|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-664 |
0e+00 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 829.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLAR 84
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 LRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNG 164
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 165 GDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEIISDRPNVPDQAAEpGNSDPDA 244
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVA-GGTEPVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 245 APAlqgkqkkgksiSAWRSTLDRLSEAFQMALLSMNAHRMRTFLTMLGIIIGIASVVTVVALGKGSQQQILSNISSLGTN 324
Cdd:PRK10535 242 NTA-----------SGWRQFVSGFREALTMAWRAMAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRAIGTN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 325 TITVFQGRGFGDNSKTaNFKTLVPADADALMTQPYVSAVSPIVSTSKTMRYQQNEANATINGVSNDYFDVKGLVFKDGQT 404
Cdd:PRK10535 311 TIDIYPGKDFGDDDPQ-YQQALKYDDLIAIQKQPWVASATPAVSQSLRLRYGNIDVAASANGVSGDYFNVYGMTFSEGNT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 405 FDQRSVRDRSQDVVIDTNTQKQFFGDGSNPIGQVVLLGSVPARIIGIVEPQTSGMGSDDTLNVYMPYTTVMSRMLGQSNV 484
Cdd:PRK10535 390 FNQEQLNGRAQVVVLDSNTRRQLFPHKADVVGEVILVGNMPATVIGVAEEKQSMFGSSKVLRVWLPYSTMSGRVMGQSWL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 485 RNIVVRINDKYSTAAAENAIVNLLTQRHGAQDIFTMNSDSIRQTIEKTTSTMTLLVSAIAVISLVVGGIGVMNIMLVSVT 564
Cdd:PRK10535 470 NSITVRVKEGYDSAEAEQQLTRLLTLRHGKKDFFTWNMDSVLKTAEKTTRTLQLFLTLVAVISLVVGGIGVMNIMLVSVT 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 565 ERTQEIGVRMAVGARQSDILQQFLIEAILVCLIGGVLGVLLSLGLGQLINKFAGGnFSVAYSSTSIIAAFVCSTLIGVVF 644
Cdd:PRK10535 550 ERTREIGIRMAVGARASDVLQQFLIEAVLVCLVGGALGITLSLLIAFTLQLFLPG-WEIGFSPLALLSAFLCSTVTGILF 628
|
650 660
....*....|....*....|
gi 491444527 645 GFLPAKNAAKLDPVAALSRE 664
Cdd:PRK10535 629 GWLPARNAARLDPVDALARE 648
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-226 |
1.02e-118 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 353.19 E-value: 1.02e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMN 163
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKNATRIIEISDGEIISD 226
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-223 |
1.63e-107 |
|
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: 324.06 E-value: 1.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| SalY |
COG0577 |
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms]; |
270-664 |
1.92e-87 |
|
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
Pssm-ID: 440342 [Multi-domain] Cd Length: 339 Bit Score: 276.78 E-value: 1.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 270 EAFQMALLSMNAHRMRTFLTMLGIIIGIASVVTVVALGKGSQQQILSNISSLGTNTITVFQGRGFgdnsktaNFKTLVPA 349
Cdd:COG0577 1 EYLRLALRSLRRNKLRSLLTVLGIAIGIALVIAILALGRGLRRSLLRDLDSLGFDLLTVSRTPGG-------SRATLSYE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 350 DA-DALMTQPYVSAVSPIVSTSKTMRYQQNE-ANATINGVSNDYFDVKGLVFKDGQTFDQRSVRDRSQDVVIDTNTQKQF 427
Cdd:COG0577 74 DLrEALRALPGVESVAPSSSGSATVRYGGGEpPSVRVLGVDPDYFRVLGIPLLAGRFFTAADDLGAPPVVVIGEALARRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 428 FGdGSNPIGQVVLLGSVPARIIGIVEPQtsgmgsddtlnvympyttvmsrmlgqsnvrnivvrindkystaaaenaIVNL 507
Cdd:COG0577 154 FG-GEDPVGKTIRLNGRPFTVVGVVEAE------------------------------------------------LRAL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 508 LTQRHGAQDIFTMNSDSIRQTIEKTTSTMTLLVSAIAVISLVVGGIGVMNIMLVSVTERTQEIGVRMAVGARQSDILQQF 587
Cdd:COG0577 185 LRRRDPGDDFEVQTLDEILAALYGVLRTLTLLLGAIAGLALLVACIGIMNLMLASVTERTREIGIRKALGASRRDILRQF 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 588 LIEAILVCLIGGVLGVLLSLGLGQLINKFAGgnFSVAYSSTSIIAAFVCSTLIGVVFGFLPAKNAAKLDPVAALSRE 664
Cdd:COG0577 265 LTEALLLALLGGLLGLLLALLLLRLLAALLG--LPVSLDPWVLLLALALSLLVGLLAGLYPARRAARLDPVEALRSE 339
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
5.76e-80 |
|
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: 253.51 E-value: 5.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 2 TKQALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQ 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 82 LARLRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVtpSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARAL 161
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 162 MNGGDVILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDMQVAKNATRIIEISDGEIISDRP 228
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-229 |
2.62e-73 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 235.72 E-value: 2.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 ReYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:COG2884 79 R-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEIISDRPN 229
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElVDRMPKRVLELEDGRLVRDEAR 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-228 |
4.31e-66 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 217.62 E-value: 4.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGEstiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLAR 84
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 LRREyFGFIFQRYHLLGDLSAEGNV------EVPAVYA--GVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVS 156
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRSllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 157 IARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEIISDRP 228
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGP 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-224 |
3.98e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 215.33 E-value: 3.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:COG1135 82 RK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-224 |
6.71e-64 |
|
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: 211.29 E-value: 6.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
22-218 |
2.75e-62 |
|
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: 205.93 E-value: 2.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 22 TIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREYFGFIFQRYHLLG 101
Cdd:TIGR03608 10 DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 DLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHS 181
Cdd:TIGR03608 90 NETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKN 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 491444527 182 GVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEI 218
Cdd:TIGR03608 170 RDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-205 |
1.10e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 206.09 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MT-KQALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEP 79
Cdd:COG1116 1 MSaAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 80 DqlarlrreyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIAR 159
Cdd:COG1116 81 D---------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 160 ALMNGGDVILADEPTGALDS----HSGVEVMRILRELNAaghTIILVTHD 205
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDAltreRLQDELLRLWQETGK---TVLFVTHD 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-228 |
8.38e-60 |
|
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: 200.49 E-value: 8.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEstiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLGDLSAEGNVEVPA--------VYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIA 158
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 159 RALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAK-NATRIIEISDGEIISDRP 228
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-228 |
6.31e-59 |
|
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: 206.68 E-value: 6.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 2 TKQALLEVSNLVREFPA-GESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLRREyFGFIFQR-YHLL------GDLSAEGnvevPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQ 152
Cdd:COG1123 336 SLRELRRR-VQMVFQDpYSSLnprmtvGDIIAEP----LRLHGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQR 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 153 QRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEIISDRP 228
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-206 |
1.02e-58 |
|
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: 196.92 E-value: 1.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlarlr 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyfGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLgTKTLNR-PSQLSGGQQQRVSIARALMNGG 165
Cdd:cd03293 76 ----GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGL-SGFENAyPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491444527 166 DVILADEPTGALDSHS----GVEVMRILRElnaAGHTIILVTHDM 206
Cdd:cd03293 151 DVLLLDEPFSALDALTreqlQEELLDIWRE---TGKTVLLVTHDI 192
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-233 |
1.25e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 197.14 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGkLEPDQLARL 85
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREyFGFIFQRYHLLGDLSAEGNVEVPAVYA-GVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNG 164
Cdd:COG1126 76 RRK-VGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 165 GDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEIISDRPnvPDQ 233
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP--PEE 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-223 |
1.31e-58 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 196.96 E-value: 1.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMN 163
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-224 |
1.87e-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: 191.18 E-value: 1.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLePDQLARL 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREYFGFIFQ-------RYHLLGDLSAEGnveVPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQQRVSI 157
Cdd:cd03257 80 RRKEIQMVFQdpmsslnPRMTIGEQIAEP---LRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 158 ARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-228 |
1.90e-56 |
|
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: 191.74 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGEstiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREyFGFIFQRYHLLGDLSAEGNVEVPAVYA--------GVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSI 157
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVLHGRLGYkptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 158 ARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEIISDRP 228
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGA 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-223 |
1.40e-55 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 188.83 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARA 160
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 161 LMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-222 |
1.63e-55 |
|
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: 188.23 E-value: 1.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGE 222
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
24-223 |
1.85e-54 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 185.31 E-value: 1.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREYFGFIFQRYHLLGDL 103
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQSFNLIPHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGV 183
Cdd:NF038007 99 SIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491444527 184 EVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:NF038007 179 AVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-226 |
2.18e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 185.65 E-value: 2.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLr 86
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyfGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKtLNRP-SQLSGGQQQRVSIARALMNGG 165
Cdd:COG1131 76 ----GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDA-ADRKvGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEIISD 226
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEeAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-222 |
2.24e-53 |
|
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: 182.28 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 8 EVSNLVREFPAGEStiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARlrr 87
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 88 eYFGFIFQ--RYHLLGDlSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:cd03225 76 -KVGLVFQnpDDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGE 222
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-226 |
1.34e-52 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 180.61 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEstiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlepDQLARLR 86
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQryhllgdlsaegNVEV----PAVYA---------GVTPSERKQRATALLTELGLGTKtLNR-PSQLSGGQQ 152
Cdd:COG1122 75 RK-VGLVFQ------------NPDDqlfaPTVEEdvafgpenlGLPREEIRERVEEALELVGLEHL-ADRpPHELSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 153 QRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEIISD 226
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDGRIVAD 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-224 |
4.69e-52 |
|
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: 179.79 E-value: 4.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:COG1127 3 EPMIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLRREyFGFIFQRYHLLGDLSAEGNVEVP-AVYAGVTPSERKQRATALLTELGL-GTKTLnRPSQLSGGQQQRVSIARAL 161
Cdd:COG1127 79 ELRRR-IGMLFQGGALFDSLTVFENVAFPlREHTDLSEAEIRELVLEKLELVGLpGAADK-MPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 162 MNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-223 |
1.11e-51 |
|
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: 177.99 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEI 223
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKElVDTTRHRVIALERGKL 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-223 |
1.17e-51 |
|
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: 177.72 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlEPDQLARLR 86
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLGDLSAEGNVEVPAVYA-GVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:cd03262 76 QK-VGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEI 223
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-224 |
1.50e-49 |
|
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: 172.69 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:cd03261 1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLGDLSAEGNVEVP-AVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDtAFAIADRIAVLYDGKIV 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-224 |
1.51e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 176.14 E-value: 1.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 8 EVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRR 87
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 88 EyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDV 167
Cdd:PRK11153 83 Q-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 168 ILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-228 |
1.46e-48 |
|
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: 172.93 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDRP--TSGSYKVSGQETGKLEPDQL 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 ARLRREYFGFIFQ------------RYHLlgdlsaegnVEVPAVYAGVTPSERKQRATALLTELGL--GTKTLNR-PSQL 147
Cdd:COG0444 81 RKIRGREIQMIFQdpmtslnpvmtvGDQI---------AEPLRIHGGLSKAEARERAIELLERVGLpdPERRLDRyPHEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 148 SGGQQQRVSIARALMNGGDVILADEPTGALDshsgV----EVMRILRELNAA-GHTIILVTHDMQVAKN---------AT 213
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALD----VtiqaQILNLLKDLQRElGLAILFITHDLGVVAEiadrvavmyAG 227
|
250
....*....|....*
gi 491444527 214 RIIEISDGEIISDRP 228
Cdd:COG0444 228 RIVEEGPVEELFENP 242
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-228 |
1.00e-47 |
|
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: 168.06 E-value: 1.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlepdqlaRL 85
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR-------RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREYFG---FIFQRY-------HLLGDLSAEgnvevPAVYAGVTpsERKQRATALLTELGLGTKTLNR-PSQLSGGQQQR 154
Cdd:COG1124 74 RKAFRRrvqMVFQDPyaslhprHTVDRILAE-----PLRIHGLP--DREERIAELLEQVGLPPSFLDRyPHQLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQV-AKNATRIIEISDGEIISDRP 228
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVvAHLCDRVAVMQNGRIVEELT 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-228 |
1.87e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 167.19 E-value: 1.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETgkLEPDQLARL 85
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREYFGFIFQRYHLLGDLSAEGNVEV-PAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNG 164
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 165 GDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVA-KNATRIIEISDGEIISDRP 228
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGD 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-224 |
3.06e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 166.73 E-value: 3.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE---TGKLEPDQLARLRREyFGFIFQRYHLL 100
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRLLRQK-VGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 101 GDLSAEGN-VEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDS 179
Cdd:COG4161 95 PHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 180 HSGVEVMRILRELNAAGHTIILVTHDMQVA-KNATRIIEISDGEII 224
Cdd:COG4161 175 EITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRII 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-224 |
8.34e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 165.57 E-value: 8.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE---TGKLEPDQLARLRREyFGFIFQRYHLL 100
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAIRELRRN-VGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 101 GDLSAEGN-VEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDS 179
Cdd:PRK11124 95 PHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 180 HSGVEVMRILRELNAAGHTIILVTHDMQVA-KNATRIIEISDGEII 224
Cdd:PRK11124 175 EITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIV 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-223 |
9.40e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.22 E-value: 9.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlR 86
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLGDlSAEGNVEVPAVYAGVTPSErkQRATALLTELGLGTKTLNRP-SQLSGGQQQRVSIARALMNGG 165
Cdd:COG4619 74 RQ-VAYVPQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDM-QVAKNATRIIEISDGEI 223
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAeEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
1.97e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 167.97 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKqALLEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:COG3842 1 MAM-PALELENVSKRY--GDVTA--LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QlarlRReyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARA 160
Cdd:COG3842 76 K----RN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 161 LMNGGDVILADEPTGALDSHS----GVEVMRILRELnaaGHTIILVTHD------MqvaknATRIIEISDGEII 224
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLreemREELRRLQREL---GITFIYVTHDqeealaL-----ADRIAVMNDGRIE 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
2.66e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 164.59 E-value: 2.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQA--LLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE----- 73
Cdd:COG4598 1 MTDTAppALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEirlkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 74 --TGKLEP---DQLARLRREyFGFIFQRYHLLGDLSAEGNV-EVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQL 147
Cdd:COG4598 77 drDGELVPadrRQLQRIRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 148 SGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEI 223
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDvSSHVVFLHQGRI 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
2.20e-45 |
|
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: 169.31 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTL-MNILGCLDRP--TSGSYKVSGQETGKLEPd 80
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPA--VDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGgrISGEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 qlaRLRREYFGFIFQRY-HLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIAR 159
Cdd:COG1123 79 ---ALRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 160 ALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDM-QVAKNATRIIEISDGEIISDRP 228
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGP 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-223 |
3.95e-45 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 160.43 E-value: 3.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREyFGFIFQRYHLLGDL 103
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGV 183
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491444527 184 EVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEI 223
Cdd:PRK10908 175 GILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHL 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-228 |
4.52e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 161.07 E-value: 4.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGestiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE--TGKLEPDQL 82
Cdd:PRK11264 2 SAIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 ARLR--REYFGFIFQRYHLLGDLSAEGNV-EVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIAR 159
Cdd:PRK11264 78 GLIRqlRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 160 ALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEIISDRP 228
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-228 |
3.82e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 158.33 E-value: 3.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGcLDRPTSGSYKVSGQEtgklep 79
Cdd:COG1121 1 MMMMPAIELENLTVSY--GGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG-LLPPTSGTVRLFGKP------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 80 dqlARLRREYFGFIFQRYHLLGD--LSAEgnvEVpaVYAGVTPS---------ERKQRATALLTELGLgTKTLNRP-SQL 147
Cdd:COG1121 70 ---PRRARRRIGYVPQRAEVDWDfpITVR---DV--VLMGRYGRrglfrrpsrADREAVDEALERVGL-EDLADRPiGEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 148 SGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLgAVREYFDRVLLLNRGLVAHG 220
|
..
gi 491444527 227 RP 228
Cdd:COG1121 221 PP 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-222 |
1.30e-43 |
|
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: 154.65 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 ReyFGFIFQRYHLLGDLSAEGNVEVPavyagvtpserkqratalltelglgtktlnrpsqLSGGQQQRVSIARALMNGGD 166
Cdd:cd03229 77 R--IGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDMQVAKN-ATRIIEISDGE 222
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-224 |
2.52e-43 |
|
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: 154.98 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlarlR 86
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 ReyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTkTLNR-PSQLSGGQQQRVSIARALMNGG 165
Cdd:cd03259 73 N--IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG-LLNRyPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVA-KNATRIIEISDGEII 224
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEAlALADRIAVMNEGRIV 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-228 |
3.09e-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: 155.42 E-value: 3.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpaGEstIQILKGIDLTIYEGELVAIVGQSGSGKSTLmniLGCLDR--------PTSGSYKVSGQETGKLE 78
Cdd:cd03260 1 IELRDLNVYY--GD--KHALKDISLDIPKGEITALIGPSGCGKSTL---LRLLNRlndlipgaPDEGEVLLDGKDIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 79 PDQLArLRREyFGFIFQRYHLLgDLSAEGNVEVPAVYAGVTP-SERKQRATALLTELGLGTKTLNR--PSQLSGGQQQRV 155
Cdd:cd03260 74 VDVLE-LRRR-VGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 156 SIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAgHTIILVTHDM-QVAKNATRIIEISDGEIISDRP 228
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMqQAARVADRTAFLLNGRLVEFGP 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-224 |
1.03e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 157.62 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgkLEPDQLARLR 86
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD---LFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 ReyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLgTKTLNR-PSQLSGGQQQRVSIARALMNGG 165
Cdd:COG1118 76 R--VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQL-EGLADRyPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHD----MQVAKnatRIIEISDGEII 224
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDqeeaLELAD---RVVVMNQGRIE 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-223 |
5.61e-42 |
|
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: 155.58 E-value: 5.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQla 83
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 rlrREYfGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMN 163
Cdd:TIGR03265 76 ---RDY-GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEI 223
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSmADRIVVMNHGVI 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-226 |
6.00e-42 |
|
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: 152.51 E-value: 6.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLvrEFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:COG1120 1 MLEAENL--SVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RreyfGFIFQRYHLLGDLSAEgnvEVpaVYAGVTP---------SERKQRATALLTELGLGTKtLNRP-SQLSGGQQQRV 155
Cdd:COG1120 77 I----AYVPQEPPAPFGLTVR---EL--VALGRYPhlglfgrpsAEDREAVEEALERTGLEHL-ADRPvDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 156 SIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-224 |
1.61e-41 |
|
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: 150.91 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGESTiqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPdqlARLR 86
Cdd:cd03295 1 IEFENVTKRYGGGKKA---VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP---VELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLGDLSAEGNVE-VPAVyAGVTPSERKQRATALLTELGLGTKTL-NR-PSQLSGGQQQRVSIARALMN 163
Cdd:cd03295 75 RK-IGYVIQQIGLFPHMTVEENIAlVPKL-LKWPKEKIRERADELLALVGLDPAEFaDRyPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 164 GGDVILADEPTGALD----SHSGVEVMRILRELnaaGHTIILVTHDMQVA-KNATRIIEISDGEII 224
Cdd:cd03295 153 DPPLLLMDEPFGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAfRLADRIAIMKNGEIV 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
25-224 |
3.40e-41 |
|
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: 149.22 E-value: 3.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLdRPTSGSYKVSGQEtgklepdqlARLRREYFGFIFQRYHLLGD- 102
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFGKP---------LEKERKRIGYVPQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 -LSAEGNVE---VPAVYAGVTPS-ERKQRATALLTELGLgTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGA 176
Cdd:cd03235 84 pISVRDVVLmglYGHKGLFRRLSkADKAKVDEALERVGL-SELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 177 LDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEIsDGEII 224
Cdd:cd03235 163 VDPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLLL-NRTVV 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-228 |
4.64e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 152.58 E-value: 4.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFPAGES-------TIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE 73
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGlfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 74 TGKLEPDQLARLRREyFGFIFQ--------RyHLLGDLSAEGnvevPAVYAGVTPSERKQRATALLTELGLGTKTLNR-P 144
Cdd:COG4608 82 ITGLSGRELRPLRRR-MQMVFQdpyaslnpR-MTVGDIIAEP----LRIHGLASKAERRERVAELLELVGLRPEHADRyP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 145 SQLSGGQQQRVSIARALMNGGDVILADEPTGALDshsgV----EVMRILRELNAA-GHTIILVTHDMQVAKNAT------ 213
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALD----VsiqaQVLNLLEDLQDElGLTYLFISHDLSVVRHISdrvavm 231
|
250
....*....|....*...
gi 491444527 214 ---RIIEISDGEIISDRP 228
Cdd:COG4608 232 ylgKIVEIAPRDELYARP 249
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-223 |
1.37e-40 |
|
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: 146.00 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPagesTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlarlr 86
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEGNVEvpavyagvtpserkqratalltelglgtktlnrpsqLSGGQQQRVSIARALMNGGD 166
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEI 223
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-226 |
1.94e-40 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 147.97 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpAGestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLr 86
Cdd:cd03219 1 LEVRGLTKRF-GG---LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyfGFI--FQRYHLLGDLSAEGNVEVPA--------VYAGVTPSERK--QRATALLTELGLGTKtLNRP-SQLSGGQQQ 153
Cdd:cd03219 76 ----GIGrtFQIPRLFPELTVLENVMVAAqartgsglLLARARREEREarERAEELLERVGLADL-ADRPaGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 154 RVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEIISD 226
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDvVMSLADRVTVLDQGRVIAE 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-223 |
4.60e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.22 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlar 84
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 lRReyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLgTKTLNR-PSQLSGGQQQRVSIARALMN 163
Cdd:COG3839 75 -RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGL-EDLLDRkPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 164 GGDVILADEPTGALDSHSGVEvMRI-LRELNAA-GHTIILVTHD----MQVaknATRIIEISDGEI 223
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVE-MRAeIKRLHRRlGTTTIYVTHDqveaMTL---ADRIAVMNDGRI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-224 |
1.14e-39 |
|
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: 146.63 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREYFGFIFQRYHLLGDLSAEGN 108
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 109 VEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALD----SHSGVE 184
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491444527 185 VMRILRELnaaGHTIILVTHDMQVA-KNATRIIEISDGEII 224
Cdd:cd03294 203 LLRLQAEL---QKTIVFITHDLDEAlRLGDRIAIMKDGRLV 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-224 |
1.18e-39 |
|
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: 153.30 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKS-TLMNILGCLDRP---TSGSYKVSGQETGK 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 77 LEPDQLARLRREYFGFIFQR-------YHLLGDLSAegnvEVPAVYAGVTPSERKQRATALLTELGL--GTKTLNR-PSQ 146
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEpmtslnpLHTIGKQIA----EVLRLHRGLSGAAARARALELLERVGIpdPERRLDAyPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 147 LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGvVRRFADRVAVMRQGEIV 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-224 |
1.27e-39 |
|
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: 153.38 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEstiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlr 86
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEgNVevpAVYA-GVTPSE-----RKQRATALLTEL--GLGTKTLNRPSQLSGGQQQRVSIA 158
Cdd:COG4988 410 RRQIAWVPQNPYLFAGTIRE-NL---RLGRpDASDEEleaalEAAGLDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 159 RALMNGGDVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-233 |
1.60e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 145.88 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQET-------GKL---EPDQLaRLRREYFGFI 93
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLkvaDKNQL-RLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 94 FQRYHLLGDLSAEGNV-EVPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQQRVSIARALMNGGDVILAD 171
Cdd:PRK10619 98 FQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 172 EPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEIISDRPnvPDQ 233
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGA--PEQ 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-174 |
1.71e-39 |
|
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: 142.02 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgkLEPDQLARLRREyFGFIFQRYHLLGDLSA 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 106 EGNVEVPAVYAGVTPSERKQRATALLTELGLG----TKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-222 |
2.11e-39 |
|
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: 142.52 E-value: 2.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 19 GESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYH 98
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 99 LLGDLSAEgNVevpavyagvtpserkqratalltelglgtktlnrpsqLSGGQQQRVSIARALMNGGDVILADEPTGALD 178
Cdd:cd03228 87 LFSGTIRE-NI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491444527 179 SHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGE 222
Cdd:cd03228 129 PETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-222 |
2.42e-39 |
|
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: 142.00 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 8 EVSNLVREFPAGestiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrR 87
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 88 EYFGFIFQryhllgdlsaegnvevpavyagvtpserkqratalltelglgtktlnrpsqLSGGQQQRVSIARALMNGGDV 167
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 168 ILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNAT-RIIEISDGE 222
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-226 |
2.99e-39 |
|
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: 145.18 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFpaGEstIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:COG0411 2 DPLLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RL---RreyfgfIFQRYHLLGDLSAEGNVEVPAVYAG---------VTPSERKQ------RATALLTELGLGTKTLNRPS 145
Cdd:COG0411 78 RLgiaR------TFQNPRLFPELTVLENVLVAAHARLgrgllaallRLPRARREereareRAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 146 QLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEI 223
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDlVMGLADRIVVLDFGRV 231
|
...
gi 491444527 224 ISD 226
Cdd:COG0411 232 IAE 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-223 |
5.04e-39 |
|
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: 143.92 E-value: 5.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlarlR 86
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 ReyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03300 73 P--VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 167 VILADEPTGALD----SHSGVEVMRILRELnaaGHTIILVTHDMQVAKN-ATRIIEISDGEI 223
Cdd:cd03300 151 VLLLDEPLGALDlklrKDMQLELKRLQKEL---GITFVFVTHDQEEALTmSDRIAVMNKGKI 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-216 |
9.07e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 143.85 E-value: 9.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlar 84
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 lrreyfGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNG 164
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 165 GDVILADEPTGALDSHSGvEVMR--ILRELNAAGHTIILVTHDMQVAKN-ATRII 216
Cdd:COG4525 153 PRFLLMDEPFGALDALTR-EQMQelLLDVWQRTGKGVFLITHSVEEALFlATRLV 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-226 |
1.51e-38 |
|
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: 143.72 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPagESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETgkLEPDQLARLR 86
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQryhllgdlsaegNVE---VPAVYA----------GVTPSERKQRATALLTELGLgTKTLNR-PSQLSGGQQ 152
Cdd:TIGR04520 77 KK-VGMVFQ------------NPDnqfVGATVEddvafglenlGVPREEMRKRVDEALKLVGM-EDFRDRePHLLSGGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 153 QRVSIARAL-MNgGDVILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDMQVAKNATRIIEISDGEIISD 226
Cdd:TIGR04520 143 QRVAIAGVLaMR-PDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-224 |
2.83e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 144.08 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlRREyFGFIFQRYHLLGDLSA 105
Cdd:COG1125 18 VDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RRR-IGYVIQQIGLFPHMTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 106 EGNVEVPAVYAGVTPSERKQRATALLTELGLGTKT-LNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALD----S 179
Cdd:COG1125 94 AENIATVPRLLGWDKERIRARVDELLELVGLDPEEyRDRyPHELSGGQQQRVGVARALAADPPILLMDEPFGALDpitrE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 180 HSGVEVMRILRELnaaGHTIILVTHDMQVA-KNATRIIEISDGEII 224
Cdd:COG1125 174 QLQDELLRLQREL---GKTIVFVTHDIDEAlKLGDRIAVMREGRIV 216
|
|
| MacB_PCD |
pfam12704 |
MacB-like periplasmic core domain; This family represents the periplasmic core domain found in ... |
286-507 |
3.66e-38 |
|
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: 140.74 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 286 TFLTMLGIIIGIASVVTVVALGKGSQQQILSNISSLGtNTITVFQGRGFGDNSktanFKTLVPADADALMTQPYVSAVSP 365
Cdd:pfam12704 1 TALTVLGIAIGVAAVIAILSLGDGLLSAVPEQISDSD-NLVVVQPGAAGGGGT----RPPLSDPDAEALRRAVPVEAVAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 366 IVSTSkTMRYQQNEANATINGVSNDYFDVKGLVFKDGQTFDQRSVRDRSQDVVIDTNTQKQFFGDGsNPIGQVVLLGSVP 445
Cdd:pfam12704 76 VVSTV-RYGNSTTERLVTVVGVDPDFFKVFGLPLAEGRFFTEADVLGGPNVVVLGESLAEKLFGGD-DPVGKTIRLNGQP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 446 ARIIGIVEPQTSGMGSDDTlnVYMPYTTVMSRMlgQSNVRNIVVRINDKYSTAAAENAIVNL 507
Cdd:pfam12704 154 FTVVGVLPDFPGSDGGGDL--VYVPLTTLQRRL--GDSVSTILVRLKDGADLAAAAAELRAL 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-231 |
5.31e-38 |
|
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: 141.32 E-value: 5.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPdqlarlR 86
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV------Q 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEGNV----EVPAVYAGVTPSERKQRATALLTELGLgTKTLNR-PSQLSGGQQQRVSIARAL 161
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVafglRVKPRSERPPEAEIRAKVHELLKLVQL-DWLADRyPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 162 MNGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHD----MQVAK-----NATRIIEISDGEIISDRPNVP 231
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDqeeaLEVADrvvvmNKGRIEQVGTPDEVYDHPASP 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-224 |
6.95e-38 |
|
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: 140.76 E-value: 6.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 rreyfGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGtKTLNRP-SQLSGGQQQRVSIARALMNG 164
Cdd:COG4555 77 -----GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLE-EFLDRRvGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 165 GDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQeVEALCDRVVILHKGKVV 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-221 |
4.78e-37 |
|
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: 137.95 E-value: 4.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFP---AGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNilgCLDR---PTSGS--YKVSGQET- 74
Cdd:COG4778 2 TTLLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLK---CIYGnylPDSGSilVRHDGGWVd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 75 -GKLEPDQLARLRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLgtktlnrPSQL------ 147
Cdd:COG4778 79 lAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 148 --SGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQV-AKNATRIIEISDG 221
Cdd:COG4778 152 tfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVrEAVADRVVDVTPF 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-224 |
8.20e-37 |
|
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: 137.12 E-value: 8.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEStiqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlEPDQLarlr 86
Cdd:cd03265 1 IEVENLVKKYGDFEA----VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVA-KNATRIIEISDGEII 224
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAeQLCDRVAIIDHGRII 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-226 |
8.57e-37 |
|
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: 135.64 E-value: 8.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRreyfGFIFQryhllgdl 103
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI----AYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 saegnvevpavyagvtpserkqrataLLTELGLGTKtLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:cd03214 81 --------------------------ALELLGLAHL-ADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 183 VEVMRILRELNAA-GHTIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:cd03214 134 IELLELLRRLARErGKTVVMVLHDLnLAARYADRVILLKDGRIVAQ 179
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-220 |
1.04e-36 |
|
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: 136.45 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDqlar 84
Cdd:COG4133 1 MMLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 lRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERkqRATALLTELGLgTKTLNRP-SQLSGGQQQRVSIARALMN 163
Cdd:COG4133 73 -YRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGL-AGLADLPvRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDmQVAKNATRIIEISD 220
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ-PLELAAARVLDLGD 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-224 |
1.33e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 144.91 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 3 KQALLEVSNLVREFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQL 82
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 arlrREYFGFIFQRYHLLGDlSAEGNVEVpaVYAGVTPSE-----RKQRATALLTEL--GLGTKTLNRPSQLSGGQQQRV 155
Cdd:COG4987 408 ----RRRIAVVPQRPHLFDT-TLRENLRL--ARPDATDEElwaalERVGLGDWLAALpdGLDTWLGEGGRRLSGGERRRL 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 156 SIARALMNGGDVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-226 |
1.64e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 139.07 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEST-IQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSY----------KVSGQETG 75
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 76 KLEPDQLARLR----------REYFGFIFQ--RYHLLgDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR 143
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 144 -PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDG 221
Cdd:PRK13651 162 sPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDG 241
|
....*
gi 491444527 222 EIISD 226
Cdd:PRK13651 242 KIIKD 246
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-224 |
6.20e-36 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 134.31 E-value: 6.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 8 EVSNLVREFPAGEStiqILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGklepdqlARLRR 87
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 88 EYFGFIFQ--RYHLLGDlsaegnvevpAVYAGVTPS-----ERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARA 160
Cdd:cd03226 71 KSIGYVMQdvDYQLFTD----------SVREELLLGlkeldAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 161 LMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-226 |
1.04e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 135.53 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGestiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCL---DRPTSGSYKVSG---QETGKL 77
Cdd:PRK09984 2 QTIIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGrtvQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 78 EPDqlARLRREYFGFIFQRYHLLGDLSAEGNVEVPAVyaGVTP----------SERKQRATALLTELGLGTKTLNRPSQL 147
Cdd:PRK09984 78 ARD--IRKSRANTGYIFQQFNLVNRLSVLENVLIGAL--GSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 148 SGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVA-KNATRIIEISDGEIIS 225
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAlRYCERIVALRQGHVFY 233
|
.
gi 491444527 226 D 226
Cdd:PRK09984 234 D 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-224 |
3.72e-35 |
|
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: 132.63 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlEPDQLarlr 86
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA--VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-224 |
4.59e-35 |
|
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: 139.82 E-value: 4.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFP-------AGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTL-MNILGCLdrPTSGSYKVSGQETGKL 77
Cdd:COG4172 275 LLEARDLKVWFPikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 78 EPDQLARLRREyFGFIFQ--------RyHLLGDLSAEGnVEVPAVyaGVTPSERKQRATALLTELGLGTKTLNR-PSQLS 148
Cdd:COG4172 353 SRRALRPLRRR-MQVVFQdpfgslspR-MTVGQIIAEG-LRVHGP--GLSAAERRARVAEALEEVGLDPAARHRyPHEFS 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 149 GGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRAlAHRVMVMKDGKVV 505
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-228 |
4.86e-35 |
|
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: 141.51 E-value: 4.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVreFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlr 86
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDlSAEGNVevpAVYAGVTPSERKQRATAL--LTE------LGLGTKTLNRPSQLSGGQQQRVSIA 158
Cdd:COG2274 548 RRQIGVVLQDVFLFSG-TIRENI---TLGDPDATDEEIIEAARLagLHDfiealpMGYDTVVGEGGSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 159 RALMNGGDVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEIISDRP 228
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-224 |
6.10e-35 |
|
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: 129.86 E-value: 6.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgklepdqlarlr 86
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyfgfifqryhllgdlsaegnvevpavYAGVTPSERKQratallteLGLGTKtlnrpSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03216 64 ----------------------------VSFASPRDARR--------AGIAMV-----YQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVTVLRDGRVV 161
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-228 |
1.05e-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: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLArlrreyfgfIFQRYHLLGDLSA 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 106 EGNV--EVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGV 183
Cdd:TIGR01184 72 RENIalAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 184 EVM-RILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDG---------EIISDRP 228
Cdd:TIGR01184 152 NLQeELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNGpaanigqilEVPFPRP 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-226 |
1.05e-34 |
|
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: 134.54 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 41 IVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDqlarlrREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTP 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 121 SERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALD----SHSGVEVMRILRELnaaG 196
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---G 151
|
170 180 190
....*....|....*....|....*....|.
gi 491444527 197 HTIILVTHDMQVAKN-ATRIIEISDGEIISD 226
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTmSDRIAIMRKGKIAQI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-216 |
2.23e-34 |
|
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: 137.80 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGESTIQilkGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlr 86
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALR---PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEgNVEVPAVYAGVTPSERKQRATALLT-----ELGLGTKTLNRPSQLSGGQQQRVSIARAL 161
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTIAE-NIRLARPDASDAEIREALERAGLDEfvaalPQGLDTPIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 162 MNGGDVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRII 216
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIV 527
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
24-223 |
2.55e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 134.06 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEpdqlARLRReyFGFIFQRYHLLGDL 103
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH----ARDRK--VGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVevpAVYAGVTPS-ER------KQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGA 176
Cdd:PRK10851 90 TVFDNI---AFGLTVLPRrERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 177 LDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAKN-ATRIIEISDGEI 223
Cdd:PRK10851 167 LDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-228 |
3.49e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 130.26 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlarlrREyFGFIFQRYHLLGDLSAEGN 108
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-----RP-VSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 109 VevpavYAGVTPS-----ERKQRATALLTELGLGTKtLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:COG3840 92 I-----GLGLRPGlkltaEQRAQVEQALERVGLAGL-LDRlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491444527 183 VEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEIISDRP 228
Cdd:COG3840 166 QEMLDLVDELCRErGLTVLMVTHDPEdAARIADRVLLVADGRIAADGP 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-228 |
3.12e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.61 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:COG1129 2 EPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLRreyFGFIFQRYHLLGDLSAEGNvevpaVYAGVTPSER--------KQRATALLTELGLGTKtLNRP-SQLSGGQQQR 154
Cdd:COG1129 78 AAG---IAIIHQELNLVPNLSVAEN-----IFLGREPRRGglidwramRRRARELLARLGLDID-PDTPvGDLSVAQQQL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 155 VSIARALMNGGDVILADEPTGALdSHSGVEVM-RILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISDRP 228
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASL-TEREVERLfRIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGP 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-226 |
7.09e-33 |
|
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: 126.68 E-value: 7.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 22 TIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARlrreyFGFIF-QRYHLL 100
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-----IGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 101 GDLSA-EGNVEVPAVYaGVTPSERKQRaTALLTELGLGTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGALD 178
Cdd:cd03267 108 WDLPViDSFYLLAAIY-DLPPARFKKR-LDELSELLDLEELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 179 SHSGVEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEIISD 226
Cdd:cd03267 186 VVAQENIRNFLKEYNRErGTTVLLTSHYMKdIEALARRVLVIDKGRLLYD 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-220 |
9.45e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 126.25 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVrefpAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGcLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:COG0410 2 PMLEVENLH----AGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RL--------RReyfgfIFqryhllGDLSAEGNVEVPAvYAGVTPSERKQ---RATAL---LTELglgtktLNRP-SQLS 148
Cdd:COG0410 77 RLgigyvpegRR-----IF------PSLTVEENLLLGA-YARRDRAEVRAdleRVYELfprLKER------RRQRaGTLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 149 GGQQQRVSIARALMNGGDVILADEPTGALdSHSGV-EVMRILRELNAAGHTIILVTHdmqvakNATRIIEISD 220
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPSLGL-APLIVeEIFEIIRRLNREGVTILLVEQ------NARFALEIAD 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
24-228 |
9.85e-33 |
|
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: 126.74 E-value: 9.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSG-SYKVSGQETGKLEPDQLarlrREYFGF----IFQRYH 98
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWEL----RKRIGLvspaLQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 99 llGDLSAEgNVEVPAVYAGV----TPSER-KQRATALLTELGLGTKtLNRP-SQLSGGQQQRVSIARALMNGGDVILADE 172
Cdd:COG1119 93 --RDETVL-DVVLSGFFDSIglyrEPTDEqRERARELLELLGLAHL-ADRPfGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 173 PTGALDSHSGVEVMRILRELNAAGH-TIILVTHDMQ-VAKNATRIIEISDGEIISDRP 228
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGP 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-226 |
1.08e-32 |
|
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: 125.30 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 30 DLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDqlarlrREYFGFIFQRYHLLGDLSAEGNV 109
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 110 EVpavyaGVTPS-----ERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVE 184
Cdd:cd03298 92 GL-----GLSPGlkltaEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491444527 185 VMRILRELNA-AGHTIILVTHDMQVAKN-ATRIIEISDGEIISD 226
Cdd:cd03298 167 MLDLVLDLHAeTKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQ 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-224 |
2.03e-32 |
|
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: 124.61 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGestiQILKGIDLTIYEGeLVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlEPDQLarlr 86
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-224 |
2.39e-32 |
|
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: 124.25 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDqLARLr 86
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-LRRI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyfGFIFQRYHLLGDLSAEGNVEVPAVYAGVtpseRKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03268 75 ----GALIEAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEII 224
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLsEIQKVADRIGIINKGKLI 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-282 |
3.09e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.29 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE-TGKLEPDQLARLRREyFGFIFQ-RYHLLGDL 103
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERViTAGKKNKKLKPLRKK-VGIVFQfPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 183 VEVMRILRELN-AAGHTIILVTHDMQ-VAKNATRIIEISDG---------EIISDrpnvPDQAAEPGNSDPDAApALQGK 251
Cdd:PRK13634 182 KEMMEMFYKLHkEKGLTTVLVTHSMEdAARYADQIVVMHKGtvflqgtprEIFAD----PDELEAIGLDLPETV-KFKRA 256
|
250 260 270
....*....|....*....|....*....|...
gi 491444527 252 --QKKGKSISAWRSTLDRLSEAFQmALLSMNAH 282
Cdd:PRK13634 257 leEKFGISFPKPCLTLEELAHEVV-QLLRKGGH 288
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-220 |
4.66e-32 |
|
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: 123.70 E-value: 4.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVrefpAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGcLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:cd03224 1 LEVENLN----AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMG-LLPPRSGSIRFDGRDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RreyFGFIFQRYHLLGDLSAEGNVEVpAVYAGvTPSERKQRATALLTEL-GLGTKTLNRPSQLSGGQQQRVSIARALMNG 164
Cdd:cd03224 76 G---IGYVPEGRRIFPELTVEENLLL-GAYAR-RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 165 GDVILADEPTGALdSHSGV-EVMRILRELNAAGHTIILVTHdmqvakNATRIIEISD 220
Cdd:cd03224 151 PKLLLLDEPSEGL-APKIVeEIFEAIRELRDEGVTILLVEQ------NARFALEIAD 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
8.78e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.72 E-value: 8.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 2 TKQALLEVSNLVreFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQ 81
Cdd:PRK13632 3 NKSVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 82 LarlrREYFGFIFQR--YHLLGdLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLgTKTLNR-PSQLSGGQQQRVSIA 158
Cdd:PRK13632 81 I----RKKIGIIFQNpdNQFIG-ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKePQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 159 RALMNGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-226 |
1.64e-31 |
|
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: 122.02 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIyEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQ---ETGK---LEPDQlarlRReyFGFIFQRYHLLGD 102
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQQ----RK--IGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEGNVEVpaVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:cd03297 90 LNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 183 VEVMRILRELNAAGH-TIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:cd03297 168 LQLLPELKQIKKNLNiPVIFVTHDLsEAEYLADRIVVMEDGRLQYI 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-225 |
1.95e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 124.12 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREYFGFIFQ--RYHLLG 101
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 DlSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSH 180
Cdd:PRK13646 101 D-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491444527 181 SGVEVMRILRELNA-AGHTIILVTHDM-QVAKNATRIIEISDGEIIS 225
Cdd:PRK13646 180 SKRQVMRLLKSLQTdENKTIILVSHDMnEVARYADEVIVMKEGSIVS 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-226 |
4.41e-31 |
|
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: 121.16 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEstIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlr 86
Cdd:cd03245 3 IEFRNVSFSYPNQE--IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHL----------LGDLSAEGN-VEVPAVYAGVTPSERKQRAtalltelGLGTKTLNRPSQLSGGQQQRV 155
Cdd:cd03245 77 RRNIGYVPQDVTLfygtlrdnitLGAPLADDErILRAAELAGVTDFVNKHPN-------GLDLQIGERGRGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 156 SIARALMNGGDVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEIISD 226
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-225 |
5.09e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.43 E-value: 5.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 3 KQALLEVSNLVREFPagESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgkLEPDQL 82
Cdd:PRK13635 2 KEEIIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 ARLRREyFGFIFQR--YHLLGdlsaeGNVEVPAVYA----GVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVS 156
Cdd:PRK13635 77 WDVRRQ-VGMVFQNpdNQFVG-----ATVQDDVAFGleniGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 157 IARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGH-TIILVTHDMQVAKNATRIIEISDGEIIS 225
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| LolE |
COG4591 |
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ... |
447-664 |
9.83e-31 |
|
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: 121.95 E-value: 9.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 447 RIIGIVEpqtSGMGSDDTLNVYMPYTTVMSRMLGQSNVRNIVVRINDKYSTAAAENAIVNLLtqrhgaQDIFTMNSDSIR 526
Cdd:COG4591 69 TVVGIFE---SGGYELDGSLVYVPLETAQELLGLGDQVSGILVKLKDGADAEAVAAALEAAL------PGLEVKTWRELN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 527 QTIEKTTSTMTLLVSAIAVISLVVGGIGVMNIMLVSVTERTQEIGVRMAVGARQSDILQQFLIEAILVCLI------GGV 600
Cdd:COG4591 140 AALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLERTREIGILKALGASRRQIRRIFLLEGLLLGLIggllglLLG 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 601 LGVLLSLGLGQLINKFAGGNFSVAYSSTSIIAAFVCSTLIGVVFGFLPAKNAAKLDPVAALSRE 664
Cdd:COG4591 220 LLLALLLNALLGILLPFIFALPVSLSPSDVLLALLLALLISLLASLYPARRAARLDPVEALRGE 283
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-226 |
9.89e-31 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 119.78 E-value: 9.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlEPDQlARL 85
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAE-ARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RreyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGtKTLNRP-SQLSGGQQQRVSIARALMNG 164
Cdd:cd03266 79 R---LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGME-ELLDRRvGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 165 GDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEIISD 226
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYE 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-249 |
1.02e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 121.33 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFP-----AGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:PRK10419 3 LLNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLRREyFGFIFQR-------YHLLGDLSAEgnvevPAVY-AGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQ 151
Cdd:PRK10419 83 QRKAFRRD-IQMVFQDsisavnpRKTVREIIRE-----PLRHlLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 152 QQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHT-IILVTHDMQ-VAKNATRIIEISDGEIISDRPn 229
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRlVERFCQRVMVMDNGQIVETQP- 235
|
250 260
....*....|....*....|
gi 491444527 230 vpdqAAEPGNSDPDAAPALQ 249
Cdd:PRK10419 236 ----VGDKLTFSSPAGRVLQ 251
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-223 |
1.32e-30 |
|
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: 119.28 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlarlr 86
Cdd:cd03301 1 VELENVTKRF--GNVTA--LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03301 72 RD-IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 167 VILADEPTGALDSHSGV----EVMRILRELNAaghTIILVTHDMQVAKN-ATRIIEISDGEI 223
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVqmraELKRLQQRLGT---TTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-224 |
2.35e-30 |
|
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: 119.26 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEpdqLARLRReYFGFIFQRYHLLGDLS 104
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRR-QIGLVSQDVFLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEgNVevpaVYA--GVTPSERKQRA-TALLTEL------GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTG 175
Cdd:cd03251 93 AE-NI----AYGrpGATREEVEEAArAANAHEFimelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 176 ALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:cd03251 168 ALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-224 |
4.47e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.28 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHLLGDl 103
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQDTFLFSG- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVevpaVYA--GVTPSE-----RKQRATALLTEL--GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:COG1132 429 TIRENI----RYGrpDATDEEveeaaKAAQAHEFIEALpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 175 GALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:COG1132 505 SALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-224 |
4.55e-30 |
|
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: 118.49 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLepdQLARLRREyFGFIFQRYHLLGDl 103
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRA-IGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEvpavYAGVTPSERKQRATALLTEL---------GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:cd03253 90 TIGYNIR----YGRPDATDEEVIEAAKAAQIhdkimrfpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 175 GALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:cd03253 166 SALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-224 |
5.07e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.93 E-value: 5.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE-TGKLEPDQLARLRREyFGFIFQ--RYHLLGD 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHiTPETGNKNLKKLRKK-VSLVFQfpEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEgNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHS 181
Cdd:PRK13641 102 TVLK-DVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491444527 182 GVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEII 224
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
1.00e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.64 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGEstiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgkLEPDQLARL 85
Cdd:PRK13639 1 ILETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP---IKYDKKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 R-REYFGFIFQRY-HLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMN 163
Cdd:PRK13639 75 EvRKTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEIIS 225
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDlVPVYADKVYVMSDGKIIK 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-220 |
1.06e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.81 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDRP--TSGSYKVSGQETGKLEPDQlarlRReyFGFIFQRYHLLG 101
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQ----RR--IGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 DLSAEGNVEVpAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHS 181
Cdd:COG4136 90 HLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491444527 182 GVEVMRILRE-LNAAGHTIILVTHDMQVAKNATRIIEISD 220
Cdd:COG4136 169 RAQFREFVFEqIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-226 |
1.17e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.81 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 8 EVSNLVREFPAGES-----------------TIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNIL-GCLdRPTSGSYKV 69
Cdd:COG4586 3 EVENLSKTYRVYEKepglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 70 SGqetgkLEPdqlARLRREY---FGFIF-QRYHLLGDLSAEGNVEV-PAVYaGVTPSERKQRATALLTELGLGTKtLNRP 144
Cdd:COG4586 82 LG-----YVP---FKRRKEFarrIGVVFgQRSQLWWDLPAIDSFRLlKAIY-RIPDAEYKKRLDELVELLDLGEL-LDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 145 -SQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDG 221
Cdd:COG4586 152 vRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDdIEALCDRVIVIDHG 231
|
....*
gi 491444527 222 EIISD 226
Cdd:COG4586 232 RIIYD 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-252 |
2.78e-29 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 119.44 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQ-----ETGKLEPdqlARLRReyFGFIFQRYHLLGDL 103
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLP---PHRRR--IGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEvpAVYAGVTPSERKQRATALLTELGLGTKtLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:COG4148 93 SVRGNLL--YGRKRAPRAERRISFDEVVELLGIGHL-LDRrPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 183 VEVMRILRELNAAGHT-IILVTHDMQ-VAKNATRIIEISDGEIIsdrpnvpdqAAEPGN---SDPDAAPALQGKQ 252
Cdd:COG4148 170 AEILPYLERLRDELDIpILYVSHSLDeVARLADHVVLLEQGRVV---------ASGPLAevlSRPDLLPLAGGEE 235
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-226 |
4.00e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.37 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNIL-GCLdRPTSGSYKVSGQETGKLEPDQLARLRreyfGFIFQRYHLLGD 102
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARRR----AVLPQHSSLAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEgnvEVpaVYAGVTP-----SERKQRATALLTELGLGTKtLNRP-SQLSGGQQQRVSIARAL------MNGGD-VIL 169
Cdd:COG4559 90 FTVE---EV--VALGRAPhgssaAQDRQIVREALALVGLAHL-AGRSyQTLSGGEQQRVQLARVLaqlwepVDGGPrWLF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 170 ADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEIISD 226
Cdd:COG4559 164 LDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQ 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
24-223 |
5.23e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 116.32 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYkVSGQETgklepdqLARLRrEYFGFIFQRYHLLGDL 103
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAP-------LAEAR-EDTRLMFQDARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVpavyaGVTPSERkQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGV 183
Cdd:PRK11247 97 KVIDNVGL-----GLKGQWR-DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491444527 184 EVMRILREL-NAAGHTIILVTHDMQVA-KNATRIIEISDGEI 223
Cdd:PRK11247 171 EMQDLIESLwQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-224 |
7.18e-29 |
|
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: 113.18 E-value: 7.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLvrEFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDrPTSGSYKVSGQETGKLEpdqlaRL 85
Cdd:cd03247 1 LSINNV--SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLK-PQQGEITLDGVPVSDLE-----KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREYFGFIFQRYHLLgdlsaegnvevpavyagvtpserkqrATALLTELGLgtktlnrpsQLSGGQQQRVSIARALMNGG 165
Cdd:cd03247 73 LSSLISVLNQRPYLF--------------------------DTTLRNNLGR---------RFSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-229 |
9.88e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.40 E-value: 9.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLArl 85
Cdd:PRK11607 19 LLEIRNLTKSFDG----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 rreyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:PRK11607 93 ----INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 166 DVILADEPTGALDS----HSGVEVMRILRELnaaGHTIILVTHDMQVAKN-ATRI--------IEISDGEIISDRPN 229
Cdd:PRK11607 169 KLLLLDEPMGALDKklrdRMQLEVVDILERV---GVTCVMVTHDQEEAMTmAGRIaimnrgkfVQIGEPEEIYEHPT 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-231 |
1.05e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 117.37 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFP------AGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKL 77
Cdd:PRK11308 3 QPLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 78 EPDQLARLRREyFGFIFQR-YhllGDLSAEGNV----EVP-AVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGG 150
Cdd:PRK11308 83 DPEAQKLLRQK-IQIVFQNpY---GSLNPRKKVgqilEEPlLINTSLSAAERREKALAMMAKVGLRPEHYDRyPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 151 QQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHT-IILVTHDMQVAKNAT---------RIIEISD 220
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsYVFISHDLSVVEHIAdevmvmylgRCVEKGT 238
|
250
....*....|.
gi 491444527 221 GEIISDRPNVP 231
Cdd:PRK11308 239 KEQIFNNPRHP 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-227 |
2.71e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.96 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 3 KQALLEVSNLVREFP---------AGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGcLDRPTSGSYKVSGQ 72
Cdd:PRK15079 5 KKVLLEVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 73 ETGKLEPDQLaRLRREYFGFIFQ--------RYHlLGDLSAEgnvEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR- 143
Cdd:PRK15079 84 DLLGMKDDEW-RAVRSDIQMIFQdplaslnpRMT-IGEIIAE---PLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 144 PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKNatriieisdge 222
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKH----------- 227
|
....*
gi 491444527 223 iISDR 227
Cdd:PRK15079 228 -ISDR 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-225 |
3.66e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSG--------QETGkLEPDQ---------LARLRR 87
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpQEPP-LDDDLtvldtvldgDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 88 eyfgfIFQRYHLLGDLSAEGNvEVPAVYAGVTPS-------ERKQRATALLTELGLGTKTLNRP-SQLSGGQQQRVSIAR 159
Cdd:COG0488 92 -----LEAELEELEAKLAEPD-EDLERLAELQEEfealggwEAEARAEEILSGLGFPEEDLDRPvSELSGGWRRRVALAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 160 ALMNGGDVILADEPTGALDshsgVEVMRILRE-LNAAGHTIILVTHDM----QVaknATRIIEISDGEIIS 225
Cdd:COG0488 166 ALLSEPDLLLLDEPTNHLD----LESIEWLEEfLKNYPGTVLVVSHDRyfldRV---ATRILELDRGKLTL 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-216 |
3.78e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.56 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKL------EPDQL-ARLRREYFGFIFQRYH 98
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYvpqrseVPDSLpLTVRDLVAMGRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 99 LLGDLSAEGNVEVpavyagvtpserkqraTALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALD 178
Cdd:NF040873 88 LWRRLTRDDRAAV----------------DDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 491444527 179 SHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRII 216
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-224 |
1.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.77 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGESTiqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGklEPDQLARL 85
Cdd:PRK13644 1 MIRLENVSYSYPDGTPA---LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG--DFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RReYFGFIFQ--RYHLLGDlSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMN 163
Cdd:PRK13644 76 RK-LVGIVFQnpETQFVGR-TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-224 |
1.24e-27 |
|
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: 111.48 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 23 IQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHL--- 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLfdg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 100 -------LGDLSAEGNVEVPAVyagvtpseRKQRATALLTELGLGTKTL--NRPSQLSGGQQQRVSIARALMNGGDVILA 170
Cdd:cd03249 92 tiaenirYGKPDATDEEVEEAA--------KKANIHDFIMSLPDGYDTLvgERGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491444527 171 DEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-226 |
1.41e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.17 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNIL-GCLdRPTSGSYKVSGQETGKLEPDQLARLRreyfGFIFQRYHLLGD 102
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRR----AVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEgnvEVpaVYAGVTP-SERKQRATAL----LTELGLgTKTLNRP-SQLSGGQQQRVSIARALM------NGGDVILA 170
Cdd:PRK13548 91 FTVE---EV--VAMGRAPhGLSRAEDDALvaaaLAQVDL-AHLAGRDyPQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 171 DEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLnLAARYADRIVLLHQGRLVAD 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-226 |
1.45e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.87 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 3 KQALLEVSNLVREFPAGESTIQI--LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEpd 80
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEKlaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLRREYfGFIFQR--YHLLGDLsAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIA 158
Cdd:PRK13633 79 NLWDIRNKA-GMVFQNpdNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 159 RALMNGGDVILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDMQVAKNATRIIEISDGEIISD 226
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
26-228 |
1.91e-27 |
|
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: 118.04 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPdqlARLRREyFGFIFQRYHLL-GDLs 104
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDP---ADLRRN-IGYVPQDPRLFyGTL- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 aEGNVEVPAVYAGvtpSERKQRATAL--LTEL------GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGA 176
Cdd:TIGR03375 556 -RDNIALGAPYAD---DEEILRAAELagVTEFvrrhpdGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSA 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491444527 177 LDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEIISDRP 228
Cdd:TIGR03375 632 MDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGP 682
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-224 |
2.00e-27 |
|
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: 109.56 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 19 GESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNIL-GCLDRP-TSGSYKVSGQetgklePDQLARLRREYfGFIFQR 96
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGR------PLDKRSFRKII-GYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 97 YHLLGDLSAEGNVEVpavyagvtpserkqraTALLtelglgtktlnrpSQLSGGQQQRVSIARALMNGGDVILADEPTGA 176
Cdd:cd03213 91 DILHPTLTVRETLMF----------------AAKL-------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 177 LDSHSGVEVMRILRELNAAGHTIILVTHD--MQVAKNATRIIEISDGEII 224
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSIHQpsSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
2.18e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 113.02 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFPAGEST-IQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKV--------SG 71
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKQENeLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 72 QETGKLEPDQ-----LARLRREyFGFIFQ--RYHLLGDlSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR- 143
Cdd:PRK13631 96 NHELITNPYSkkiknFKELRRR-VSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERs 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 144 PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGE 222
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGK 253
|
..
gi 491444527 223 II 224
Cdd:PRK13631 254 IL 255
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
24-228 |
2.96e-27 |
|
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: 110.85 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLmniLGCLDR--PTSGSYKVSGQET--------GKLEPDQLarlrREYFGFI 93
Cdd:TIGR00972 15 EALKNINLDIPKNQVTALIGPSGCGKSTL---LRSLNRmnDLVPGVRIEGKVLfdgqdiydKKIDVVEL----RRRVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 94 FQRYHLLgDLSAEGNVEV-PAVYAGVTPSERKQRATALLTELGLGTKTLNR----PSQLSGGQQQRVSIARALMNGGDVI 168
Cdd:TIGR00972 88 FQKPNPF-PMSIYDNIAYgPRLHGIKDKKELDEIVEESLKKAALWDEVKDRlhdsALGLSGGQQQRLCIARALAVEPEVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 169 LADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNAT-RIIEISDGEIISDRP 228
Cdd:TIGR00972 167 LLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISdRTAFFYDGELVEYGP 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-237 |
3.65e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 113.28 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSG---QETGK---LEPDQlarlRReyFGFIFQRYHLLGD 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPEK----RR--IGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEGNVEVPavYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:TIGR02142 90 LSVRGNLRYG--MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 183 VEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEI--------ISDRPNVPDQAAEP 237
Cdd:TIGR02142 168 YEILPYLERLHAEfGIPILYVSHSLQeVLRLADRVVVLEDGRVaaagpiaeVWASPDLPWLARED 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-223 |
3.95e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.50 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFpagESTiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:PRK09452 9 SSLSPLVELRGISKSF---DGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QlarlrrEYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARA 160
Cdd:PRK09452 85 N------RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 161 LMNGGDVILADEPTGALD----SHSGVEVMRILRELnaaGHTIILVTHDMQVAKNAT-RIIEISDGEI 223
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSdRIVVMRDGRI 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-223 |
4.67e-27 |
|
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: 108.07 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVreFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlr 86
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEgNVevpavyagvtpserkqratalltelglgtktlnrpsqLSGGQQQRVSIARALMNGGD 166
Cdd:cd03246 75 GDHVGYLPQDDELFSGSIAE-NI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-226 |
5.43e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.49 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARlrreYFGFIFQRYhllgdLS 104
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR----RLALLPQHH-----LT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGnVEVPAVYA-GVTP---------SERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:PRK11231 88 PEG-ITVRELVAyGRSPwlslwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491444527 175 GALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQ 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-223 |
6.26e-27 |
|
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: 107.90 E-value: 6.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLvrefpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLAR 84
Cdd:cd03215 3 PVLEVRGL--------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 LRreyFGFIfqryhllgdlsaegnvevpavyagvtPSERKQRAtaLLTELGLGTKTLNrPSQLSGGQQQRVSIARALMNG 164
Cdd:cd03215 75 AG---IAYV--------------------------PEDRKREG--LVLDLSVAENIAL-SSLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 165 GDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEI 223
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-224 |
9.49e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 109.74 E-value: 9.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLmniLGCLDR-----P---TSGSYKVSGQETgkLEPDQ-LARLRREyFGFIF 94
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTL---LRCLNRmndliPgarVEGEILLDGEDI--YDPDVdVVELRRR-VGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 95 QR--------YhllgDlsaegNVEVPAVYAGVTPS-------ERKQRATAL-------LTELGLGtktlnrpsqLSGGQQ 152
Cdd:COG1117 99 QKpnpfpksiY----D-----NVAYGLRLHGIKSKseldeivEESLRKAALwdevkdrLKKSALG---------LSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 153 QRVSIARALMNGGDVILADEPTGALDSHSGvevMRI---LRELnAAGHTIILVTHDMQvakNATRiieISD-------GE 222
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPIST---AKIeelILEL-KKDYTIVIVTHNMQ---QAAR---VSDytaffylGE 230
|
..
gi 491444527 223 II 224
Cdd:COG1117 231 LV 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-221 |
1.13e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.40 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPaGEStiqILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQetgKLEPDQLARl 85
Cdd:PRK11248 1 MLQISHLYADYG-GKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 rreyfGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 166 DVILADEPTGALDSHSGvEVMR--ILRELNAAGHTIILVTHDMQVAK-NATRIIEISDG 221
Cdd:PRK11248 148 QLLLLDEPFGALDAFTR-EQMQtlLLKLWQETGKQVLLITHDIEEAVfMATELVLLSPG 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-224 |
1.37e-26 |
|
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: 107.75 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQetgklepdQLARLR 86
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK--------PLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEII 224
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMeLVEELCDRVLLLNKGRAV 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-226 |
1.76e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGesTI---QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:COG1101 2 LELKNLSKTFNPG--TVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RlrreYFGFIFQRyHLLG---DLSAEGNVevpAVYA----------GVTPSERKqRATALLTELGLG------TKTlnrp 144
Cdd:COG1101 80 K----YIGRVFQD-PMMGtapSMTIEENL---ALAYrrgkrrglrrGLTKKRRE-LFRELLATLGLGlenrldTKV---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 145 SQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGH-TIILVTHDMQVA-KNATRIIEISDGE 222
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQAlDYGNRLIMMHEGR 226
|
....
gi 491444527 223 IISD 226
Cdd:COG1101 227 IILD 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-223 |
1.79e-26 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 107.64 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 30 DLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPdqlarlRREYFGFIFQRYHLLGDLSAEGNV 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP------YQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 110 EVpavyaGVTPS-----ERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVE 184
Cdd:TIGR01277 92 GL-----GLHPGlklnaEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491444527 185 VMRILREL-NAAGHTIILVTHDMQ-VAKNATRIIEISDGEI 223
Cdd:TIGR01277 167 MLALVKQLcSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-226 |
2.04e-26 |
|
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: 108.34 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPdqlARLRREyFGFIFQRYHLLG--- 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP---AWLRRQ-VGVVLQENVLFNrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 -DLSAEGNVEVPAvyAGVTPSERKQRATALLTELGLGTKTL--NRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALD 178
Cdd:cd03252 93 rDNIALADPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIvgEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491444527 179 SHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEIISD 226
Cdd:cd03252 171 YESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-224 |
2.92e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.47 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFPAGestiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGS--YKVSGQETGKL- 77
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMRDGQLRDLy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 78 ---EPDQLARLRREYfGFIFQ--RYHLLGDLSAEGNVEVPAVYAGvtpsER---KQRATAL--LTELGLGTKTLN-RPSQ 146
Cdd:PRK11701 77 alsEAERRRLLRTEW-GFVHQhpRDGLRMQVSAGGNIGERLMAVG----ARhygDIRATAGdwLERVEIDAARIDdLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 147 LSGGQQQRVSIARALMNGGDVILADEPTGALDshsgVEVM-RIL-------RELNAAghtIILVTHDMQVAKN-ATRIIE 217
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD----VSVQaRLLdllrglvRELGLA---VVIVTHDLAVARLlAHRLLV 224
|
....*..
gi 491444527 218 ISDGEII 224
Cdd:PRK11701 225 MKQGRVV 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-222 |
3.63e-26 |
|
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: 106.40 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 17 PAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDRpTSGSYKVSG------QE----TGKLepdqlarl 85
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGsiayvsQEpwiqNGTI-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 rRE--YFG--FIFQRYH-------LLGDLsaegnvevpavyagvtpserKQRATALLTELGlgTKTLNrpsqLSGGQQQR 154
Cdd:cd03250 83 -REniLFGkpFDEERYEkvikacaLEPDL--------------------EILPDGDLTEIG--EKGIN----LSGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSGVEVM-RILRELNAAGHTIILVTHDMQVAKNATRIIEISDGE 222
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-224 |
3.78e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 113.60 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRP---TSGSYKVSGQetgKLEPDQLarlrREYFGFIFQRYHLL 100
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM---PIDAKEM----RAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 101 GDLSAEGNVEVPA---VYAGVTPSERKQRATALLTELGLGT--KTL----NRPSQLSGGQQQRVSIARALMNGGDVILAD 171
Cdd:TIGR00955 112 PTLTVREHLMFQAhlrMPRRVTKKEKRERVDEVLQALGLRKcaNTRigvpGRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 172 EPTGALDSHSGVEVMRILRELNAAGHTIILVTHD--MQVAKNATRIIEISDGEII 224
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRVA 246
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
24-209 |
5.68e-26 |
|
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: 105.58 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARlrREYFGFIFQryhllgdl 103
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLER--RQRVGLVFQ-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVPAVYA---------GVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:TIGR01166 76 DPDDQLFAADVDQdvafgplnlGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*
gi 491444527 175 GALDSHSGVEVMRILRELNAAGHTIILVTHDMQVA 209
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-208 |
6.22e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.12 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 23 IQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlarlrREyFGFIFQRYHLLGD 102
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RG-VGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDS--- 179
Cdd:PRK11000 90 LSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalr 169
|
170 180 190
....*....|....*....|....*....|
gi 491444527 180 -HSGVEVMRILRELnaaGHTIILVTHDmQV 208
Cdd:PRK11000 170 vQMRIEISRLHKRL---GRTMIYVTHD-QV 195
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-224 |
7.75e-26 |
|
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: 106.27 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNL---VREFpagestiqILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDqla 83
Cdd:cd03299 1 LKVENLskdWKEF--------KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 rlrREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLgTKTLNR-PSQLSGGQQQRVSIARALM 162
Cdd:cd03299 70 ---KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRkPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 163 NGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLI 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-233 |
7.91e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.12 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREYFGFIFQRYHLLGDLSA 105
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 106 EGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEV 185
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 186 MRILRELNAAGH-TIILVTHDMQVA-KNATRIIEISDGEIIsdRPNVPDQ 233
Cdd:PRK10070 204 QDELVKLQAKHQrTIVFISHDLDEAmRIGDRIAIMQNGEVV--QVGTPDE 251
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-226 |
1.10e-25 |
|
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: 105.69 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 14 REFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEpdqlarlrreyFGFI 93
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-----------LGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 94 FQryhllGDLSAEGNVEVPAVYAGVTPSERKQR--ATALLTELGlgtKTLNRP-SQLSGGQQQRVSIARALMNGGDVILA 170
Cdd:cd03220 95 FN-----PELTGRENIYLNGRLLGLSRKEIDEKidEIIEFSELG---DFIDLPvKTYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 171 DEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPsSIKRLCDRALVLEKGKIRFD 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-225 |
1.10e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.13 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEstiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlepdQLARLR 86
Cdd:PRK13647 5 IEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA----ENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIFQRYH-LLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:PRK13647 78 RSKVGLVFQDPDdQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEIIS 225
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLA 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-224 |
1.20e-25 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 105.70 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03218 77 ---IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDmqvAKNATRIIE----ISDGEII 224
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VRETLSITDrayiIYEGKVL 212
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-224 |
1.39e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.48 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLdrPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHLL-G 101
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELDPESW----RKHLSWVGQNPQLPhG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 DLSAegNVEVPAVYAgvTPSERKQ---RATAL----LTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:PRK11174 438 TLRD--NVLLGNPDA--SDEQLQQaleNAWVSeflpLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 175 GALDSHSGVEVMRILRElNAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:PRK11174 514 ASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-226 |
1.53e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.72 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAgESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQetgKLEPDQLARL 85
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREyFGFIFQR--YHLLGdLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMN 163
Cdd:PRK13642 80 RRK-IGMVFQNpdNQFVG-ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAAGH-TIILVTHDMQVAKNATRIIEISDGEIISD 226
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-224 |
1.78e-25 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 111.35 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGEstIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgkLEPDQLARL 85
Cdd:TIGR02203 330 DVEFRNVTFRYPGRD--RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD---LADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREyFGFIFQRYHLLGDLSAEgNVEVPAVyaGVTPSERKQRA--TALLTE------LGLGTKTLNRPSQLSGGQQQRVSI 157
Cdd:TIGR02203 405 RRQ-VALVSQDVVLFNDTIAN-NIAYGRT--EQADRAEIERAlaAAYAQDfvdklpLGLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 158 ARALMNGGDVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-271 |
1.90e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREYFGFIFQ-RYHLLGDLS 104
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGV 183
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 184 EVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEII-SDRPNVPDQAAEPGNSDPDAAPAL----QGKQKKGKS 257
Cdd:PRK13649 183 ELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVlSGKPKDIFQDVDFLEEKQLGVPKItkfaQRLADRGIS 262
|
250
....*....|....
gi 491444527 258 ISAWRSTLDRLSEA 271
Cdd:PRK13649 263 FSSLPITIEEFREV 276
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-224 |
1.91e-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: 105.68 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGEStiqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 -----RLRREYFGFIFQ--RYHLLGDLSAEGNVEVPAVYAGVTPSER-KQRATALLTELGLG-TKTLNRPSQLSGGQQQR 154
Cdd:TIGR02323 77 eaerrRLMRTEWGFVHQnpRDGLRMRVSAGANIGERLMAIGARHYGNiRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAK-NATRIIEISDGEII 224
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-224 |
1.96e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 106.07 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGES-----TIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQetgKLEP 79
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 80 ---DQLARLRReyfgFIFQryhllgDLSAEGN--------VEVPAVYA-GVTPSERKQRATALLTELGL-GTKTLNRPSQ 146
Cdd:COG4167 80 gdyKYRCKHIR----MIFQ------DPNTSLNprlnigqiLEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 147 LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHiSDKVLVMHQGEVV 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-213 |
2.40e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 2 TKQALLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQ 81
Cdd:COG3845 1 MMPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 82 LARLRreyFGFIFQRYHLLGDLSAEGNV----EvPAVYAGVTPSERKQRATALLTELGLGTKtLNRP-SQLSGGQQQRVS 156
Cdd:COG3845 77 AIALG---IGMVHQHFMLVPNLTVAENIvlglE-PTKGGRLDRKAARARIRELSERYGLDVD-PDAKvEDLSVGEQQRVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 157 IARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHD----MQVAKNAT 213
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKlrevMAIADRVT 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-225 |
4.42e-25 |
|
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: 104.23 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 20 ESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHL 99
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 100 ----------LGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGlgtktlNRPSQLSGGQQQRVSIARALMNGGDVIL 169
Cdd:cd03254 89 fsgtimenirLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLG------ENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 170 ADEPTGALDSHSGVEVMRILRELNaAGHTIILVTHDMQVAKNATRIIEISDGEIIS 225
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-224 |
4.71e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.96 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLM-NILGCLDrPTSGSYKVSGQetgKLEPDQLARl 85
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGILA-PDSGEVLWDGE---PLDPEDRRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 rreyFGFifqryhllgdLSAE-G-----NVEVPAVY----AGVTPSERKQRATALLTELGLGTKtLNRPSQ-LSGGQQQR 154
Cdd:COG4152 73 ----IGY----------LPEErGlypkmKVGEQLVYlarlKGLSKAEAKRRADEWLERLGLGDR-ANKKVEeLSKGNQQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSgVEVMR-ILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEII 224
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVN-VELLKdVIRELAAKGTTVIFSSHQMeLVEELCDRIVIINKGRKV 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-224 |
6.23e-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: 109.12 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLD--RPTSGS--YKVS------------ 70
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRiiYHVAlcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 71 --GQET----GKLEP---------DQLARLRREYFGFIFQR-YHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTEL 134
Cdd:TIGR03269 77 kvGEPCpvcgGTLEPeevdfwnlsDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 135 GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQV-AKNA 212
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEViEDLS 236
|
250
....*....|..
gi 491444527 213 TRIIEISDGEII 224
Cdd:TIGR03269 237 DKAIWLENGEIK 248
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
352-661 |
6.87e-25 |
|
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: 110.29 E-value: 6.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 352 DALMTQPYVSAVS-----PIVSTSKTMRYQ---------QNEANATINGVSNDYFDVKGLVFKDGQTFDQRSVRDRSQDV 417
Cdd:TIGR03434 483 ERLRALPGVESAAlasslPLSGNGWSGGVTiegrpppppGEEPLADYRRVSPGYFETMGIPLLRGRDFTERDTAGSPPVA 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 418 VIDTNTQKQFFGDGsNPIGQVVLLG---SVPARIIGIVE-PQTSGMGSDDTLNVYMPYTtvmsrmlgQSNVRN--IVVRi 491
Cdd:TIGR03434 563 IVNEAFARRYFPGE-DPIGKRIRLGgddGPWFEIVGVVGdVRYAGLDEPPRPEVYLPYA--------QSPDRGmtLVVR- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 492 ndkysTAAAENAIVNLLTQR----HGAQDIFTMNSdsIRQTIEKTTST---MTLLVSAIAVISLVVGGIGVMNIMLVSVT 564
Cdd:TIGR03434 633 -----TAGDPAALAAAVRRAvraiDPNLPVYDVRT--MEEQVDRSLAQerfLALLLGLFAALALLLAAIGLYGVLAYSVA 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 565 ERTQEIGVRMAVGARQSDILQQFLIEAILVCLIGGVLGVLLSLGLGQLInkfAGGNFSV-AYSSTSIIAAFVCSTLIGVV 643
Cdd:TIGR03434 706 QRTREIGIRMALGAQRGDVLRLVLRQGLRLAAAGLAIGLAAALALARLL---ASLLFGVsPTDPLTFAAVAALLLAVALL 782
|
330
....*....|....*...
gi 491444527 644 FGFLPAKNAAKLDPVAAL 661
Cdd:TIGR03434 783 ACYLPARRAARVDPMIAL 800
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-224 |
1.01e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 103.62 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLAR----LR-----------RE 88
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrlaiLRqenhinsrltvRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 89 YFGFifQRY-HLLGDLSAEGNVEVpavyagvtpserkQRATALLTELGLGTKTLNrpsQLSGGQQQRVSIARALMNGGDV 167
Cdd:COG4604 95 LVAF--GRFpYSKGRLTAEDREII-------------DEAIAYLDLEDLADRYLD---ELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 168 ILADEPTGALD-SHSgVEVMRILREL-NAAGHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:COG4604 157 VLLDEPLNNLDmKHS-VQMMKLLRRLaDELGKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-208 |
1.04e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.08 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPdqlaR 84
Cdd:PRK11650 2 AGLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP----A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 LRReyFGFIFQRYHLLGDLSAEGNVEvpavY----AGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARA 160
Cdd:PRK11650 75 DRD--IAMVFQNYALYPHMSVRENMA----YglkiRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491444527 161 LMNGGDVILADEPTGALDS----HSGVEVMRILRELNAaghTIILVTHDmQV 208
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRLKT---TSLYVTHD-QV 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
2.12e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.99 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 2 TKQALLEVSNLvrEFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQ 81
Cdd:PRK11160 334 ADQVSLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 82 LarlrREYFGFIFQRYHLLGDlSAEGNVEVPAvyagvtPSERKQRATALLTELGLGT-----KTLN-------RpsQLSG 149
Cdd:PRK11160 412 L----RQAISVVSQRVHLFSA-TLRDNLLLAA------PNASDEALIEVLQQVGLEKlleddKGLNawlgeggR--QLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 150 GQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-204 |
2.31e-24 |
|
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: 101.96 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 11 NLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRP---TSGSYKVSGQEtgkLEPDQLarlrR 87
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP---RKPDQF----Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 88 EYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQR----ATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMN 163
Cdd:cd03234 81 KCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTH 204
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-221 |
2.70e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.18 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:PRK09700 5 YISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RreyFGFIFQRYHLLGDLSAEGNvevpaVYAGVTP------------SERKQRATALLTELGLGTKTLNRPSQLSGGQQQ 153
Cdd:PRK09700 81 G---IGIIYQELSVIDELTVLEN-----LYIGRHLtkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 154 RVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDG 221
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-224 |
4.37e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE-TGKlePDQLARLRREyFGFIFQ--RYHLLGD 102
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDiTDK--KVKLSDIRKK-VGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 lSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTL--NRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSH 180
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYkdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 181 SGVEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:PRK13637 179 GRDEILNKIKELHKEyNMTIILVSHSMEdVAKLADRIIVMNKGKCE 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-220 |
8.47e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.38 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgklepdQLA 83
Cdd:PRK11288 2 SPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-------MRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLRREYFG----FIFQRYHLLGDLSAEGNV---EVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVS 156
Cdd:PRK11288 71 ASTTAALAagvaIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 157 IARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQvaknatRIIEISD 220
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME------EIFALCD 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-205 |
9.82e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.26 E-value: 9.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QlarlrREyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQR---ATALLTELGLGTKTLNrpsQLSGGQQQRVSI 157
Cdd:PRK11432 77 Q-----RD-ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRvkeALELVDLAGFEDRYVD---QISGGQQQRVAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 158 ARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHD 205
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHD 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-224 |
1.39e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 104.88 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 23 IQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVS-GQE---TGKLEPDQLARLRReYFGFIFQRYH 98
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPGPDGRGRAKR-YIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 99 L------LGDLSAEGNVEVPAVYAgvtpserKQRATALLTELGLGTK----TLNR-PSQLSGGQQQRVSIARALMNGGDV 167
Cdd:TIGR03269 376 LyphrtvLDNLTEAIGLELPDELA-------RMKAVITLKMVGFDEEkaeeILDKyPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 168 ILADEPTGALDSHSGVEVMR-ILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEII 224
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIV 507
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-226 |
1.80e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.77 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 12 LVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEpdqlarlrreyFG 91
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE-----------LG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 92 FIFQryhllGDLSAEGNVEVPAVYAGVTPSERKQR--ATALLTELGlgtKTLNRP-SQLSGGQQQRVSIARALMNGGDVI 168
Cdd:COG1134 97 AGFH-----PELTGRENIYLNGRLLGLSRKEIDEKfdEIVEFAELG---DFIDQPvKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 169 LADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:COG1134 169 LVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMgAVRRLCDRAIWLEKGRLVMD 227
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-237 |
1.82e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 99.15 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 31 LTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlepdqlarlRREYFGFIFQRYHLLGD--LSAEGn 108
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK---------GWRHIGYVPQRHEFAWDfpISVAH- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 109 vevpAVYAGVT----PSERKQRATALLTELGLGTKTL----NRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGALDS 179
Cdd:TIGR03771 71 ----TVMSGRTghigWLRRPCVADFAAVRDALRRVGLtelaDRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 180 HSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEIISDrpNVPDQAAEP 237
Cdd:TIGR03771 147 PTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIAD--GTPQQLQDP 202
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-208 |
2.61e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 101.34 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 2 TKQALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKS-TLMNILGCLDRP--TSGSYKVSGQETGKLE 78
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 79 PDQLARLRREYFGFIFQR-------YHLLGdlsaEGNVEVPAVYAGVTPSERKQRATALLTELGL--GTKTLNR-PSQLS 148
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDpmtslnpYMRVG----EQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeARKRMKMyPHEFS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 149 GGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRIL----RELNAAghtIILVTHDMQV 208
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTA---IIMITHDLGV 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-205 |
3.12e-23 |
|
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: 103.98 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTL-MNILGCLDrPTSGSYKVSGQETGKLEPDQLARLrreyFGFIFQRYHLLgDL 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLlATLAGLLD-PLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVPAvyAGVTPSE-----RKQRATALLTEL--GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGA 176
Cdd:TIGR02868 424 TVRENLRLAR--PDATDEElwaalERVGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|.
gi 491444527 177 LDSHSGVEvmrILRELNAA--GHTIILVTHD 205
Cdd:TIGR02868 502 LDAETADE---LLEDLLAAlsGRTVVLITHH 529
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-224 |
5.57e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 100.20 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKS-TLMNILGCLDRP---TSGSYKVSGQETGKLEPD 80
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLRREYFGFIFQryhllgDLSAEGN---------VEVPAVYAGVTPSERKQRATALLTELGL---GTKTLNRPSQLS 148
Cdd:PRK11022 82 ERRNLVGAEVAMIFQ------DPMTSLNpcytvgfqiMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 149 GGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILREL----NAAghtIILVTHDMQ-VAKNATRIIEISDGEI 223
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqkeNMA---LVLITHDLAlVAEAAHKIIVMYAGQV 232
|
.
gi 491444527 224 I 224
Cdd:PRK11022 233 V 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-228 |
6.26e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 102.77 E-value: 6.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEP--DQ 81
Cdd:PRK10762 2 QALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPksSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 82 LARLrreyfGFIFQRYHLLGDLSAEGNV----EVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSI 157
Cdd:PRK10762 78 EAGI-----GIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 158 ARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQvaknatRIIEI-------SDGEIISDRP 228
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLK------EIFEIcddvtvfRDGQFIAERE 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-225 |
7.13e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.99 E-value: 7.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLdRPTSGSYKVSGQETGKLEPDQLARlRREYFG------FIFQRYHL 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELAR-HRAYLSqqqsppFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 100 LgDLSAEGNVEVPAVyagvtpserkQRATALLTE-LGLGTKtLNRP-SQLSGGQQQRVSIARALMN-------GGDVILA 170
Cdd:COG4138 90 L-ALHQPAGASSEAV----------EQLLAQLAEaLGLEDK-LSRPlTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 171 DEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIIS 225
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLnHTLRHADRVWLLKQGKLVA 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-222 |
1.49e-22 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 94.05 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGestiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSgqetgklepdqlarlR 86
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------S 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REYFGFIfqryhllgdlsaegnvevpavyagvtpserkqratalltelglgtktlnrpSQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03221 62 TVKIGYF---------------------------------------------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 167 VILADEPTGALDSHSgveVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGE 222
Cdd:cd03221 91 LLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-226 |
1.52e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.72 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGqetgklEP-DQLA 83
Cdd:PRK13537 6 APIDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG------EPvPSRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMN 163
Cdd:PRK13537 76 RHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEIISD 226
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAE 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-301 |
1.55e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 101.67 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:PRK15439 6 TTAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLrreyfG--FIFQRYHLLGDLSAEGNV--EVPAvyagvtPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVS 156
Cdd:PRK15439 82 KAHQL-----GiyLVPQEPLLFPNLSVKENIlfGLPK------RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 157 IARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEII----SDRPNVP 231
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLpEIRQLADRISVMRDGTIAlsgkTADLSTD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 232 D--QAAEPG--NSDPDAAP----ALQGKQKKgKSISAWRSTLDRLS-EAFQMALLSMNAhrmrtfltmlGIIIGIASVV 301
Cdd:PRK15439 231 DiiQAITPAarEKSLSASQklwlELPGNRRQ-QAAGAPVLTVEDLTgEGFRNISLEVRA----------GEILGLAGVV 298
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-225 |
2.09e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREYFGFIFQ-RYHLLGDLSAEG 107
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfPESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 108 NVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVM 186
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491444527 187 RILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIIS 225
Cdd:PRK13643 185 QLFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIIS 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-224 |
2.47e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREfpagestiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 --------RREYfGfifqryhLLGDLSAEGNVeVPAVYAGVTP----SERKQRATA--LLTELGLGTKTLNRP-SQLSGG 150
Cdd:COG1129 328 giayvpedRKGE-G-------LVLDLSIRENI-TLASLDRLSRggllDRRRERALAeeYIKRLRIKTPSPEQPvGNLSGG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 151 QQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPeLLGLSDRILVMREGRIV 473
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-220 |
2.52e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.60 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:PRK11300 3 QPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLrreyfGFI--FQRYHLLGDLSAEGNVEVP-------AVYAGV--TPSERK------QRATALLTELGLgTKTLNRPS- 145
Cdd:PRK11300 79 RM-----GVVrtFQHVRLFREMTVIENLLVAqhqqlktGLFSGLlkTPAFRRaesealDRAATWLERVGL-LEHANRQAg 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 146 QLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVaknatrIIEISD 220
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKL------VMGISD 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-225 |
2.65e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.77 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCL-----DRPTSGSYKVSGqetGKLEPDQLARLRREyFGFIFQ--RYH 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPA---NLKKIKEVKRLRKE-IGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 99 LLGDlSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGAL 177
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 178 DSHSGVEVMRILRELNAA-GHTIILVTHDM-QVAKNATRIIEISDGEIIS 225
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEyKKRIIMVTHNMdQVLRIADEVIVMHEGKVIS 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-225 |
3.50e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 95.67 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpaGEStiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLR 86
Cdd:TIGR03410 1 LEVSNLNVYY--GQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATAL---LTELglgtktLNRPS-QLSGGQQQRVSIARALM 162
Cdd:TIGR03410 77 ---IAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELfpvLKEM------LGRRGgDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 163 NGGDVILADEPTgaldshSGV------EVMRILRELNA-AGHTIILVTHDMQVAKN-ATRIIEISDGEIIS 225
Cdd:TIGR03410 148 TRPKLLLLDEPT------EGIqpsiikDIGRVIRRLRAeGGMAILLVEQYLDFARElADRYYVMERGRVVA 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-228 |
3.73e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 30 DLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlarlrREyFGFIFQRYHLLGDLSAEGNV 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR-----RP-VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 110 EVpavyaGVTP-----SERKQRATALLTELGLgTKTLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGV 183
Cdd:PRK10771 93 GL-----GLNPglklnAAQREKLHAIARQMGI-EDLLARlPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491444527 184 EVMRILRELNAAGH-TIILVTHDMQ-VAKNATRIIEISDGEIISDRP 228
Cdd:PRK10771 167 EMLTLVSQVCQERQlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGP 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-219 |
5.27e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.17 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLvrEFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:PRK10247 2 QENSPLLQLQNV--GYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLarlrREYFGFIFQRYHLLGDlSAEGNVEVPAVYAGVTPSERKQRATalLTELGLGTKTLNRP-SQLSGGQQQRVSIAR 159
Cdd:PRK10247 78 IY----RQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTILTKNiAELSGGEKQRISLIR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 160 ALMNGGDVILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDMQVAKNATRIIEIS 219
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-210 |
9.87e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.82 E-value: 9.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgklEPDQlARLRREYFGFIFQRYHLLGDLS 104
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP----VPAR-ARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVE 184
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180
....*....|....*....|....*.
gi 491444527 185 VMRILRELNAAGHTIILVTHDMQVAK 210
Cdd:PRK13536 211 IWERLRSLLARGKTILLTTHFMEEAE 236
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-215 |
2.70e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 95.36 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLD---RPTSGSYKVSGQETGKLEPD 80
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLRREYFGFIFQ--RYHL-----LGDLSAEGnveVPAVYAGVT----PSERKQRATALLTELGLG--TKTLNR-PSQ 146
Cdd:COG4170 82 ERRKIIGREIAMIFQepSSCLdpsakIGDQLIEA---IPSWTFKGKwwqrFKWRKKRAIELLHRVGIKdhKDIMNSyPHE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 147 LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHT-IILVTHDMQ-VAKNATRI 215
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTsILLISHDLEsISQWADTI 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-228 |
2.79e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.82 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCL-----DRPTSGSYKVSGQETGKLE 78
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 79 pdqLARLRREyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERK--QRATALLTELGLGTKTLNR----PSQLSGGQQ 152
Cdd:PRK14247 77 ---VIELRRR-VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLWDEVKDRldapAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 153 QRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAgHTIILVTH-DMQVAKNATRIIEISDGEIISDRP 228
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHfPQQAARISDYVAFLYKGQIVEWGP 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-228 |
3.92e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.31 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILgCLDRPtSGSYkvSGQETGKLEPDQLA 83
Cdd:PRK13549 3 EYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYP-HGTY--EGEIIFEGEELQAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLR---REYFGFIFQRYHLLGDLS-AE----GNVEVPAvyaGVTPSERK-QRATALLTELGLGTKTLNRPSQLSGGQQQR 154
Cdd:PRK13549 75 NIRdteRAGIAIIHQELALVKELSvLEniflGNEITPG---GIMDYDAMyLRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 155 VSIARALMNGGDVILADEPTGALdSHSGVEV-MRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISDRP 228
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASL-TESETAVlLDIIRDLKAHGIACIYISHKLnEVKAISDTICVIRDGRHIGTRP 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-223 |
5.60e-21 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 97.13 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNIL-GCLdRPTSGSYKVSGQETGKLEPDQL 82
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 ARlrreYFGFIFQRYHLLGDLSAE-----GNVEVPAVYAGVtpseRKQRATALLTELGLGTKTL--NRPSQLSGGQQQRV 155
Cdd:COG4618 405 GR----HIGYLPQDVELFDGTIAEniarfGDADPEKVVAAA----KLAGVHEMILRLPDGYDTRigEGGARLSGGQRQRI 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 156 SIARALMngGD---VILaDEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:COG4618 477 GLARALY--GDprlVVL-DEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-223 |
7.55e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.10 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRReyfgfIFQRYHLLGDL 103
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA-----LVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVPAVY---AGVTPSERKQRATALLTEL--GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALD 178
Cdd:TIGR00958 570 SVRENIAYGLTDtpdEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 179 shsgVEVMRILREL-NAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:TIGR00958 650 ----AECEQLLQESrSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-223 |
8.82e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 91.38 E-value: 8.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHLLG-- 101
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLFArs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 --DLSAEGNVEVPavYAGVTPSERKQRATALLTELGLG--TKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGAL 177
Cdd:cd03248 104 lqDNIAYGLQSCS--FECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 178 DSHSGVEVMRILRELNAAgHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:cd03248 182 DAESEQQVQQALYDWPER-RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-235 |
1.07e-20 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 96.02 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgkLEPDQLARLrREYFGFIFQRYHLLGDLSAEGN 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREAY-RQLFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 109 VEVPAvyagvtpserkqRATALLTELGLGTKT-------LNRpsQLSGGQQQRVSIARALMNGGDVILADE------PTg 175
Cdd:COG4615 427 EADPA------------RARELLERLELDHKVsvedgrfSTT--DLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE- 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 176 aldshsgvevMR------ILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEIISDRPNVPDQAA 235
Cdd:COG4615 492 ----------FRrvfyteLLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-224 |
1.85e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.80 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLepdQLARLRReYFGFIFQRYHLLgDL 103
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLRR-NIAVVFQDAGLF-NR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVPAvyAGVTPSERK---QRATAL----LTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGA 176
Cdd:PRK13657 424 SIEDNIRVGR--PDATDEEMRaaaERAQAHdfieRKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491444527 177 LDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:PRK13657 502 LDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-223 |
1.85e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLr 86
Cdd:PRK09536 4 IDVSDLSVEF--GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyFGFIFQRYHLLGDLSAEGNVEV---P--AVYAGVTPSERKQRATALltELGLGTKTLNRP-SQLSGGQQQRVSIARA 160
Cdd:PRK09536 79 ---VASVPQDTSLSFEFDVRQVVEMgrtPhrSRFDTWTETDRAAVERAM--ERTGVAQFADRPvTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 161 LMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQV-AKNATRIIEISDGEI 223
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRV 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-228 |
2.04e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.06 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCL-----DRPTSGSYKVSGQETGKLEPDQLaRLRREyFGFIFQRYH 98
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI-EVRRE-VGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 99 LLGDLSAEGNVEVPAVYAGVTPS--ERKQRATALLTELGLGTKTLNR----PSQLSGGQQQRVSIARALMNGGDVILADE 172
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGLVKSkkELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 173 PTGALDSHSGVEVMRILRELNAAgHTIILVTHD-MQVAKNATRIIEISDGEIISDRP 228
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKE-YTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-224 |
4.05e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQET--GK--LEPDQLaRLRREyFGFIFQRYHLL 100
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfGKdiFQIDAI-KLRKE-VGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 101 GDLSAEGNVEVPAVYAGVTPS-ERKQRATALLTELGLGTKT---LNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTG 175
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVydrLNSPaSQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 176 ALDSHSGVEVMRILRELNAAgHTIILVTHD-MQVAKNATRIIEISDGEII 224
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNpQQVARVADYVAFLYNGELV 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-224 |
4.45e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.00 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGESTI-------QILKGIDLTIYEGELVAIVGQSGSGKST----LMNILgcldrPTSGSYKVSGQ 72
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 73 ETGKLEPDQLARLRREyFGFIFQ--------RYHLLgDLSAEGnVEVPavYAGVTPSERKQRATALLTELGLGTKTLNR- 143
Cdd:PRK15134 348 PLHNLNRRQLLPVRHR-IQVVFQdpnsslnpRLNVL-QIIEEG-LRVH--QPTLSAAQREQQVIAVMEEVGLDPETRHRy 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 144 PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGH-TIILVTHDMQVAKN-ATRIIEISDG 221
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRAlCHQVIVLRQG 502
|
...
gi 491444527 222 EII 224
Cdd:PRK15134 503 EVV 505
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-228 |
4.51e-20 |
|
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: 89.48 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQ--------- 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQdpvlfsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 96 RYHL--LGDLSAEgnvEVPAVYAGVtpserKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEP 173
Cdd:cd03244 95 RSNLdpFGEYSDE---ELWQALERV-----GLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 174 TGALDSHSGVEVMRILRElNAAGHTIILVTHDMQVAKNATRIIEISDGEII-SDRP 228
Cdd:cd03244 167 TASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVeFDSP 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-224 |
5.58e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSgqetgklepdqlARLRREYFGfifQRYHLL-GD 102
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------------ETVKIGYFD---QHQEELdPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEGNVevpavyAGVTPSERKQRATALLTELGLGTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHS 181
Cdd:COG0488 394 KTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 182 gvevmriLRELNAA-----GhTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:COG0488 468 -------LEALEEAlddfpG-TVLLVSHDRYfLDRVATRILEFEDGGVR 508
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-224 |
6.08e-20 |
|
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: 88.35 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLD-RPTSGSYKVSGQETGKLEPDQLARLrreyfG-FI-FQRyhl 99
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEERARL-----GiFLaFQY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 100 lgdlsaegnvevPAVYAGVTPSErkqrataLLTELGLGtktlnrpsqLSGGQQQRVSIARALMNGGDVILADEPTGALDS 179
Cdd:cd03217 86 ------------PPEIPGVKNAD-------FLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491444527 180 HSGVEVMRILRELNAAGHTIILVTHDMQVAK--NATRIIEISDGEII 224
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-223 |
8.66e-20 |
|
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: 93.18 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARlr 86
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reYFGFIFQRYHLLGDLSAEG------NVEVPAVYAGVTPSErkqrATALLTELGLGTKTL--NRPSQLSGGQQQRVSIA 158
Cdd:TIGR01842 393 --HIGYLPQDVELFPGTVAENiarfgeNADPEKIIEAAKLAG----VHELILRLPDGYDTVigPGGATLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 159 RALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-204 |
1.12e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.41 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPdqlarLRREYFGFIFQRYHLLGDLS 104
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-----EPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNVEVpavYAGVTPSERKQRATALlTELGLgTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGALDShSGV 183
Cdd:TIGR01189 90 ALENLHF---WAAIHGGAQRTIEDAL-AAVGL-TGFEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGV 163
|
170 180
....*....|....*....|..
gi 491444527 184 E-VMRILRELNAAGHTIILVTH 204
Cdd:TIGR01189 164 AlLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-228 |
1.31e-19 |
|
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: 87.47 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEStiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEpdqLARLR 86
Cdd:cd03369 7 IEVENLSVRYAPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 REyFGFIFQRYHLLgDLSAEGNVEVPAVYagvtpSERKQRATALLTELGLgtktlnrpsQLSGGQQQRVSIARALMNGGD 166
Cdd:cd03369 82 SS-LTIIPQDPTLF-SGTIRSNLDPFDEY-----SDEEIYGALRVSEGGL---------NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 167 VILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEIIS-DRP 228
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIIDYDKILVMDAGEVKEyDHP 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-223 |
1.33e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.04 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQetgKLEPDQLARLRrEYFGFIFQ---------- 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLR-KHIGIVFQnpdnqfvgsi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 96 -RYHLLGDLSaegNVEVPAvyagvtpSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:PRK13648 101 vKYDVAFGLE---NHAVPY-------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 175 GALDSHSGVEVMRILRELNAAGH-TIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-228 |
1.96e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVRefpAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:COG3845 257 VLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RreyFGFI---FQRYHLLGDLSAEGNV------EVPAVYAG-VTPSERKQRATALLTELGLGTKTLNRP-SQLSGGQQQR 154
Cdd:COG3845 334 G---VAYIpedRLGRGLVPDMSVAENLilgryrRPPFSRGGfLDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHD----MQVaknATRIIEISDGEIISDRP 228
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDldeiLAL---SDRIAVMYEGRIVGEVP 485
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-215 |
2.50e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 89.48 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLD---RPTSGSYKVSGQETGKLEPDQ 81
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGVTKdnwRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 82 LARLRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSE--------RKQRATALLTELGLGT-KTLNR--PSQLSGG 150
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGrwwqrfgwRKRRAIELLHRVGIKDhKDAMRsfPYELTEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 151 QQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGH-TIILVTHDMQ-VAKNATRI 215
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHDLQmLSQWADKI 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-226 |
2.54e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARlrreYFGFIFQRYHLLGDLS 104
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEgnvevPAVYAGVTPSE------RKQRATALLTEL-GLGTKTLNRPS--QLSGGQQQRVSIARALMNGGDVILADEPTG 175
Cdd:PRK10253 98 VQ-----ELVARGRYPHQplftrwRKEDEEAVTKAMqATGITHLADQSvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491444527 176 ALDSHSGVEVMRILRELN-AAGHTIILVTHDM-QVAKNATRIIEISDGEIISD 226
Cdd:PRK10253 173 WLDISHQIDLLELLSELNrEKGYTLAAVLHDLnQACRYASHLIALREGKIVAQ 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-224 |
2.66e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.39 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGcLDRPTSGSYKVSGQETGKLEPDQLA 83
Cdd:COG1137 2 MTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYmIVG-LVKPDSGRIFLDGEDITHLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLrreyfGF--------IFQRyhllgdLSAEGNVEvpAV--YAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQ 153
Cdd:COG1137 77 RL-----GIgylpqeasIFRK------LTVEDNIL--AVleLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 154 RVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGhtI-ILVThDMQVakNAT-RIIE----ISDGEII 224
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG--IgVLIT-DHNV--RETlGICDrayiISEGKVL 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-228 |
4.78e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 90.65 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFpageSTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILgCLDRPT---SGSYKVSGQEtgkLEPDQL 82
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYPHgtwDGEIYWSGSP---LKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 ARLRREYFGFIFQRYHLLGDLSAEGNV----EVPAVYAGVTPSERKQRATALLTELGLGTKTLNRP-SQLSGGQQQRVSI 157
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 158 ARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISDRP 228
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLnEVKAVCDTICVIRDGQHVATKD 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-210 |
6.14e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 6.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKS-TLMNILGCLDRP----TSGSYKVSGQETGKLE 78
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 79 PDQLARLRREYFGFIFQRYHL-LGDL-SAEGNV-EVPAVYAGVTPSERKQRATALLTELGL--GTKTLNR-PSQLSGGQQ 152
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVsLNPLhTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDyPHQLSGGER 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 153 QRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAK 210
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVR 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-223 |
8.44e-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: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 9 VSNLVREF-PAGESTIQILkgiDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETgKLEPDQLarlrR 87
Cdd:TIGR01257 931 VKNLVKIFePSGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAV----R 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 88 EYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDV 167
Cdd:TIGR01257 1003 QSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 168 ILADEPTGALDSHSGVEVMRILRELNaAGHTIILVTHDMQVAKN-ATRIIEISDGEI 223
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-221 |
8.80e-19 |
|
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: 85.46 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 21 STIQILKGIDLTIYEGELVAIVGQSGSGKSTLM-NILGCLDRPTSGSYKVSGQETGKLEPDQLARlRREYFGFIFQRYHL 99
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSR-NRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 100 LgDLSAEGNV--EVP---AVYAGVTPSERKQRATALLTeLGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:cd03290 91 L-NATVEENItfGSPfnkQRYKAVTDACSLQPDIDLLP-FGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 175 GALDSHSGVEVMR--ILRELNAAGHTIILVTHDMQVAKNATRIIEISDG 221
Cdd:cd03290 169 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-216 |
9.04e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 9.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNL--VRefpaGEstiQIL-KGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQL 82
Cdd:PRK13538 1 MLEARNLacER----DE---RILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 ARLRreYFGfifqryHLLG---DLSAEGNVevpAVYAGVTPSERKQRATALLTELGL-GTKTLnrP-SQLSGGQQQRVSI 157
Cdd:PRK13538 74 QDLL--YLG------HQPGiktELTALENL---RFYQRLHGPGDDEALWEALAQVGLaGFEDV--PvRQLSAGQQRRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 158 ARALMNGGDVILADEPTGALDSHsGVEVM-RILRELNAAGHTIILVTH-DMQVAKNATRII 216
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAIDKQ-GVARLeALLAQHAEQGGMVILTTHqDLPVASDKVRKL 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-224 |
1.58e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETgKLEPDQLARL 85
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 rREYFGFIFQRY-HLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLgTKTLNRPSQ-LSGGQQQRVSIARALMN 163
Cdd:PRK13636 81 -RESVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDiVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-225 |
1.59e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAgESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgkLEPDQLAR 84
Cdd:PRK13650 3 NIIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 LRREyFGFIFQR--YHLLGdLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALM 162
Cdd:PRK13650 79 IRHK-IGMVFQNpdNQFVG-ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 163 NGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAKNATRIIEISDGEIIS 225
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-224 |
2.56e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.21 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 3 KQALLEVSNLVREFPAGEStiqiLKGIDLTIYEGELVAIVGQSGSGKSTLmniLGCLDR--------PTSGSYKVSGQET 74
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKA----LNSVSLDFYPNEITALIGPSGSGKSTL---LRSINRmndlnpevTITGSIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 75 GKLEPDQLaRLRREyFGFIFQRYHLLgDLSAEGNVEVPAVYAGVTPS-------ERKQRATALLTELG--LGTKTLNrps 145
Cdd:PRK14239 75 YSPRTDTV-DLRKE-IGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKqvldeavEKSLKGASIWDEVKdrLHDSALG--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 146 qLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAgHTIILVTHDMQvakNATRIIEIS----DG 221
Cdd:PRK14239 149 -LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQ---QASRISDRTgfflDG 223
|
...
gi 491444527 222 EII 224
Cdd:PRK14239 224 DLI 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-224 |
5.54e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.77 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtgkLEPDQLARLRrEYFGFIFQRYHLLGDLSA 105
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLR-NQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 106 EgNVevpaVYAGVTPSERKQ--RATALL--------TELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTG 175
Cdd:PRK11176 435 N-NI----AYARTEQYSREQieEAARMAyamdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 176 ALDSHSGVEVMRILRELNaAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:PRK11176 510 ALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-218 |
7.45e-18 |
|
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: 82.54 E-value: 7.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGsyKVSgqetgkLEPDQLARLRREYFGFIFQRYHLLG--- 101
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG--RVL------LNGGPLDFQRDSIARGLLYLGHAPGikt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 DLSAEGNVEVPAVYAGvtpseRKQRATALlTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHS 181
Cdd:cd03231 87 TLSVLENLRFWHADHS-----DEQVEEAL-ARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 491444527 182 GVEVMRILRELNAAGHTIILVTH-DMQVAKNATRIIEI 218
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHqDLGLSEAGARELDL 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-228 |
8.09e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.08 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 16 FPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRrEYFGFIFQ 95
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR-EKVGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 96 R--YHLLGdLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEP 173
Cdd:PRK13640 92 NpdNQFVG-ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 174 TGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAKNATRIIEISDGEII-SDRP 228
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLLaQGSP 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-224 |
1.07e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 86.80 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHLLGDL 103
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEgNVEvpavYAGVTPSERKQRATALLTEL---------GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:COG5265 448 IAY-NIA----YGRPDASEEEVEAAARAAQIhdfieslpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 175 GALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:COG5265 523 SALDSRTERAIQAALREV-ARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-225 |
1.19e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQ-----ETG-KLEPDQlarlRReyFGFIFQRYHLLGD 102
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaEKGiCLPPEK----RR--IGYVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEGNVEvpavYaGVTPSERKQ--RATALLtelGLGtKTLNR-PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDS 179
Cdd:PRK11144 91 YKVRGNLR----Y-GMAKSMVAQfdKIVALL---GIE-PLLDRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491444527 180 HSGVEVMRILRELNAAGHTIIL-VTHDMQ-VAKNATRIIEISDGEIIS 225
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILyVSHSLDeILRLADRVVVLEQGKVKA 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-224 |
1.77e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 20 ESTIQILKGIDLTIYEGELVAIVGQSGSGKStlMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRREYFGFIFQ---- 95
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQnprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 96 --------RYHLLGDLSAegnvevpavyAGVTPSErkQRATALLTELGLGT--KTLNR-PSQLSGGQQQRVSIARALMNG 164
Cdd:PRK10418 91 afnplhtmHTHARETCLA----------LGKPADD--ATLTAALEAVGLENaaRVLKLyPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 165 GDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGvVARLADDVAVMSHGRIV 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-223 |
2.24e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHLLGDLSA 105
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY----RKLFSAVFTDFHLFDQLLG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 106 EGNVEVPavyagvtpserKQRATALLTELGLGTKTL---NRPS--QLSGGQQQRVSIARALMNGGDVILADEPTGALDSH 180
Cdd:PRK10522 415 PEGKPAN-----------PALVEKWLERLKMAHKLEledGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491444527 181 SGVEVMR-ILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:PRK10522 484 FRREFYQvLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-209 |
2.42e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.52 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTlmnILGCLDR-----PT---SGSYKVSGQETGKLEPDQLARLRReyFGFIFQRY 97
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKST---ILRCFNRlndliPGfrvEGKVTFHGKNLYAPDVDPVEVRRR--IGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 98 HLLGDlSAEGNVEVPAVYAGVTPS-----ERKQRATALLTELGlgTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADE 172
Cdd:PRK14243 101 NPFPK-SIYDNIAYGARINGYKGDmdelvERSLRQAALWDEVK--DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 491444527 173 PTGALDSHSGVEVMRILRELNAAgHTIILVTHDMQVA 209
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQA 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-282 |
2.56e-17 |
|
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: 86.54 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDRpTSGSYKVSGQ-----ETGKLEPDQLAR-------LRREYFGF 92
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGSvayvpQQAWIQNDSLREnilfgkaLNEKYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 93 IFQRYHLLGDLSaegnvevpavyagVTPSERKqratallTELGlgTKTLNrpsqLSGGQQQRVSIARALMNGGDVILADE 172
Cdd:TIGR00957 733 VLEACALLPDLE-------------ILPSGDR-------TEIG--EKGVN----LSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 173 PTGALDSHSGVEVMR--ILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEI--ISDRPNVPDQ-------------AA 235
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKIseMGSYQELLQRdgafaeflrtyapDE 866
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 491444527 236 EPGNSDPDAAPALQGKQKKGKSISAWRSTLDRLSEAFQMALLSMNAH 282
Cdd:TIGR00957 867 QQGHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSD 913
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-231 |
2.66e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAGES-------TIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLE 78
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 79 PDQLARLRREyFGFIFQR-YHLLGDLSAEG-NVEVPAVYAGVTPSERKQRATA-LLTELGLGTKTLNR-PSQLSGGQQQR 154
Cdd:PRK10261 393 PGKLQALRRD-IQFIFQDpYASLDPRQTVGdSIMEPLRVHGLLPGKAAAARVAwLLERVGLLPEHAWRyPHEFSGGQRQR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKNAT---------RIIEISDGEII 224
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERIShrvavmylgQIVEIGPRRAV 551
|
....*..
gi 491444527 225 SDRPNVP 231
Cdd:PRK10261 552 FENPQHP 558
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-224 |
4.07e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.27 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVrefpAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILgcLDRP----TSGSYKVSGQETGKLEPDQL 82
Cdd:COG0396 1 LEIKNLH----VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGHPkyevTSGSILLDGEDILELSPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 ARLrreyfG--FIFQRyhllgdlsaegNVEVPavyaGVT------------------PSERKQRATALLTELGLGTKTLN 142
Cdd:COG0396 75 ARA-----GifLAFQY-----------PVEIP----GVSvsnflrtalnarrgeelsAREFLKLLKEKMKELGLDEDFLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 143 RP--SQLSGGQQQRVSIARALMNGGDVILADEPtgalDSHSGVEVMRILRE----LNAAGHTIILVTHdmqvaknATRII 216
Cdd:COG0396 135 RYvnEGFSGGEKKRNEILQMLLLEPKLAILDET----DSGLDIDALRIVAEgvnkLRSPDRGILIITH-------YQRIL 203
|
250
....*....|....*..
gi 491444527 217 E---------ISDGEII 224
Cdd:COG0396 204 DyikpdfvhvLVDGRIV 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-210 |
4.29e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.62 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 13 VREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLmniLGCLDRPTS--GSYKVSGQ-----ETGKLEPDQLARL 85
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTF---LKCLNRMNEleSEVRVEGRveffnQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREyFGFIFQRYHLLgDLSAEGNVEVPAVYAGVTPS-------ERKQRATALLTELGlgTKTLNRPSQLSGGQQQRVSIA 158
Cdd:PRK14258 87 RRQ-VSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491444527 159 RALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGH-TIILVTHDM-QVAK 210
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLhQVSR 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-224 |
4.81e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.08 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 23 IQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLepdQLARLRREYFGFIFQRYHLLGD 102
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 103 LSAEGNVEVPAVYAGVTP-SERKQRATALLTELGlgTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHS 181
Cdd:PRK11614 95 MTVEENLAMGGFFAERDQfQERIKWVYELFPRLH--ERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491444527 182 GVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEII 224
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVV 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-210 |
5.12e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.39 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 8 EVSNLVREFPAGESTIQ--ILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCL-DRPTSGSYKVSGQETGKLEP--DQ 81
Cdd:COG2401 26 RVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGALkGTPVAGCVDVPDNQFGREASliDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 82 LARLrreyfgfifqryhllGDLSAegnvevpavyagvtpserkqrATALLTELGLGTKTL--NRPSQLSGGQQQRVSIAR 159
Cdd:COG2401 106 IGRK---------------GDFKD---------------------AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491444527 160 ALMNGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAK 210
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDVID 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-204 |
7.20e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNL--VRefpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGklepdqlar 84
Cdd:PRK13539 3 LEGEDLacVR----GGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 lrreyFGFIFQRYHLLG-------DLSAEGNVEVPAVYAGVTPSerkqRATALLTELGLGtKTLNRPSQ-LSGGQQQRVS 156
Cdd:PRK13539 68 -----DPDVAEACHYLGhrnamkpALTVAENLEFWAAFLGGEEL----DIAAALEAVGLA-PLAHLPFGyLSAGQKRRVA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491444527 157 IARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTH 204
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-244 |
1.43e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLvrEFPAGEStiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:PRK11831 2 QSVANLVDMRGV--SFTRGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLRREyFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPsERKQRATAL--LTELGLGTKTLNRPSQLSGGQQQRVSIA 158
Cdd:PRK11831 78 RLYTVRKR-MSMLFQSGALFTDMNVFDNVAYPLREHTQLP-APLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 159 RALMNGGDVILADEPTGALDSHS-GVEVmRILRELNAA-GHTIILVTHDMqvaknaTRIIEISD-GEIISDRPNVPDQAA 235
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITmGVLV-KLISELNSAlGVTCVVVSHDV------PEVLSIADhAYIVADKKIVAHGSA 228
|
....*....
gi 491444527 236 EPGNSDPDA 244
Cdd:PRK11831 229 QALQANPDP 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-237 |
1.54e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.22 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREF--PAG---ESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQetgkle 78
Cdd:PRK15112 2 ETLLEVRNLSKTFryRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 79 pdQLA----RLRREYFGFIF----------QRYHLLGDLSAEGNVEvpavyagVTPSERKQRATALLTELGLGTKTLN-R 143
Cdd:PRK15112 76 --PLHfgdySYRSQRIRMIFqdpstslnprQRISQILDFPLRLNTD-------LEPEQREKQIIETLRQVGLLPDHASyY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 144 PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQVAKNAT-RIIEISDG 221
Cdd:PRK15112 147 PHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISdQVLVMHQG 226
|
250
....*....|....*.
gi 491444527 222 EIIsDRPNVPDQAAEP 237
Cdd:PRK15112 227 EVV-ERGSTADVLASP 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-208 |
1.67e-16 |
|
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: 83.30 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 35 EGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVsgqetgklEPDQLARLRReYFGFIFQRYhlLGDLsAEGNVEV--- 111
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDE--------EPSWDEVLKR-FRGTELQDY--FKKL-ANGEIKVahk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 112 -------PAVYAGVTPS------ERKqRATALLTELGLgTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGAL 177
Cdd:COG1245 166 pqyvdliPKVFKGTVREllekvdERG-KLDELAEKLGL-ENILDRDiSELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|.
gi 491444527 178 DSHSGVEVMRILRELNAAGHTIILVTHDMQV 208
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-221 |
5.72e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEstiQILKGIDLTIYEGELVAIVGQSGSGKSTLMNIL--------GCLDRPtsgsykvsgqetgklE 78
Cdd:COG4178 363 LALEDLTLRTPDGR---PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsGRIARP---------------A 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 79 PDQLArlrreyfgFIFQR-YHLLGDL-SAegnvevpAVYAGVTPSERKQRATALLTELGLGT------KTLNRPSQLSGG 150
Cdd:COG4178 425 GARVL--------FLPQRpYLPLGTLrEA-------LLYPATAEAFSDAELREALEAVGLGHlaerldEEADWDQVLSLG 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 151 QQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRElNAAGHTIILVTHDMQVAKNATRIIEISDG 221
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-225 |
9.45e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.60 E-value: 9.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILgcldrptSGSYKvSGQETGKLEPD-QLAR 84
Cdd:NF040905 1 ILEMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGVYP-HGSYEGEILFDgEVCR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 LRR----EYFG--FIFQRYHLLGDLS-AE----GNvEvPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQ 153
Cdd:NF040905 69 FKDirdsEALGivIIHQELALIPYLSiAEniflGN-E-RAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 154 RVSIARALmnGGDV---ILaDEPTGAL-DSHSGvEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIIS 225
Cdd:NF040905 147 LVEIAKAL--SKDVkllIL-DEPTAALnEEDSA-ALLDLLLELKAQGITSIIISHKLnEIRRVADSITVLRDGRTIE 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-204 |
1.08e-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: 75.74 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 10 SNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGclDRPTSGSykVSGQET--GKLEPDQLARlrr 87
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGV--ITGEILinGRPLDKNFQR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 88 eYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKqratalltelglgtktlnrpsqlsggqqqRVSIARALMNGGDV 167
Cdd:cd03232 80 -STGYVEQQDVHSPNLTVREALRFSALLRGLSVEQRK-----------------------------RLTIGVELAAKPSI 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 491444527 168 ILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTH 204
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-208 |
1.66e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 35 EGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYkvsgqeTGKLEPDQLarLRReYFGFIFQRYhlLGDLsAEGNVEV--- 111
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDY------EEEPSWDEV--LKR-FRGTELQNY--FKKL-YNGEIKVvhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 112 -------PAVYAGVT------PSERKqRATALLTELGLgTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGAL 177
Cdd:PRK13409 166 pqyvdliPKVFKGKVrellkkVDERG-KLDEVVERLGL-ENILDRDiSELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|.
gi 491444527 178 DSHSGVEVMRILRELnAAGHTIILVTHDMQV 208
Cdd:PRK13409 244 DIRQRLNVARLIREL-AEGKYVLVVEHDLAV 273
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-228 |
1.71e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.17 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNIL-GCLDRP-------TSGSYKVSGQETGKLEPDQLARLR-------REY 89
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRavlpqaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 90 FGFIFQRYHLLGDLSAegnvevpAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARAL-------- 161
Cdd:PRK13547 96 FAFSAREIVLLGRYPH-------ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 162 -MNGGDVILADEPTGALD---SHSGVEVMRIL-RELNAAGHTIIlvtHDMQV-AKNATRIIEISDGEIISDRP 228
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDlahQHRLLDTVRRLaRDWNLGVLAIV---HDPNLaARHADRIAMLADGAIVAHGA 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
2.19e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.77 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFpagESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGqetgklEPDQLARL 85
Cdd:PRK13652 3 LIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG------EPITKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 R--REYFGFIFQRYH-LLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALM 162
Cdd:PRK13652 74 RevRKFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 163 NGGDVILADEPTGALDSHSGVEVMRILRELNAA-GHTIILVTHDMQ-VAKNATRIIEISDGEIIS 225
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVA 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-228 |
2.54e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.67 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 38 LVAIVGQSGSGKSTLMNILGCLDRPTSGsYKVSGQET--GK--LEPDQLARLRREyFGFIFQRYHLLgDLSAEGNVEVPA 113
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlgGRsiFNYRDVLEFRRR-VGMLFQRPNPF-PMSIMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 114 VYAGVTP-SERKQRATALLTELGLGTKTLNR----PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRI 188
Cdd:PRK14271 126 RAHKLVPrKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491444527 189 LRELnAAGHTIILVTHDM-QVAKNATRIIEISDGEIISDRP 228
Cdd:PRK14271 206 IRSL-ADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGP 245
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-225 |
4.29e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.84 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILG---CLDrptsgsykvsgqeTGKLEPDQ---LARLR----REYFGFIF 94
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD-------------DGRIIYEQdliVARLQqdppRNVEGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 95 --------------QRYHLLGDLSAEgnvevpavyagvTPSER--------------------KQRATALLTELGLGTKT 140
Cdd:PRK11147 85 dfvaegieeqaeylKRYHDISHLVET------------DPSEKnlnelaklqeqldhhnlwqlENRINEVLAQLGLDPDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 141 lnRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDshsgVEVMRILRE--LNAAGhTIILVTHDMQVAKN-ATRIIE 217
Cdd:PRK11147 153 --ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGflKTFQG-SIIFISHDRSFIRNmATRIVD 225
|
....*...
gi 491444527 218 ISDGEIIS 225
Cdd:PRK11147 226 LDRGKLVS 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-222 |
4.31e-15 |
|
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: 75.48 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 35 EGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKvsgqetgklEPDQLARLRREYFGFIFQRY--HLLGDlsaEGNVEVP 112
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD---------DPPDWDEILDEFRGSELQNYftKLLEG---DVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 113 AVYAGVTPSERKQRATALLTE-------------LGLgTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGALD 178
Cdd:cd03236 93 PQYVDLIPKAVKGKVGELLKKkdergkldelvdqLEL-RHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491444527 179 SHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGE 222
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-221 |
6.66e-15 |
|
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: 74.22 E-value: 6.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLM---------------------NILGCLDRPTSGSykVSGqetgkLEP----D 80
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDS--IEG-----LSPaiaiD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 Q--LARLRREYFGFIFQRYHLLGDLsaegnvevpavYAGVTPSERKQrataLLTELGLGTKTLNRPSQ-LSGGQQQRVSI 157
Cdd:cd03270 84 QktTSRNPRSTVGTVTEIYDYLRLL-----------FARVGIRERLG----FLVDVGLGYLTLSRSAPtLSGGEAQRIRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 158 ARALMNG--GDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDG 221
Cdd:cd03270 149 ATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPG 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-225 |
7.31e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 32 TIYEGELVAIVGQSGSGKSTLMN-ILGCLdrPTSGSYKVSGQETGKLEPDQLARlRREYFG------FIFQRYHLLgDLS 104
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLArMAGLL--PGSGSIQFAGQPLEAWSAAELAR-HRAYLSqqqtppFAMPVFQYL-TLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 aegnvevpaVYAGVTPSERKQRATALLTELGLGTKtLNRP-SQLSGGQQQRVSIA-------RALMNGGDVILADEPTGA 176
Cdd:PRK03695 94 ---------QPDKTRTEAVASALNEVAEALGLDDK-LGRSvNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491444527 177 LDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIIS 225
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLA 213
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-221 |
8.41e-15 |
|
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: 72.74 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNilgcldrptSGSYKVSGQETGKLEPdqlarlRREYFGFIFqryhlLGDLSA 105
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLP------KFSRNKLIF-----IDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 106 egnvevpavyagvtpserkqratalLTELGLGTKTLNRP-SQLSGGQQQRVSIARALMNG--GDVILADEPTGALDSHSG 182
Cdd:cd03238 71 -------------------------LIDVGLGYLTLGQKlSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 491444527 183 VEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDG 221
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
26-218 |
8.42e-15 |
|
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: 74.96 E-value: 8.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILG-CLDRPTSGSYKVSG--------QETGKLEP-DQ--LARLRRE---- 88
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYpALARRLHLKKEQPGnhdrieglEHIDKVIViDQspIGRTPRSnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 89 Y---FGFIFQ---------RYH-------LLG-------DLSAEGNVEVpavYAGVTPSERKQRAtalLTELGLGTKTLN 142
Cdd:cd03271 91 YtgvFDEIRElfcevckgkRYNretlevrYKGksiadvlDMTVEEALEF---FENIPKIARKLQT---LCDVGLGYIKLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 143 RPS-QLSGGQQQRVSIARALMN---GGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEI 218
Cdd:cd03271 165 QPAtTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDL 244
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-238 |
9.70e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.04 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTL-MNILGCLdRPTSGSYKVSGQETGKLEPDQLARlrREYFGFIFQ---RYHL 99
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKPLDYSKRGLLAL--RQQVATVFQdpeQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 100 LGDLsaEGNVEVPAVYAGVTPSERKQRATALLTeLGLGTKTLNRPSQ-LSGGQQQRVSIARALMNGGDVILADEPTGALD 178
Cdd:PRK13638 92 YTDI--DSDIAFSLRNLGVPEAEITRRVDEALT-LVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 179 SHSGVEVMRILRELNAAGHTIILVTHDMQVaknatrIIEISDGEIISDRPNVPDQaAEPG 238
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSHDIDL------IYEISDAVYVLRQGQILTH-GAPG 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-223 |
1.19e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDRPTSGSYKVSGqeTGKLEPdQL-----ARLRRE-YFGFIFQryh 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG--TVAYVP-QVswifnATVRDNiLFGSPFD--- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 99 llgdlsaegnvevPAVYagvtpsERKQRATAL-----------LTELGlgtktlNRPSQLSGGQQQRVSIARALMNGGDV 167
Cdd:PLN03130 707 -------------PERY------ERAIDVTALqhdldllpggdLTEIG------ERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 168 ILADEPTGALDSHSGVEVMR--ILRELNaaGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFDkcIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-206 |
1.34e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVREFPAGESTiqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGK-LEP 79
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNGHTA---LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 80 DQLARLRRE-----YFGFIFQRYHLLGDLSAEGNVEVPAvyagvtpSERKQRATALLTELGLGTKTLNRPSQLSGGQQQR 154
Cdd:PRK15056 78 NLVAYVPQSeevdwSFPVLVEDVVMMGRYGHMGWLRRAK-------KRDRQIVTAALARVDMVEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM 206
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNL 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-224 |
1.49e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 4 QALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKS-TLMNILGCLDRptSGSYKVSGQ---------- 72
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--AGGLVQCDKmllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 73 -ETGKLEPDQLARLRREYFGFIFQRyhLLGDLS-----AEGNVEVPAVYAGVTPSERKQRATALLTELGL--GTKTLNR- 143
Cdd:PRK10261 88 iELSEQSAAQMRHVRGADMAMIFQE--PMTSLNpvftvGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeAQTILSRy 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 144 PSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNA-AGHTIILVTHDMQ-VAKNATRIIEISDG 221
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGvVAEIADRVLVMYQG 245
|
...
gi 491444527 222 EII 224
Cdd:PRK10261 246 EAV 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-225 |
7.16e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARlrreyfgfifQRYHLLGDL- 103
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----------KVAYLPQQLp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEVPAVYAGVTP---------SERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:PRK10575 96 AAEGMTVRELVAIGRYPwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491444527 175 GALDSHSGVEVMRILRELNAA-GHTIILVTHDMQV-AKNATRIIEISDGEIIS 225
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMaARYCDYLVALRGGEMIA 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-224 |
8.67e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.59 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSG------SYKVS--GQETgKLEPDQLARlrreyfGFIFQ 95
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpGIKVGylPQEP-QLDPTKTVR------ENVEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 96 RYHLLGDLSAEGNvEVPAVYAgvtpsERKQRATALLTELG--------LGTKTLNR-----------P------SQLSGG 150
Cdd:TIGR03719 92 GVAEIKDALDRFN-EISAKYA-----EPDADFDKLAAEQAelqeiidaADAWDLDSqleiamdalrcPpwdadvTKLSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 151 QQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELnaAGhTIILVTHDMQVAKNATR-IIEISDGEII 224
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHDRYFLDNVAGwILELDRGRGI 237
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-204 |
9.22e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALLEVSNLVrefpAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGclDRP----TSGSYKVSGQETGK 76
Cdd:CHL00131 2 NKNKPILEIKNLH----ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 77 LEPDQLARLRreyfgfIFqryhllgdLSAEGNVEVPavyaGVT---------PSERKQRA-------------TALLTEL 134
Cdd:CHL00131 76 LEPEERAHLG------IF--------LAFQYPIEIP----GVSnadflrlayNSKRKFQGlpeldplefleiiNEKLKLV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 135 GLGTKTLNRPSQ--LSGGQQQRVSIAR-ALMNGGDVILaDEPTGALDSHSGVEVMRILRELNAAGHTIILVTH 204
Cdd:CHL00131 138 GMDPSFLSRNVNegFSGGEKKRNEILQmALLDSELAIL-DETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-223 |
1.00e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSykVSGQETGKLEPDQL----ARLRREYFGFIFQRYHLL 100
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR--VWAERSIAYVPQQAwimnATVRGNILFFDEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 101 GDLsaegnVEVPAVYAGVtpserKQRATALLTELGlgTKTLNrpsqLSGGQQQRVSIARALMNGGDVILADEPTGALDSH 180
Cdd:PTZ00243 753 ADA-----VRVSQLEADL-----AQLGGGLETEIG--EKGVN----LSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491444527 181 SGVEVMR--ILRELnaAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:PTZ00243 817 VGERVVEecFLGAL--AGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-225 |
1.46e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 5 ALLEVSNLVREFPAGestiQILKGIDLTIYEGELVAIVGQSGSGKST-LMNILGCLDRpTSGSYKVSGQETGKLEPDqlA 83
Cdd:PRK10895 2 ATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGIVPR-DAGNIIIDDEDISLLPLH--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 84 RLRREyFGFIFQRYHLLGDLSAEGNV-EVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALM 162
Cdd:PRK10895 75 RARRG-IGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 163 NGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNA-TRIIEISDGEIIS 225
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVcERAYIVSQGHLIA 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-223 |
2.67e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDRPTSGSYKVSGqeTGKLEPDqlarlrreyFGFIFQryhllgdls 104
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG--SVAYVPQ---------VSWIFN--------- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 aeGNVEVPAVYAGVTPSERKQRA---TALLTELGL-----GTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGA 176
Cdd:PLN03232 693 --ATVRENILFGSDFESERYWRAidvTALQHDLDLlpgrdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491444527 177 LDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-205 |
2.86e-13 |
|
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: 72.66 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSgqETGKLepdqlarlr 86
Cdd:TIGR03719 323 IEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKL--------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyfGFIFQ-RYHLLG------------DLSAEGNVEVPAvyagvtpserkqRATallteLGL----GTKTLNRPSQLSG 149
Cdd:TIGR03719 388 ----AYVDQsRDALDPnktvweeisgglDIIKLGKREIPS------------RAY-----VGRfnfkGSDQQKKVGQLSG 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 150 GQQQRVSIARALMNGGDVILADEPTGALDshsgVEVMRILRE--LNAAGHTIIlVTHD 205
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEalLNFAGCAVV-ISHD 499
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-224 |
3.09e-13 |
|
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: 68.83 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 11 NLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLdrpTSGSYKVSGQET-GKLEPDQlarlrrey 89
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHyNGIPYKE-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 90 fgfIFQRYHllGDL--SAEGNVEVPavyagvtpserkqratALLTELGLGTKTLNRPSQ----LSGGQQQRVSIARALMN 163
Cdd:cd03233 77 ---FAEKYP--GEIiyVSEEDVHFP----------------TLTVRETLDFALRCKGNEfvrgISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 164 GGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHdMQVAKNAT----RIIEISDGEII 224
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSL-YQASDEIYdlfdKVLVLYEGRQI 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-223 |
3.68e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLvrefpAGEStiqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNIL-GCLDRpTSGSYKVSGQETGKLEP-DQLAR 84
Cdd:PRK10762 258 LKVDNL-----SGPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPqDGLAN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 lrreyfGFIF-----QRYHLLGDLSAEGNVEVPAV-----YAGVTPSERKQRATALLTELgLGTKTLNRPSQ---LSGGQ 151
Cdd:PRK10762 328 ------GIVYisedrKRDGLVLGMSVKENMSLTALryfsrAGGSLKHADEQQAVSDFIRL-FNIKTPSMEQAiglLSGGN 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 152 QQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEI 223
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRI 473
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
387-661 |
6.26e-13 |
|
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: 72.16 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 387 VSNDYFDVKGLVFKDGQTFDQRSVRDRSQDVVIDTNT--QKQFFGDgSNPIGQVVLLGSVPARIIGIVEPQTSGMGSDDt 464
Cdd:TIGR03434 115 VSANFFPVLGVQPALGRLFTPEDDRPGAPPVVVLSYAlwQRRFGGD-PAVVGRTIRLNGRPYTVVGVMPPGFTFPGRDP- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 465 lNVYMP---YTTVMSRMLGQSNVRNIVVRINDKYSTAAAE---NAIVNLLTQRHGAQDI-FTMNSDSIRQTIEKTTSTMT 537
Cdd:TIGR03434 193 -DVWVPlamDPALAGSANRGSRWLRVIGRLKPGVTLAQAQaelDAIAARLAAAYPDTNAgRGLAVTPLRESLVGDVRPPL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 538 LLVSAIAVISLVVGGIGVMNIMLVSVTERTQEIGVRMAVGARQSDILQQFLIEAILVCLIGGVLGVLLSLGLGQLINKFA 617
Cdd:TIGR03434 272 LVLLGAVGLVLLIACANVANLLLARAAARQREIAVRLALGAGRGRLVRQLLTESLLLALAGGALGLLLAYWGLRLLLALL 351
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 491444527 618 GGNFSVAYSST---SIIA-AFVCSTLIGVVFGFLPAKNAAKLDPVAAL 661
Cdd:TIGR03434 352 PASLPRLLEISldgRVLLfALALSLLTGLLFGLAPALQATRSDLAEAL 399
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-222 |
9.93e-13 |
|
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: 69.12 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTL-MNILGCLDrPTSGSYKVSGQ-----ETGKLEPDQLarlrRE--YFGFIFQR 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLlMLILGELE-PSEGKIKHSGRisfssQFSWIMPGTI----KEniIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 97 YHLLGDLSAEGNVEVPAVYAgvtpserkQRATALLTELGLgtktlnrpsQLSGGQQQRVSIARALMNGGDVILADEPTGA 176
Cdd:cd03291 127 YRYKSVVKACQLEEDITKFP--------EKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 177 LDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGE 222
Cdd:cd03291 190 LDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-236 |
2.00e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 14 REFPAGESTIQI--LKG------IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLAR- 84
Cdd:PRK11288 249 RPRPLGEVRLRLdgLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRa 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 ---LRREyfgfifqryhllgDLSAEGNVEVPAV-------------YAGVTPSERKQRATALLTELGLGTKTLNRPSQ-- 146
Cdd:PRK11288 329 gimLCPE-------------DRKAEGIIPVHSVadninisarrhhlRAGCLINNRWEAENADRFIRSLNIKTPSREQLim 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 147 -LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHD-MQVAKNATRIIEISDGEII 224
Cdd:PRK11288 396 nLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRIA 475
|
250
....*....|..
gi 491444527 225 SDRPNvpDQAAE 236
Cdd:PRK11288 476 GELAR--EQATE 485
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-238 |
2.25e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.13 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 13 VREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGF 92
Cdd:PRK10789 318 IRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 93 IFQRYHLLGDlSAEGNVEVPAVYAgvTPSERKQRAT-------ALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGG 165
Cdd:PRK10789 394 VSQTPFLFSD-TVANNIALGRPDA--TQQEIEHVARlasvhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELnAAGHTIILVTHDMQVAKNATRIIEISDGEIISdRPNVPDQAAEPG 238
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTEASEILVMQHGHIAQ-RGNHDQLAQQSG 541
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-220 |
2.25e-12 |
|
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: 65.64 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGEStiqILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYkvsgqetGKLEPDQLArlr 86
Cdd:cd03223 1 IELENLSLATPDGRV---LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------GMPEGEDLL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyfgFIFQR-YHLLGDLsaegnvevpavyagvtpseRKQratalltelglgtktLNRPSQ--LSGGQQQRVSIARALMN 163
Cdd:cd03223 68 -----FLPQRpYLPLGTL-------------------REQ---------------LIYPWDdvLSGGEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491444527 164 GGDVILADEPTGALDshSGVEvMRILRELNAAGHTIILVTHDMQVAKNATRIIEISD 220
Cdd:cd03223 109 KPKFVFLDEATSALD--EESE-DRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| FtsX |
pfam02687 |
FtsX-like permease family; This is a family of predicted permeases and hypothetical ... |
541-657 |
2.51e-12 |
|
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: 64.19 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 541 SAIAVISLVVGGIGVMNIMLVSVTERTQEIGVRMAVGARQSDILQQFLIEAILVCLIGGVLGVLLSLGLGQLINK---FA 617
Cdd:pfam02687 1 ILFSLLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVIGLLLGLLLAKLIAIllySS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 491444527 618 GGNFSVAYSSTSIIAAFVCSTLIGVVFGFLPAKNAAKLDP 657
Cdd:pfam02687 81 GISLPILVPPLSILIALLLALLIALLASLLPALRIRKINP 120
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-237 |
3.52e-12 |
|
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: 66.66 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 19 GESTIQILKGidlTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSG---------SYKVSgqetgKLEPDQlarlrrey 89
Cdd:cd03237 11 GEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdieieldtvSYKPQ-----YIKADY-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 90 fgfifqryhllgdlsaEGNVEvpAVYAGVTPS--ERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDV 167
Cdd:cd03237 75 ----------------EGTVR--DLLSSITKDfyTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 168 ILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAKN-ATRIIeISDGEiisdrPNVPDQAAEP 237
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFaENNEKTAFVVEHDIIMIDYlADRLI-VFEGE-----PSVNGVANPP 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-221 |
3.83e-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: 69.94 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTL-MNILGCLDrPTSGSYKVSGQ-----ETGKLEPDQLarlrRE--YFGFIFQR 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLlMMIMGELE-PSEGKIKHSGRisfspQTSWIMPGTI----KDniIFGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 97 YHllgdlsaegnvevpavYAGVTPSERKQRATALLTE-----LGLGTKTLnrpsqlSGGQQQRVSIARALMNGGDVILAD 171
Cdd:TIGR01271 516 YR----------------YTSVIKACQLEEDIALFPEkdktvLGEGGITL------SGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491444527 172 EPTGALDSHSGVEVM-RILRELnAAGHTIILVTHDMQVAKNATRIIEISDG 221
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFeSCLCKL-MSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
24-206 |
8.36e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQetgklepdqlarLRreyFGFIFQRYHLlgDL 103
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR---IGYVPQKLYL--DT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVEvpaVYAGVTPSERKQRATALLTELGLGtKTLNRPSQ-LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:PRK09544 81 TLPLTVN---RFLRLRPGTKKEDILPALKRVQAG-HLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*...
gi 491444527 183 VE----VMRILRELNAAghtIILVTHDM 206
Cdd:PRK09544 157 VAlydlIDQLRRELDCA---VLMVSHDL 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-208 |
9.84e-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: 67.89 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 32 TIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSG--------SYKvsGQEtgkLEPDQLARLRreyfgfifqryHLLGDL 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlkiSYK--PQY---ISPDYDGTVE-----------EFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEgNVEVPAVYagvtpserkqraTALLTELGLgTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:COG1245 426 NTD-DFGSSYYK------------TEIIKPLGL-EKLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180
....*....|....*....|....*..
gi 491444527 183 VEVMRILREL-NAAGHTIILVTHDMQV 208
Cdd:COG1245 492 LAVAKAIRRFaENRGKTAMVVDHDIYL 518
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-202 |
4.17e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 21 STIQILKGI------------DLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLARLRRE 88
Cdd:PRK10938 2 SSLQISQGTfrlsdtktlqlpSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 89 yfgfIFQRYHllGDLSAEGNVEVPAVYAGVTPSERK--QRATALLTELGLgTKTLNRP-SQLSGGQQQRVSIARALMNGG 165
Cdd:PRK10938 82 ----EWQRNN--TDMLSPGEDDTGRTTAEIIQDEVKdpARCEQLAQQFGI-TALLDRRfKYLSTGETRKTLLCQALMSEP 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 491444527 166 DVILADEPTGALDSHSGVEVMRILRELNAAGHTIILV 202
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-236 |
5.36e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 27 KGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEP-DQLAR-------LRREYfGFifqryh 98
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKgmayiteSRRDN-GF------ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 99 lLGDLSAEGNVEVP-----AVYAG----VTPSERKQRATALLTELGLGTKTLNRP-SQLSGGQQQRVSIARALMNGGDVI 168
Cdd:PRK09700 353 -FPNFSIAQNMAISrslkdGGYKGamglFHEVDEQRTAENQRELLALKCHSVNQNiTELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 169 LADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISDRPNVPDQAAE 236
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-260 |
5.79e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 23 IQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlepDQLARLRREYFGFIFQ------- 95
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLK---DINLKWWRSKIGVVSQdpllfsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 96 ------RYHL--LGDLSAEGN---------------------------------------VEVPAVYAGVTPSE-----R 123
Cdd:PTZ00265 475 siknniKYSLysLKDLEALSNyynedgndsqenknkrnscrakcagdlndmsnttdsnelIEMRKNYQTIKDSEvvdvsK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 124 KQRATALLTELGLGTKTL--NRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTI-I 200
Cdd:PTZ00265 555 KVLIHDFVSALPDKYETLvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItI 634
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 201 LVTHDMQVAKNATRIIEISDGEiISDRPNVPDQAAEPGNSDPDAAPALQGKQKKGKSISA 260
Cdd:PTZ00265 635 IIAHRLSTIRYANTIFVLSNRE-RGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNN 693
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
26-218 |
6.18e-11 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 65.80 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMN--ILGCLDR------PTSGSYK-VSGQE----------------------- 73
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANrlngakTVPGRYTsIEGLEhldkvihidqspigrtprsnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 74 -TGKLEP-DQL------ARLR-----REYF-------------GFIFQRYHLLGDLS--------AEGNVEVPAV-YAGV 118
Cdd:TIGR00630 704 yTGVFDEiRELfaetpeAKVRgytpgRFSFnvkggrceacqgdGVIKIEMHFLPDVYvpcevckgKRYNRETLEVkYKGK 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 119 TPSE--------------------RKQRataLLTELGLGTKTLNRPS-QLSGGQQQRVSIARALM---NGGDVILADEPT 174
Cdd:TIGR00630 784 NIADvldmtveeayeffeavpsisRKLQ---TLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELSkrsTGRTLYILDEPT 860
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 491444527 175 GALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEI 218
Cdd:TIGR00630 861 TGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDL 904
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-205 |
7.98e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.19 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 21 STIQILKGIDL-------TIYEGELVAIVGQSGSGKSTLMNIL--------GCLDRPTSGSYKVSGQETGKLEPDQLARL 85
Cdd:PRK10636 5 SSLQIRRGVRVlldnataTINPGQKVGLVGKNGCGKSTLLALLkneisadgGSYTFPGNWQLAWVNQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 ---RREYFgfifQRYHLLGDLSAEGNVEVPAVYAG----VTPSERKQRATALLTELGLGTKTLNRP-SQLSGGQQQRVSI 157
Cdd:PRK10636 85 idgDREYR----QLEAQLHDANERNDGHAIATIHGkldaIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491444527 158 ARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAaghTIILVTHD 205
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHD 205
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-205 |
8.61e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 42 VGQSGSGKSTLMNILGCLDRPTSGSykVS---GQETGKLEPDQlarlrreyfgFIFQRYHLLgDLSAEGNVEVPAV---- 114
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGN--VSldpNERLGKLRQDQ----------FAFEEFTVL-DTVIMGHTELWEVkqer 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 115 ---YAGVTPSER--------------------KQRATALLTELGLGTKTLNRP-SQLSGGQQQRVSIARALMNGGDVILA 170
Cdd:PRK15064 100 driYALPEMSEEdgmkvadlevkfaemdgytaEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 491444527 171 DEPTGALDSHSgvevMRILRE-LNAAGHTIILVTHD 205
Cdd:PRK15064 180 DEPTNNLDINT----IRWLEDvLNERNSTMIIISHD 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-227 |
9.59e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 9.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 6 LLEVSNLVREFpaGESTIQILKGidlTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSG--------SYKvsGQEtgkL 77
Cdd:PRK13409 340 LVEYPDLTKKL--GDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpelkiSYK--PQY---I 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 78 EPDQLARLRrEYFGFIFQRYHllgdlSAEGNVEVpavyagVTPserkqratallteLGLgTKTLNRP-SQLSGGQQQRVS 156
Cdd:PRK13409 410 KPDYDGTVE-DLLRSITDDLG-----SSYYKSEI------IKP-------------LQL-ERLLDKNvKDLSGGELQRVA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491444527 157 IARALMNGGDVILADEPTGALDSHSGVEVMRILR---ELNAAghTIILVTHDmqvaknatrIIEIsdgEIISDR 227
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRriaEEREA--TALVVDHD---------IYMI---DYISDR 523
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-224 |
1.45e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 22 TIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCldrPTSGSYK-VSGQET-GKLEPDQLARlrreyfgfifqryHL 99
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIgVEGVITyDGITPEEIKK-------------HY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 100 LGDL--SAEGNVEVPAV------------------YAGVTPSERKQRATAL-LTELGL----GTKTLNRPSQ-LSGGQQQ 153
Cdd:TIGR00956 137 RGDVvyNAETDVHFPHLtvgetldfaarcktpqnrPDGVSREEYAKHIADVyMATYGLshtrNTKVGNDFVRgVSGGERK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491444527 154 RVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHdMQVAKNA----TRIIEISDGEII 224
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAI-YQCSQDAyelfDKVIVLYEGYQI 290
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-237 |
1.45e-10 |
|
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: 60.66 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 33 IYEGELVAIVGQSGSGKSTLMNILGcldrptsgsykvsgqetGKLEPDqlarlrreyfgfifqryhllgdlsaEGNVEVP 112
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILA-----------------GQLIPN-------------------------GDNDEWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 113 avyaGVTPSERKQRAtalltelglgtktlnrpsQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILREL 192
Cdd:cd03222 60 ----GITPVYKPQYI------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491444527 193 NAAGH-TIILVTHDMQVAKNATRIIEISDGEiisdrPNVPDQAAEP 237
Cdd:cd03222 118 SEEGKkTALVVEHDLAVLDYLSDRIHVFEGE-----PGVYGIASQP 158
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-224 |
1.57e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.14 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 1 MTKQALlEVSNLVREFPAGEstiqILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSgqETGKLepd 80
Cdd:PRK15064 315 LHRNAL-EVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--ENANI--- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 qlarlrreyfGFIFQryhllgDLSAEGNVEVP-----AVYAgvTPSERKQRATALLTELGLGTKTLNRPSQ-LSGGQQQR 154
Cdd:PRK15064 385 ----------GYYAQ------DHAYDFENDLTlfdwmSQWR--QEGDDEQAVRGTLGRLLFSQDDIKKSVKvLSGGEKGR 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 155 VSIARALMNGGDVILADEPTGALDshsgvevMRILRELNAA-----GhTIILVTHDMQ-VAKNATRIIEISDGEII 224
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMAlekyeG-TLIFVSHDREfVSSLATRIIEITPDGVV 514
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-204 |
1.70e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQEtGKLEPDQLARLrreyfGFIFQRYHLLGDLS 104
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRT-----GFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNVEVPAVY---AGVTPSERKQRATALLTELGLgTKTLNRP------SQLSGGQQQRVSIARALMNGGDVILADEPTG 175
Cdd:PLN03211 157 VRETLVFCSLLrlpKSLTKQEKILVAESVISELGL-TKCENTIignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180
....*....|....*....|....*....
gi 491444527 176 ALDSHSGVEVMRILRELNAAGHTIILVTH 204
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
267-664 |
1.98e-10 |
|
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: 64.05 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 267 RLSEAFQMALLSMNAHRMRTFLtmLGIIIGIASVVTVVALGKGSQQQILSNISSLGTNTITVFQGRGFGDnsktanfKTL 346
Cdd:COG3127 3 SLRLALRLAWRDLRAGELRLLL--LALVLGVAAVAAVGSFSDRLQAGLARQARELLGGDLVLRSDQPLPA-------AWL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 347 VPADADALMTQPYVSAVSPIVSTSKTMRyqqneanATINGVSNDYFDVKGLVFKDGQTF-DQRSVRDRSQDVVIDTNTQK 425
Cdd:COG3127 74 AQARALGLRVSRTVEFRSMARAGDGSQL-------VEVKAVDGAYPLYGELELAPAPPLaDALAGGPAPGEVWVDPRLLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 426 QFfgdGSNpIGQVVLLGSVPARIIGIV--EPQTSGMGSDDTLNVYMPYTTVMSRMLGQSNVRnivvrINDKYSTAAAENA 503
Cdd:COG3127 147 RL---GLK-VGDTIRLGDATFTIAGVLtrEPDRGGGGFSLAPRVLINLADLEATGLIQPGSR-----VRYRYLVAGPDAD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 504 IVNL---LTQRHGA-QDIFTMNSDS--IRQTIEKTTSTMTLlvsaIAVISLVVGGIGVMNIMLVSVTERTQEIGVRMAVG 577
Cdd:COG3127 218 LEALrawLEPALPAgQRVRTVEDARpeLGRALDRAEQFLLL----VALLALLLAGVAVANAARRYVARRLDTIALLRCLG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 578 ARQSDILQQFLIEAILVCLIGGVLGVLLSLGLGQLINKFAGGNFSV----AYSSTSIIAAFVCSTLIGVVFGFLPAKNAA 653
Cdd:COG3127 294 ASRRQIFRIYLLQLLLLGLLGSLLGLLLGALLQALLAALLADLLPVplepALSPLPLLLGLLVGLLVLLLFALPPLLRLR 373
|
410
....*....|.
gi 491444527 654 KLDPVAALSRE 664
Cdd:COG3127 374 RVPPLRVLRRD 384
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-221 |
2.23e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 64.08 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 124 KQRaTALLTELGLGTKTLNRP-SQLSGGQQQRVSIARAL---MNGGDVILaDEPTGALDSHSGVEVMRILRELNAAGHTI 199
Cdd:PRK00635 454 KSR-LSILIDLGLPYLTPERAlATLSGGEQERTALAKHLgaeLIGITYIL-DEPSIGLHPQDTHKLINVIKKLRDQGNTV 531
|
90 100
....*....|....*....|..
gi 491444527 200 ILVTHDMQVAKNATRIIEISDG 221
Cdd:PRK00635 532 LLVEHDEQMISLADRIIDIGPG 553
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-223 |
2.32e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQlaRLRReyfGFIF-----QRYHLLGDL 103
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ--RLAR---GLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 104 SAEGNVeVPAVYAGVTPSERKQRATALLTEL--GLGTKtLNRPSQ----LSGGQQQRVSIARALMNGGDVILADEPTGAL 177
Cdd:PRK15439 357 PLAWNV-CALTHNRRGFWIKPARENAVLERYrrALNIK-FNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491444527 178 DSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEI 223
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLeEIEQMADRVLVMHQGEI 481
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-218 |
3.01e-10 |
|
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: 59.30 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGcldrptsgsykvsgqetgklepdqlarlrreyFGFIFQRYHLLGDLS 104
Cdd:cd03227 10 YFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG--------------------------------LALGGAQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNVEVPAVYAgvtpserkQRATALLtelglgtktlnrpsQLSGGQQQRVSIARAL----MNGGDVILADEPTGALDSH 180
Cdd:cd03227 58 VKAGCIVAAVSA--------ELIFTRL--------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR 115
|
170 180 190
....*....|....*....|....*....|....*...
gi 491444527 181 SGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEI 218
Cdd:cd03227 116 DGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-204 |
4.01e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEpdqlarlRREYFGFIFQRYHLLGDLS 104
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNVEVPAVYAGVTPserKQRATALLTELGLG--TKTLNRpsQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSG 182
Cdd:PRK13543 99 TLENLHFLCGLHGRRA---KQMPGSALAIVGLAgyEDTLVR--QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
170 180
....*....|....*....|..
gi 491444527 183 VEVMRILRELNAAGHTIILVTH 204
Cdd:PRK13543 174 TLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-215 |
4.19e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTIYEGELVAIVGQSGSGKSTLMNIL-GCLDrPTSGSYKVSGQEtgkLEPDQLARLRReyFGFIFQRYHLLGDLSAEG 107
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLP-ASEGEAWLFGQP---VDAGDIATRRR--VGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 108 NVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTgaldshSGVE-VM 186
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT------SGVDpVA 432
|
170 180 190
....*....|....*....|....*....|....*
gi 491444527 187 R-----ILRELN-AAGHTIILVTHDMQVAKNATRI 215
Cdd:NF033858 433 RdmfwrLLIELSrEDGVTIFISTHFMNEAERCDRI 467
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
523-664 |
1.26e-09 |
|
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: 61.36 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 523 DSIRQTIEKTTSTMTLLVSAIAVISLVVGGIGVMNIMLVSVTERTQEIGVRMAVGARQSDILQQFLIEAILVCLIGGVLG 602
Cdd:COG3127 690 DAILDQVRDILDQVSLAVEFLAGFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLA 769
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491444527 603 VLLSLGLGQLINKFAgGNFSVAYSSTSIIAAFVCSTLIGVVFGFLPAKNAAKLDPVAALSRE 664
Cdd:COG3127 770 ALLAELAGWALARFV-FDLPFSPPWWLWLAGLLGGALLVLLAGLLGARRVLRQPPLEVLREE 830
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-223 |
1.35e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 22 TIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQetgklepdqlarlrreyFGFIFQRYHLLG 101
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAISAGLSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 DLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHS 181
Cdd:PRK13546 99 QLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491444527 182 GVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEI 223
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLgQVRQFCTKIAWIEGGKL 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-205 |
1.71e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpaGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSgqETGKLepdqlarlr 86
Cdd:PRK11819 325 IEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVKL--------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 87 reyfGFIFQ-RYHLLG------------DLSAEGNVEVPA-VYAG---VTPSERKQRAtalltelglgtktlnrpSQLSG 149
Cdd:PRK11819 390 ----AYVDQsRDALDPnktvweeisgglDIIKVGNREIPSrAYVGrfnFKGGDQQKKV-----------------GVLSG 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 150 GQQQRVSIARALMNGGDVILADEPTGALDshsgVEVMRILRE--LNAAGHTIIlVTHD 205
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLD----VETLRALEEalLEFPGCAVV-ISHD 501
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-204 |
2.17e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlepdQLARLRREyFGFIFQRYHLLGDLS 104
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQKQ-LCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNvevpaVYAGVTPSERKQRATALLTELGLGtKTLNRP-SQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGV 183
Cdd:PRK13540 91 LREN-----CLYDIHFSPGAVGITELCRLFSLE-HLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|.
gi 491444527 184 EVMRILRELNAAGHTIILVTH 204
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-218 |
3.85e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 60.23 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 131 LTELGLGTKTLNRP-SQLSGGQQQRVSIARALMNGGD---VILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM 206
Cdd:PRK00635 793 LCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
90
....*....|..
gi 491444527 207 QVAKNATRIIEI 218
Cdd:PRK00635 873 HVVKVADYVLEL 884
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-224 |
6.49e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSG------SYKVsG---QETgKLEPDQ---------LARL 85
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGearpapGIKV-GylpQEP-QLDPEKtvrenveegVAEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RReyfgfIFQRYHllgdlsaegnvEVPAVYAgvTPSERKQratALLTELG-------------LGTK------TLNRP-- 144
Cdd:PRK11819 99 KA-----ALDRFN-----------EIYAAYA--EPDADFD---ALAAEQGelqeiidaadawdLDSQleiamdALRCPpw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 145 ----SQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSgVEVM-RILRELnaAGhTIILVTHDMQVAKNATR-IIEI 218
Cdd:PRK11819 158 dakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLeQFLHDY--PG-TVVAVTHDRYFLDNVAGwILEL 233
|
....*.
gi 491444527 219 SDGEII 224
Cdd:PRK11819 234 DRGRGI 239
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-221 |
7.69e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLepdQLARLRREyFGFIFQRyHLLGDLS 104
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY---GLRELRRQ-FSMIPQD-PVLFDGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNV---------EVPAVYAGVTPSERkqraTALLTElGLGTKTLNRPSQLSGGQQQRVSIARALMN-GGDVILADEPT 174
Cdd:PTZ00243 1400 VRQNVdpfleassaEVWAALELVGLRER----VASESE-GIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491444527 175 G----ALDSHSGVEVMRILrelnaAGHTIILVTHDMQVAKNATRIIEISDG 221
Cdd:PTZ00243 1475 AnidpALDRQIQATVMSAF-----SAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
13-204 |
1.05e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.70 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 13 VREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGclDRPT----SGSYKVSG----QETgklepdqLAR 84
Cdd:PLN03140 883 MKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--GRKTggyiEGDIRISGfpkkQET-------FAR 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 LRreyfGFIFQryhllGDL-SAEGNVEVPAVYAGV------TPSERKQRATALLTEL----GLGTKTLNRP--SQLSGGQ 151
Cdd:PLN03140 954 IS----GYCEQ-----NDIhSPQVTVRESLIYSAFlrlpkeVSKEEKMMFVDEVMELveldNLKDAIVGLPgvTGLSTEQ 1024
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491444527 152 QQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTH 204
Cdd:PLN03140 1025 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-223 |
1.25e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGclDRPTSGSYKVS--GQETGKLEpdQLARLRReYFGFIFQRYHL-- 99
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlITG--DHPQGYSNDLTlfGRRRGSGE--TIWDIKK-HIGYVSSSLHLdy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 100 -----LGDLSAEGNVEVPAVYAGVtpSERKQR-ATALLTELGLGTKTLNRPSQ-LSGGQQQRVSIARALMNGGDVILADE 172
Cdd:PRK10938 350 rvstsVRNVILSGFFDSIGIYQAV--SDRQQKlAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDE 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491444527 173 PTGALDSHSGVEVMRILRELNAAGHTIIL-VTHDMQVAKNAT--RIIEISDGEI 223
Cdd:PRK10938 428 PLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAEDAPACIthRLEFVPDGDI 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-221 |
2.45e-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: 57.33 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 131 LTELGLGTKTLNRPSQ-LSGGQQQRVSIARALMNG--GDVILADEPTGAL---DSHSGVEVMRILRELnaaGHTIILVTH 204
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAGtLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLhqrDNRRLINTLKRLRDL---GNTLIVVEH 548
|
90
....*....|....*..
gi 491444527 205 DMQVAKNATRIIEISDG 221
Cdd:TIGR00630 549 DEDTIRAADYVIDIGPG 565
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-223 |
3.90e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 55.25 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDrpTSGSYKVSGQETGKLEPDQLarl 85
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVPLQKW--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 rREYFGFIFQRYHLLgdlsaEGNVEVPAVYAGVTPSERKQRATallTELGLGTKTLNRPSQL-----------SGGQQQR 154
Cdd:cd03289 76 -RKAFGVIPQKVFIF-----SGTFRKNLDPYGKWSDEEIWKVA---EEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSGVEVMRILRElNAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-228 |
7.49e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLepdQLARLRREYFgfIFQRYHLLGDLS 104
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRRVLS--IIPQSPVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 AEGNVEVPAVYAGVTPSERKQRA----TALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSH 180
Cdd:PLN03232 1326 VRFNIDPFSEHNDADLWEALERAhikdVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 181 SGVEVMRILRElNAAGHTIILVTHDMQVAKNATRIIEISDGEIIS-DRP 228
Cdd:PLN03232 1406 TDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEyDSP 1453
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-226 |
7.96e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 7 LEVSNLVREFpaGEstIQILKGIDLTIYEGELVAIVGQSGSGKSTlmnilGCLdrptsgSYKVSGQETGKlEPDQLAR-- 84
Cdd:NF000106 14 VEVRGLVKHF--GE--VKAVDGVDLDVREGTVLGVLGP*GAA**R-----GAL------PAHV*GPDAGR-RPWRF*Twc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 85 -----LRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIAR 159
Cdd:NF000106 78 anrraLRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 160 ALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKN-ATRIIEISDGEIISD 226
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIAD 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-205 |
8.14e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 8.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 16 FPAGESTIQILK-GIDLTiyegELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSgqetgklepdqlARLRREyfgfIF 94
Cdd:PLN03073 518 YPGGPLLFKNLNfGIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS------------AKVRMA----VF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 95 QRYHLLG-DLSAEGNVEVPAVYAGVTpserKQRATALLTELGL-GTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADE 172
Cdd:PLN03073 578 SQHHVDGlDLSSNPLLYMMRCFPGVP----EQKLRAHLGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
170 180 190
....*....|....*....|....*....|...
gi 491444527 173 PTGALDSHSgveVMRILRELNAAGHTIILVTHD 205
Cdd:PLN03073 654 PSNHLDLDA---VEALIQGLVLFQGGVLMVSHD 683
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-211 |
8.79e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNI-LGCLdRPTSGSYKVSGqetgKLEpdqLArlrreYFGfifQRYHLLG- 101
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRIHCGT----KLE---VA-----YFD---QHRAELDp 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 -----DLSAEGNVEVpavyagvTPSERKQRATALLTELGLGTKTLNRPSQ-LSGGQQQRVSIARALMNGGDVILADEPTG 175
Cdd:PRK11147 397 ektvmDNLAEGKQEV-------MVNGRPRHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|....*...
gi 491444527 176 ALDshsgVEVMRILREL--NAAGhTIILVTHDMQVAKN 211
Cdd:PRK11147 470 DLD----VETLELLEELldSYQG-TVLLVSHDRQFVDN 502
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-216 |
9.06e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 9.06e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491444527 147 LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILREL-NAAGHTIILVTHDMQVAKNATRII 216
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-223 |
9.27e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETgklepdqlarlrreyfgFIFQRYHLLGDLSA 105
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAA-----------------LIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 106 EGNVEVPAVYAGVTpSERKQRATALLTELGLGTKTLNRPSQ-LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVE 184
Cdd:PRK13545 103 IENIELKGLMMGLT-KEKIKEIIPEIIEFADIGKFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491444527 185 VMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEI 223
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHSLsQVKSFCTKALWLHYGQV 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-204 |
1.11e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 11 NLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGclDRPTSGsYKVSGQETGKLEPDQLARLRReyF 90
Cdd:TIGR00956 764 NLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRLVNGRPLDSSFQRS--I 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 91 GFIFQRYHLLGDLSAEGNVEVPAVY---AGVTPSER-------------KQRATALLTELGLGtktlnrpsqLSGGQQQR 154
Cdd:TIGR00956 839 GYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSKSEKmeyveevikllemESYADAVVGVPGEG---------LNVEQRKR 909
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491444527 155 VSIARALMNGGDVIL-ADEPTGALDSHSGVEVMRILRELNAAGHTIILVTH 204
Cdd:TIGR00956 910 LTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
146-225 |
1.72e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 54.72 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 146 QLSGGQQ------QRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVaknatriIEIS 219
Cdd:NF041034 779 ALSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEEL-------KEIS 851
|
....*.
gi 491444527 220 DgEIIS 225
Cdd:NF041034 852 D-YIIS 856
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-223 |
2.64e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHLLG--- 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQDPVLFSgsl 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 --DLSAEGNVEVPAVYAGVTPSERKQRATALLTelGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDS 179
Cdd:TIGR00957 1377 rmNLDPFSQYSDEEVWWALELAHLKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491444527 180 HSGVEVMRILRElNAAGHTIILVTHDMQVAKNATRIIEISDGEI 223
Cdd:TIGR00957 1455 ETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-228 |
2.69e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 10 SNLVREFPAgestIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQE----TGKLEPDQLARL 85
Cdd:PRK10982 2 SNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfkSSKEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 86 RREYFGFIFQRYHL----LGDLSAEGNVevpavyagVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARAL 161
Cdd:PRK10982 78 VHQELNLVLQRSVMdnmwLGRYPTKGMF--------VDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 162 MNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISDRP 228
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQWIATQP 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-229 |
6.63e-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: 49.29 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 36 GELVAIVGQSGSGKSTLMNILgcldrptsgsykvsgqetgklepdqLARLRREYFGFIFqryhllgdLSAEGNVEVpavy 115
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL-------------------------ARELGPPGGGVIY--------IDGEDILEE---- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 116 agvtpserkqratalLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILR----- 190
Cdd:smart00382 45 ---------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491444527 191 -ELNAAGHTIILVTHDMQVAKNATrIIEISDGEIISDRPN 229
Cdd:smart00382 110 lLKSEKNLTVILTTNDEKDLGPAL-LRRRFDRRIVLLLIL 148
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
131-218 |
6.93e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.72 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 131 LTELGLGTKTLNRPS-QLSGGQQQRVSIARALM---NGGDVILADEPTGALDSHSgVEV-MRILRELNAAGHTIILVTHD 205
Cdd:COG0178 810 LQDVGLGYIKLGQPAtTLSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHD-IRKlLEVLHRLVDKGNTVVVIEHN 888
|
90
....*....|...
gi 491444527 206 MQVAKNATRIIEI 218
Cdd:COG0178 889 LDVIKTADWIIDL 901
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
131-218 |
7.42e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.72 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 131 LTELGLGTKTLNRPSQ-LSGGQQQRVSIARA----LMNggdV--ILaDEPTGAL---DSHSGVEVMRILRELnaaGHTII 200
Cdd:COG0178 469 LVDVGLDYLTLDRSAGtLSGGEAQRIRLATQigsgLVG---VlyVL-DEPSIGLhqrDNDRLIETLKRLRDL---GNTVI 541
|
90
....*....|....*...
gi 491444527 201 LVTHDMQVAKNATRIIEI 218
Cdd:COG0178 542 VVEHDEDTIRAADYIIDI 559
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-224 |
8.29e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.03 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQLarlrREYFGFIFQRYHLLGDls 104
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLAD-- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 105 aegnvevpAVYAGVT-----PSERKQRA--TALLTEL------GLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILAD 171
Cdd:PRK10790 430 --------TFLANVTlgrdiSEEQVWQAleTVQLAELarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491444527 172 EPTGALDSHSGVEVMRILRELNAAGhTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHT-TLVVIAHRLSTIVEADTILVLHRGQAV 553
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
145-229 |
2.65e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 145 SQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEI 223
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELpEVLGLSDRVLVMHEGKL 483
|
....*.
gi 491444527 224 ISDRPN 229
Cdd:PRK13549 484 KGDLIN 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-229 |
5.33e-06 |
|
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: 49.44 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 2 TKQALLEVSNLVREFPAgESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMN-ILGCLDRPTSGSYKVSGQETGKLEPD 80
Cdd:TIGR02633 253 IGDVILEARNLTCWDVI-NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 81 QLARLRREYFGFIFQRYHLLGDLSAEGNVEVPAV--YAGVTPSERKQRATALLTE---LGLGTKTLNRP-SQLSGGQQQR 154
Cdd:TIGR02633 332 QAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLksFCFKMRIDAAAELQIIGSAiqrLKVKTASPFLPiGRLSGGNQQK 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491444527 155 VSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM-QVAKNATRIIEISDGEIISDRPN 229
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKGDFVN 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-224 |
6.66e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 25 ILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLepdQLARLRREyFGFIFQ--------- 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKV-LGIIPQapvlfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 96 RYHLlgDLSAEGNvevpavyaGVTPSERKQRA----TALLTELGLGTKTLNRPSQLSGGQQQRVSIARALMNGGDVILAD 171
Cdd:PLN03130 1330 RFNL--DPFNEHN--------DADLWESLERAhlkdVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491444527 172 EPTGALDSHSGVEVMRILRELNAAGhTIILVTHDMQVAKNATRIIEISDGEII 224
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFKSC-TMLIIAHRLNTIIDCDRILVLDAGRVV 1451
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-174 |
8.69e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKlepdqlARLRREyfgfIFQR--------- 96
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD------ARHRRA----VCPRiaympqglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 97 ---YHllgDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLgTKTLNRPS-QLSGGQQQRVSIARALMNGGDVILADE 172
Cdd:NF033858 87 knlYP---TLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL-APFADRPAgKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
..
gi 491444527 173 PT 174
Cdd:NF033858 163 PT 164
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-207 |
1.49e-05 |
|
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: 48.47 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 3 KQALLEVSNLVREFPAGESTIqiLKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVSGQETGKLEPDQl 82
Cdd:TIGR01257 1934 KTDILRLNELTKVYSGTSSPA--VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 83 arlrREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPSERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALM 162
Cdd:TIGR01257 2011 ----HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 163 NGGDVILADEPTGALDSHSGV----EVMRILRElnaaGHTIILVTHDMQ 207
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRmlwnTIVSIIRE----GRAVVLTSHSME 2131
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-204 |
1.78e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 24 QILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLD--RPTSGSYKVSGQETGKLEPDQLArlrREYFGFIFQRyhllg 101
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQY----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 102 dlsaegNVEVPAV---------------YAGVTPSER-------KQRATALLTELGLGTKTLNrpSQLSGGQQQRVSIAR 159
Cdd:PRK09580 87 ------PVEIPGVsnqfflqtalnavrsYRGQEPLDRfdfqdlmEEKIALLKMPEDLLTRSVN--VGFSGGEKKRNDILQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491444527 160 ALMNGGDVILADEPTGALDshsgVEVMRILRE----LNAAGHTIILVTH 204
Cdd:PRK09580 159 MAVLEPELCILDESDSGLD----IDALKIVADgvnsLRDGKRSFIIVTH 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
147-223 |
1.99e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 1.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491444527 147 LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNAT-RIIEISDGEI 223
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITdRILVMSNGLV 469
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
26-56 |
5.20e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 5.20e-05
10 20 30
....*....|....*....|....*....|..
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTLMN-IL 56
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTL 656
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
146-219 |
7.04e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 146 QLSGGQQQ------RVSIARALMNGGDVILADEPTGALDS-HSGVEVMRILRELNAAGH-TIILVTHDMQVAKNATRIIE 217
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNfQLIVITHDEELVDAADHIYR 194
|
..
gi 491444527 218 IS 219
Cdd:cd03240 195 VE 196
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
147-206 |
1.27e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 147 LSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDM 206
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSEL 464
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-213 |
1.59e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 18 AGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVS-GQETGKLEPDQLARLRREyfgfifqr 96
Cdd:PRK10636 320 AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRAD-------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 97 yhllgdlsaegnvEVPAVY-AGVTPSERKQRATALLTELGL-GTKTLNRPSQLSGGQQQRVSIARALMNGGDVILADEPT 174
Cdd:PRK10636 392 -------------ESPLQHlARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190
....*....|....*....|....*....|....*....
gi 491444527 175 GALDSHSGVEVMRILRELNAAghtIILVTHDMQVAKNAT 213
Cdd:PRK10636 459 NHLDLDMRQALTEALIDFEGA---LVVVSHDRHLLRSTT 494
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
26-52 |
2.45e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 2.45e-04
10 20
....*....|....*....|....*..
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTL 52
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
29-205 |
2.79e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 29 IDLTiyeGELVAIVGQSGSGKSTLMN-ILGCLDRPTSGSYKVSGQ--ETGKLEP---------DQLARLRR---EYFGFI 93
Cdd:COG0419 19 IDFD---DGLNLIVGPNGAGKSTILEaIRYALYGKARSRSKLRSDliNVGSEEAsvelefehgGKRYRIERrqgEFAEFL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 94 FQRY--------HLLG-DLSAEGNVEVPAVYAGVTPS-ERKQRATALLTELGLGTKTLNRPSQLSGGQQQRVSIARALmn 163
Cdd:COG0419 96 EAKPserkealkRLLGlEIYEELKERLKELEEALESAlEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLL-- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491444527 164 ggDVILaDepTGALDSHSGVEVMRILRELNaaghtiiLVTHD 205
Cdd:COG0419 174 --SLIL-D--FGSLDEERLERLLDALEELA-------IITHV 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
126-204 |
3.42e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 126 RATALLTELGLGTKT-LNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSgveVMRILRELNAAGHTIILVTH 204
Cdd:PLN03073 323 RAASILAGLSFTPEMqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSH 399
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
122-221 |
3.69e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 122 ERKQRATALLTELGLGTKTLNRP-SQLSGGQQQRVSIARALM---NGGDVILADEPTGALDSHSGVEVMRILRELNAAGH 197
Cdd:PRK00635 1674 KKIQKPLQALIDNGLGYLPLGQNlSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGH 1753
|
90 100
....*....|....*....|....
gi 491444527 198 TIILVTHDMQVAKNATRIIEISDG 221
Cdd:PRK00635 1754 SVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
130-216 |
3.83e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491444527 130 LLTELGLGTKTLNRPS-QLSGGQQQRVSIARALM---NGGDVILADEPTGAL---DSHSGVEVMRILRELnaaGHTIILV 202
Cdd:PRK00349 813 TLVDVGLGYIKLGQPAtTLSGGEAQRVKLAKELSkrsTGKTLYILDEPTTGLhfeDIRKLLEVLHRLVDK---GNTVVVI 889
|
90
....*....|....
gi 491444527 203 THDMQVAKNATRII 216
Cdd:PRK00349 890 EHNLDVIKTADWII 903
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
26-52 |
1.78e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.78e-03
10 20
....*....|....*....|....*..
gi 491444527 26 LKGIDLTIYEGELVAIVGQSGSGKSTL 52
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
35-63 |
3.74e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.30 E-value: 3.74e-03
10 20 30
....*....|....*....|....*....|
gi 491444527 35 EGELVAIVGQSGSGKSTLMN-ILGCLDRPT 63
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNaLLPELVLAT 113
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
35-63 |
5.23e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 39.33 E-value: 5.23e-03
10 20 30
....*....|....*....|....*....|
gi 491444527 35 EGELVAIVGQSGSGKSTLMN-ILGCLDRPT 63
Cdd:COG1162 165 KGKTSVLVGQSGVGKSTLINaLLPDADLAT 194
|
|
| CDC_Septin |
cd01850 |
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
27-56 |
7.10e-03 |
|
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.
Pssm-ID: 206649 Cd Length: 275 Bit Score: 38.68 E-value: 7.10e-03
10 20 30
....*....|....*....|....*....|
gi 491444527 27 KGIDLTIYegelvaIVGQSGSGKSTLMNIL 56
Cdd:cd01850 1 RGFQFNIM------VVGESGLGKSTFINTL 24
|
|
| |
