREDLD--LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---- 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 REHFGFIFQRYHLMAHlTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQ----LSGGQQQRVSIARALM 160
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSG-SLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEggenLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 161 NGGEVILADEPTGALDSQSGKEVMAILKQlNQQGHTVIIVTHDPLIAQQADRIIEIKDGQI 221
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-203 |
1.77e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 1 MSALLELNNVS---RLYTNGEE---DTVV----------LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGE 64
Cdd:PRK13546 1 MNVSVNIKNVTkeyRIYRTNKErmkDALIpkhknktffaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 65 YKVAGQCvadmesdqlaalrrehfGFIFQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYRPSQ 144
Cdd:PRK13546 81 VDRNGEV-----------------SVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490367952 145 LSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD 203
Cdd:PRK13546 144 YSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHN 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-222 |
2.20e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 3 ALLELNNVSRLYTNGEEDTVV--LDQISLTINAGEMVAIIGASGSGKSTLMNILGC----LDKPSSGEYKVAGQCVADME 76
Cdd:TIGR00956 54 LLKILTRGFRKLKKFRDTKTFdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 77 SDqlaaLRRE---------HFGfifqryhlmaHLTAEQNVEIPAI-------YAGKSTEQRKERARAL-LTRLGLAeriH 139
Cdd:TIGR00956 134 KH----YRGDvvynaetdvHFP----------HLTVGETLDFAARcktpqnrPDGVSREEYAKHIADVyMATYGLS---H 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 140 YRPSQ--------LSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVThdplIAQQA- 210
Cdd:TIGR00956 197 TRNTKvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA----IYQCSq 272
|
250
....*....|....*...
gi 490367952 211 ------DRIIEIKDGQII 222
Cdd:TIGR00956 273 dayelfDKVIVLYEGYQI 290
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-202 |
5.31e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 5 LELNNVsRLYTNGEEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYkvagqCVADMESDQLAALR 84
Cdd:PTZ00265 383 IQFKNV-RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-----IINDSHNLKDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 85 --REHFGFIFQ-------------RYHL-----MAHLTAEQNVEIPAIYAGKSTEQRKERARA-----LLTRLGLAERIH 139
Cdd:PTZ00265 457 wwRSKIGVVSQdpllfsnsiknniKYSLyslkdLEALSNYYNEDGNDSQENKNKRNSCRAKCAgdlndMSNTTDSNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 140 YR--------------------------------------PSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGK 181
Cdd:PTZ00265 537 MRknyqtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260
....*....|....*....|..
gi 490367952 182 EVMAILKQLN-QQGHTVIIVTH 202
Cdd:PTZ00265 617 LVQKTINNLKgNENRITIIIAH 638
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-222 |
5.63e-08 |
|
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: 56.17 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 145 LSGGQQQRVSIARALM---NGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEI----- 216
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
....*..
gi 490367952 217 -KDGQII 222
Cdd:TIGR00630 910 dGGGTVV 916
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-214 |
6.19e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 30 TINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGE--------YKvaGQCVadmESDQlaalrrehfgfifqryhlmaHL 101
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEvdpelkisYK--PQYI---KPDY--------------------DG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 102 TAEQNVE-IPAIYAGK--STEqrkeraraLLTRLGLaERIHYRP-SQLSGGQQQRVSIARALMNGGEVILADEPTGALD- 176
Cdd:PRK13409 416 TVEDLLRsITDDLGSSyyKSE--------IIKPLQL-ERLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDv 486
|
170 180 190
....*....|....*....|....*....|....*....
gi 490367952 177 SQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRII 214
Cdd:PRK13409 487 EQRLAVAKAIRRIAEEREATALVVDHDiYMIDYISDRLM 525
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-214 |
9.73e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 9.73e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 145 LSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEV-MAILKQLNQQGHTVIIVTHDPLIAQQADRII 214
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIeKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
137-214 |
1.01e-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: 52.19 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 137 RIHYRPS--QLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGH-TVIIVTHDPLIAQQ-ADR 212
Cdd:cd03222 62 TPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYlSDR 141
|
..
gi 490367952 213 II 214
Cdd:cd03222 142 IH 143
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
117-224 |
1.53e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 117 STEQRKERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHT 196
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
90 100
....*....|....*....|....*....
gi 490367952 197 VIIVTHDPLIAQQ-ADRIIEIKDGQIISD 224
Cdd:NF000106 197 VLLTTQYMEEAEQlAHELTVIDRGRVIAD 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-203 |
1.67e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 6 ELNNVSRLYtngeEDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNI-LGCLdKPSSGEYKvagqCVADMES---DQL- 80
Cdd:PRK11147 321 EMENVNYQI----DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRIH----CGTKLEVayfDQHr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 AALRREHfgfifqryhlmahlTAEQNVEipaiyAGKSTEQRKERARALLTRLglaERIHYRPSQ-------LSGGQQQRV 153
Cdd:PRK11147 392 AELDPEK--------------TVMDNLA-----EGKQEVMVNGRPRHVLGYL---QDFLFHPKRamtpvkaLSGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490367952 154 SIARALMNGGEVILADEPTGALDSqsgkEVMAILKQL--NQQGhTVIIVTHD 203
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDV----ETLELLEELldSYQG-TVLLVSHD 496
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-219 |
3.17e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.86 E-value: 3.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 145 LSGGQQQRVSIARALMNG--GEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDG 219
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGPG 565
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-226 |
6.50e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVAGQCVADMESDQlaALrrEH-FGFIFQRYHLMAHLT 102
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--AL--ENgISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 103 AEQNVEIpAIYAGKS--TEQRK--ERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQ 178
Cdd:PRK10982 90 VMDNMWL-GRYPTKGmfVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490367952 179 SGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQIISDNN 226
Cdd:PRK10982 169 EVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQWIATQP 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-219 |
7.02e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 143 SQLSGGQQQRVSIARALMNGGE---VILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIKDG 219
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-219 |
7.95e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 34 GEMVAIIGASGSGKSTLMNILgcldkpssgeykvagqcvadmesdqLAALRREHFGFIFqryhlmahLTAeqnveipaiy 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL-------------------------ARELGPPGGGVIY--------IDG---------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 114 agksteqrkERARALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAI------L 187
Cdd:smart00382 39 ---------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 490367952 188 KQLNQQGHTVIIVTHDPLIAQQA------DRIIEIKDG 219
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLI 147
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
144-223 |
8.76e-07 |
|
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: 49.91 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 144 QLSGGQQQ------RVSIARALMNGGEVILADEPTGALDSQSGKEVMA-ILKQLNQQGH-TVIIVTHDPLIAQQADRIIE 215
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAeIIEERKSQKNfQLIVITHDEELVDAADHIYR 194
|
....*....
gi 490367952 216 I-KDGQIIS 223
Cdd:cd03240 195 VeKDGRQKS 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-221 |
1.72e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 37 VAIIGASGSGKSTLMNILGCLDKPSSGE-YKVAGQCVAdmesdqlaalrrehfgfIFQRYHLMAhLTAEQNveiPAIYAG 115
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTvFRSAKVRMA-----------------VFSQHHVDG-LDLSSN---PLLYMM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 116 KSTEQRKE-RARALLTRLGLAERIHYRPS-QLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSgkeVMAILKQLNQQ 193
Cdd:PLN03073 597 RCFPGVPEqKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLF 673
|
170 180
....*....|....*....|....*....
gi 490367952 194 GHTVIIVTHDP-LIAQQADRIIEIKDGQI 221
Cdd:PLN03073 674 QGGVLMVSHDEhLISGSVDELWVVSEGKV 702
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
118-216 |
1.93e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.18 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 118 TEQRKERARALL----TRLGLAERI--HY----RPSQ-LSGGQQQRVSIARA----LMNggeV--ILaDEPTGAL---DS 177
Cdd:COG0178 448 TEREAEIAERILkeirSRLGFLVDVglDYltldRSAGtLSGGEAQRIRLATQigsgLVG---VlyVL-DEPSIGLhqrDN 523
|
90 100 110
....*....|....*....|....*....|....*....
gi 490367952 178 QsgkEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEI 216
Cdd:COG0178 524 D---RLIETLKRLRDLGNTVIVVEHDEDTIRAADYIIDI 559
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
145-221 |
6.18e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 6.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490367952 145 LSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQI 221
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEmPELLGITDRILVMSNGLV 469
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-202 |
6.26e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGcldkpSSGEYKVAGQCVADMESDQLAALRREHFG-FIFqryhl 97
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLA-----GREDYEVTGGTVEFKGKDLLELSPEDRAGeGIF----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 mahLTAEQNVEIPAI-----YAGKSTEQRKERARALLTRLGLAERIHYRPSQL---------------SGGQQQRVSIAR 157
Cdd:PRK09580 82 ---MAFQYPVEIPGVsnqffLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490367952 158 ALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTH 202
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-222 |
6.67e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 23 VLDQISLTINAGEMVAIIGASGSGKSTLMNIL------GCLDK-------PSSGEY--KVAGQC-VADMESDQL------ 80
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrktgGYIEGdirisgfPKKQETfaRISGYCeQNDIHSPQVtvresl 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 81 ---AALR-------REHFGFIFQRYHLMaHLTAEQN--VEIPAIyAGKSTEQRKeraralltrlglaerihyrpsqlsgg 148
Cdd:PLN03140 975 iysAFLRlpkevskEEKMMFVDEVMELV-ELDNLKDaiVGLPGV-TGLSTEQRK-------------------------- 1026
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490367952 149 qqqRVSIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIA--QQADRIIEIK-DGQII 222
Cdd:PLN03140 1027 ---RLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDifEAFDELLLMKrGGQVI 1100
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
126-220 |
7.05e-06 |
|
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: 47.26 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 126 RALLTRLGLAERIHYRP-SQLSGGQQQRVSIARAL-------MNGG---EVILADEPTGALDSQSGKEVMAILKQLNQQG 194
Cdd:cd03279 104 RIVLLPQGEFDRFLARPvSTLSGGETFLASLSLALalsevlqNRGGarlEALFIDEGFGTLDPEALEAVATALELIRTEN 183
|
90 100
....*....|....*....|....*.
gi 490367952 195 HTVIIVTHDPLIAQQADRIIEIKDGQ 220
Cdd:cd03279 184 RMVGVISHVEELKERIPQRLEVIKTP 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-222 |
9.97e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 20 DTVVLDQISLTINAGEMVAIIGASGSGKSTL-MNILG-CLDKPSSGEYKVAGQ-----CVADMESDQLAALR--REHFGF 90
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrSYGRNISGTVFKDGKevdvsTVSDAIDAGLAYVTedRKGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 91 IF----QRYHLMAHLtaeqnveiPAIYAGKSTEQRKERAralltrlgLAERihYR-------PS------QLSGGQQQRV 153
Cdd:NF040905 352 NLiddiKRNITLANL--------GKVSRRGVIDENEEIK--------VAEE--YRkkmniktPSvfqkvgNLSGGNQQKV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 154 SIARALMNGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHD-PLIAQQADRIIEIKDGQII 222
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSElPELLGMCDRIYVMNEGRIT 483
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
95-217 |
1.19e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 95 YHLMAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIhyRPSQ-LSGGQQQRVSIARAL-------MNGGEVI 166
Cdd:TIGR00618 902 LYANVRLANQSEGRFHGRYADSHVNARKYQGLALLVADAYTGSV--RPSAtLSGGETFLASLSLALaladllsTSGGTVL 979
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490367952 167 ---LADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEIK 217
Cdd:TIGR00618 980 dslFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVK 1033
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-222 |
3.21e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.33 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 145 LSGGQQQRVSIARALM---NGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEI----- 216
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLgpegg 906
|
....*..
gi 490367952 217 -KDGQII 222
Cdd:COG0178 907 dGGGEIV 913
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-221 |
3.27e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 4 LLELNNVSRLYTngeeDTVVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYKVA-GQCVADMESDQLAA 82
Cdd:PRK10636 312 LLKMEKVSAGYG----DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 83 LRREHfgfifqryHLMAHLTAeqnveipaiYAGKSTEQrkeRARALLTRLGL-AERIHYRPSQLSGGQQQRVSIARALMN 161
Cdd:PRK10636 388 LRADE--------SPLQHLAR---------LAPQELEQ---KLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367952 162 GGEVILADEPTGALDSQSGKevmAILKQLNQQGHTVIIVTHDP-LIAQQADRIIEIKDGQI 221
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQ---ALTEALIDFEGALVVVSHDRhLLRSTTDDLYLVHDGKV 505
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-202 |
6.72e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 28 SLTINAGEMVAIIGASGSGKSTLMNILG----------C----LDKPSSGEYKVAGQCV--ADMESDQLaaLRREHFGFI 91
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipknCqilhVEQEVVGDDTTALQCVlnTDIERTQL--LEEEAQLVA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 92 FQRYHLMAHLTAEQNVEIPAIYAGKSTEQRKE----------------RARALLTRLGL-AERIHYRPSQLSGGQQQRVS 154
Cdd:PLN03073 275 QQRELEFETETGKGKGANKDGVDKDAVSQRLEeiykrlelidaytaeaRAASILAGLSFtPEMQVKATKTFSGGWRMRIA 354
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490367952 155 IARALMNGGEVILADEPTGALDSQSgkeVMAILKQLNQQGHTVIIVTH 202
Cdd:PLN03073 355 LARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSH 399
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
37-203 |
7.68e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 37 VAIIGASGSGKSTLMN-ILGCLDKPSSGEYKVAGQCVADMESDQLAALRREHFGFIF------------------QRYHL 97
Cdd:COG0419 26 NLIVGPNGAGKSTILEaIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRYrierrqgefaefleakpsERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 98 MAHLTAEQNVEIPAIYAGKSTEQRKERARALLTRLGLAERIHYR------PSQLSGGQQQRVSIARALmnggEVILaDep 171
Cdd:COG0419 106 LKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlsgldpIETLSGGERLRLALADLL----SLIL-D-- 178
|
170 180 190
....*....|....*....|....*....|..
gi 490367952 172 TGALDSQSGKEVMAILKQLNqqghtviIVTHD 203
Cdd:COG0419 179 FGSLDEERLERLLDALEELA-------IITHV 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-204 |
4.23e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 19 EDTVVLDqISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGE--YKvagqcvadmeSDQLAALRREHFGFIFQRYH 96
Cdd:PRK13541 12 EQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNiyYK----------NCNINNIAKPYCTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 97 LMAHLTAEQNVEIPA-IYAGKSTEQrkerarALLTRLGLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGAL 175
Cdd:PRK13541 81 LKLEMTVFENLKFWSeIYNSAETLY------AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180
....*....|....*....|....*....
gi 490367952 176 DSQSGKEVMAILKQLNQQGHTVIIVTHDP 204
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSHLE 183
|
|
| FtsX |
COG2177 |
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning]; |
513-633 |
8.12e-04 |
|
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441780 [Multi-domain] Cd Length: 292 Bit Score: 41.74 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 513 AEKTTQTMQLFLTLVAVISLVVGGIGVMNIML---VSVTERTREIGI-RMaVGARASDVMQQFLIESVLVCLVGGLLGIS 588
Cdd:COG2177 156 VERLFALLNLLRLVGLVLAALLLLAAVLLIGNtirLAIYSRREEIEImKL-VGATDGFIRRPFLLEGALLGLLGGLLALL 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 490367952 589 LSFAIAMFASMM----LPNWHFVFQPTALISAFACSTAIGVIFGFLPAR 633
Cdd:COG2177 235 LLALLYLLLVSAladgLAFLSLLSLGGLLLLLLLLLLLLGALLGALGSR 283
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
22-209 |
1.41e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 40.43 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 22 VVLDQISLTINAGEMVAIIGASGSGKSTLMNILGCLDKPSSGEYkvagqcvADMESDQLaALRREHFgfifqryhLMAHL 101
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDF-------IGLRGDAL-PLGANSF--------ILPGL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 102 TAEQNVEIPAIYAGKSTEQRKERARALLTrlgLAERIHYRPSQLSGGQQQRVSIARALMNGGEVILADEPTGALDSQSGK 181
Cdd:PRK15177 65 TGEENARMMASLYGLDGDEFSHFCYQLTQ---LEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQL 141
|
170 180
....*....|....*....|....*....
gi 490367952 182 EVMAILK-QLNQQGhtVIIVTHDPLIAQQ 209
Cdd:PRK15177 142 RMQAALAcQLQQKG--LIVLTHNPRLIKE 168
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
24-54 |
1.92e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|..
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMN-IL 54
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTL 656
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-54 |
2.82e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 2.82e-03
10 20 30
....*....|....*....|....*....|..
gi 490367952 24 LDQISLTINAGEMVAIIGASGSGKSTLMN-IL 54
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
145-222 |
9.90e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367952 145 LSGGQQQRVSIARALM---NGGEVILADEPTGALDSQSGKEVMAILKQLNQQGHTVIIVTHDPLIAQQADRIIEI----- 216
Cdd:PRK00349 831 LSGGEAQRVKLAKELSkrsTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLgpegg 910
|
....*..
gi 490367952 217 -KDGQII 222
Cdd:PRK00349 911 dGGGEIV 917
|
|
| |
