|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-226 |
2.51e-111 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 319.30 E-value: 2.51e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYKTrfKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDA 81
Cdd:COG1136 3 PLLELRNLTKSYGT--GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 SSFRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAII 161
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 162 TKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASRAQRVLFIKDGILYNQI 226
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-220 |
4.02e-98 |
|
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: 285.54 E-value: 4.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTrfKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASS 83
Cdd:cd03255 1 IELKNLSKTYGG--GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03255 79 FRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-217 |
1.35e-89 |
|
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: 263.71 E-value: 1.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 6 VQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFR 85
Cdd:TIGR03608 1 LKNISKKFGDK------VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 86 RERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPE 165
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFI 217
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-222 |
9.28e-81 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 241.88 E-value: 9.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 7 QHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRR 86
Cdd:COG2884 5 ENVSKRY-----PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 eRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEI 166
Cdd:COG2884 80 -RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 167 LLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTA-AASRAQRVLFIKDGIL 222
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElVDRMPKRVLELEDGRL 215
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-222 |
9.39e-73 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 221.13 E-value: 9.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRFKgnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAS 82
Cdd:NF038007 1 MLNMQNAEKCYITKTI--KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:NF038007 79 ILRRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDGIL 222
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-222 |
4.89e-67 |
|
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: 207.29 E-value: 4.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYKTRfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIkNKDA 81
Cdd:COG4181 7 PIIELRGLTKTVGTG--AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 -SSFRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPlkQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG4181 84 rARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 161 ITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASRAQRVLFIKDGIL 222
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
1.12e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 202.24 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTRfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknKD 80
Cdd:COG1116 5 APALELRGVSKRFPTG--GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASSFRRERlGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG1116 75 VTGPGPDR-GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 161 ITKPEILLADEPTGALDSKSSAAL-LDVFDAINASGQTILMVTHSTA-AASRAQRVL 215
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLqDELLRLWQETGKTVLFVTHDVDeAVFLADRVV 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-221 |
4.49e-64 |
|
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: 199.01 E-value: 4.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAS 82
Cdd:TIGR02673 1 MIEFHNVSKAY-----PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:TIGR02673 76 LLRR-RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTA-AASRAQRVLFIKDGI 221
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-222 |
5.97e-64 |
|
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: 199.64 E-value: 5.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDAS 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPV--LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP---VTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRReRLGFVFQD----FNLLdtLSVKDNILLPLVLSRRPlkQMMTQVEAISRQLGIH-SLLEKYPYEISGGQKQRVAVA 157
Cdd:COG1124 76 AFRR-RVQMVFQDpyasLHPR--HTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 158 RAIITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASR-AQRVLFIKDGIL 222
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-220 |
2.73e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 198.38 E-value: 2.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 6 VQHVKKIYKTrfKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFR 85
Cdd:COG1135 4 LENLSKTFPT--KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 86 ReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEaisrqlgihSLLE---------KYPYEISGGQKQRVAV 156
Cdd:COG1135 82 R-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVA---------ELLElvglsdkadAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 157 ARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
1.61e-61 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 201.29 E-value: 1.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYKTRFKGnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDA 81
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKG-GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 SSFRReRLGFVFQD-FNLLD-TLSVKDNILLPLVLSRR-PLKQMMTQVEAISRQLGIH-SLLEKYPYEISGGQKQRVAVA 157
Cdd:COG1123 338 RELRR-RVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 158 RAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDG 481
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
7.63e-61 |
|
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: 7.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAS 82
Cdd:cd03257 1 LLEVKNLSVSFPTG--GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 sFRRERLGFVFQD-FNLLD-TLSVKDNILLPLVLSRRPLKQMM--TQVEAISRQLGIHS-LLEKYPYEISGGQKQRVAVA 157
Cdd:cd03257 79 -IRRKEIQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSKKEArkEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 158 RAIITKPEILLADEPTGALDSKSSAALLDVFDAI-NASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
9.51e-61 |
|
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: 190.42 E-value: 9.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdasS 83
Cdd:cd03259 1 LELKGLSKTY------GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03259 69 PERRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAI-NASGQTILMVTHSTA-AASRAQRVLFIKDG 220
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEeALALADRIAVMNEG 207
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
2.76e-60 |
|
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: 189.61 E-value: 2.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTrfKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtATIKNKDAss 83
Cdd:cd03293 1 LEVRNVSKTYGG--GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---EPVTGPGP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frreRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03293 74 ----DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 164 PEILLADEPTGALDSKSSAAL-LDVFDAINASGQTILMVTHSTA-AASRAQRVL 215
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLqEELLDIWRETGKTVLLVTHDIDeAVFLADRVV 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-203 |
3.82e-60 |
|
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: 189.71 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 6 VQHVKKIYKTRfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFR 85
Cdd:cd03258 4 LKNVSKVFGDT--GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 86 ReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPE 165
Cdd:cd03258 82 R-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTH 203
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITH 199
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-220 |
2.66e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 187.51 E-value: 2.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKiyktRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtATIKNKDAS 82
Cdd:COG1126 1 MIEIENLHK----SFGDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED-LTDSKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRplkqmMTQVEAISR------QLGIHSLLEKYPYEISGGQKQRVAV 156
Cdd:COG1126 74 KLRR-KVGMVFQQFNLFPHLTVLENVTLAPIKVKK-----MSKAEAEERamelleRVGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 157 ARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGG 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-220 |
5.85e-59 |
|
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: 186.38 E-value: 5.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASS 83
Cdd:COG1122 1 IELENLSFSY-----PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQD-----FNLldtlSVKDNI---LLPLVLSRrplKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVA 155
Cdd:COG1122 73 LRR-KVGLVFQNpddqlFAP----TVEEDVafgPENLGLPR---EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 156 VARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTA-AASRAQRVLFIKDG 220
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-233 |
8.00e-57 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 181.33 E-value: 8.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKiyktRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAS 82
Cdd:COG1127 5 MIEVRNLTK----SFGDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRReRLGFVFQDFNLLDTLSVKDNILLPLV-LSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAII 161
Cdd:COG1127 79 ELRR-RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 162 TKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDGILynqIFKGDKSE 233
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAiADRVAVLADGKI---IAEGTPEE 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-222 |
5.18e-56 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 178.37 E-value: 5.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 10 KKIYKTRfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRReRL 89
Cdd:cd03292 4 INVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 90 GFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLA 169
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 170 DEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQ-RVLFIKDGIL 222
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-220 |
2.76e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.56 E-value: 2.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDA 81
Cdd:COG3638 1 PMLELRNLSKRY-----PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 SSFRReRLGFVFQDFNLLDTLSVKDNILLPLvLSRRPLKQMMTQV----------EAISRqLGIHSLLEKYPYEISGGQK 151
Cdd:COG3638 76 RRLRR-RIGMIFQQFNLVPRLSVLTNVLAGR-LGRTSTWRSLLGLfppedreralEALER-VGLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 152 QRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRyADRIIGLRDG 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
2.90e-55 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 187.62 E-value: 2.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MT-LLDVQHVKKIYKTrfKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNK 79
Cdd:PRK10535 1 MTaLLELKDIRRSYPS--GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 80 DASSFRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK10535 79 ALAQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 160 IITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-220 |
4.55e-55 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 175.73 E-value: 4.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDassfRRERLGFVFQD 95
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNL-LDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTG 174
Cdd:cd03225 84 PDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092440915 175 ALDSKSSAALLDVFDAINASGQTILMVTHSTA-AASRAQRVLFIKDG 220
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-222 |
6.56e-55 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 175.41 E-value: 6.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 8 HVKKIYKtRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTaTIKNKDASSFRRe 87
Cdd:cd03262 2 EIKNLHK-SFGDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 88 RLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQmmtQVEAISRQL----GIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKA---EAEERALELlekvGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGIL 222
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-220 |
2.29e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.85 E-value: 2.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVkkiyktRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkDASS 83
Cdd:COG4619 1 LELEGL------SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQDFNLLDTlSVKDNILLPLVLSRRPLKqmMTQVEAISRQLGI-HSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:COG4619 72 WRR-QVAYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-222 |
3.90e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 177.96 E-value: 3.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKD 80
Cdd:COG3839 1 MASLELENVSKSY------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 assfrReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG3839 75 -----R-NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 161 ITKPEILLADEPTGALDSKSSAALLDVFDAI-NASGQTILMVTHS-TAAASRAQRVLFIKDGIL 222
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDqVEAMTLADRIAVMNDGRI 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-220 |
1.44e-53 |
|
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: 173.14 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASS 83
Cdd:cd03256 1 IEVENLSKTY-----PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSL----LEKYPY----EISGGQKQRVA 155
Cdd:cd03256 76 LRR-QIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALervgLLDKAYqradQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 156 VARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREyADRIVGLKDG 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
3.67e-53 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 170.06 E-value: 3.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATikNKDASS 83
Cdd:cd03229 1 LELKNVSKRY------GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTD--LEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFVFQDFNLLDTLSVKDNILLPLvlsrrplkqmmtqveaisrqlgihsllekypyeiSGGQKQRVAVARAIITK 163
Cdd:cd03229 73 PLRRRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-203 |
1.46e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 173.75 E-value: 1.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknKD 80
Cdd:COG3842 3 MPALELENVSKRY------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--------RD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASS---FRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVA 157
Cdd:COG3842 69 VTGlppEKR-NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092440915 158 RAIITKPEILLADEPTGALDSKSSAAL-LDVFDAINASGQTILMVTH 203
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTH 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-220 |
4.70e-52 |
|
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: 166.79 E-value: 4.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDassfRRERLGFVFQD 95
Cdd:cd03228 9 SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES----LRKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLDTlSVKDNILlplvlsrrplkqmmtqveaisrqlgihsllekypyeiSGGQKQRVAVARAIITKPEILLADEPTGA 175
Cdd:cd03228 85 PFLFSG-TIRENIL-------------------------------------SGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092440915 176 LDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03228 127 LDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-233 |
5.10e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.70 E-value: 5.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTrfkgnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknKDASS 83
Cdd:COG1131 1 IEVRGLTKRYGD------KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:COG1131 71 VRR-RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGILynqIFKGDKSE 233
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRI---VADGTPDE 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-220 |
6.88e-52 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.91 E-value: 6.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 7 QHVKKIYKTrfKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRR 86
Cdd:PRK11153 5 KNISKVFPQ--GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 eRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEI 166
Cdd:PRK11153 83 -QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 167 LLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRiCDRVAVIDAG 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-220 |
3.93e-51 |
|
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: 166.52 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 9 VKKIYKtRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRReR 88
Cdd:cd03261 3 LRGLTK-SFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 89 LGFVFQDFNLLDTLSVKDNILLPL-VLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEIL 167
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 168 LADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHS-TAAASRAQRVLFIKDG 220
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-220 |
1.71e-50 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 172.40 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MT-LLDVQHVKkiykTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTA---GRVYLNGMDTATI 76
Cdd:COG1123 1 MTpLLEVRDLS----VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 77 KNKDassfRRERLGFVFQDF-NLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVA 155
Cdd:COG1123 77 SEAL----RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 156 VARAIITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTA-AASRAQRVLFIKDG 220
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGvVAEIADRVVVMDDG 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-233 |
4.02e-50 |
|
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: 164.05 E-value: 4.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKtRFKgnqveaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdass 83
Cdd:cd03299 1 LKVENLSKDWK-EFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03299 70 --KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 164 PEILLADEPTGALDSKSSAALL-DVFDAINASGQTILMVTHS-TAAASRAQRVLFIKDGILY-----NQIFKGDKSE 233
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLReELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIqvgkpEEVFKKPKNE 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-225 |
5.88e-49 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 160.71 E-value: 5.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKiyKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAS 82
Cdd:PRK10584 6 IVEVHHLKK--SVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASRAQRVLFIKDGILYNQ 225
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-222 |
7.42e-49 |
|
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: 158.71 E-value: 7.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatikNKDASS 83
Cdd:cd03230 1 IEVRNLSKRYGKK------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD-----IKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFVFQDFNLLDTLSVKDNILLplvlsrrplkqmmtqveaisrqlgihsllekypyeiSGGQKQRVAVARAIITK 163
Cdd:cd03230 70 EVKRRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTA-AASRAQRVLFIKDGIL 222
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-220 |
7.65e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.47 E-value: 7.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKiyktRFKGNQveALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATikNKDAss 83
Cdd:COG1118 3 IEVRNISK----RFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT--NLPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frRER-LGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:COG1118 73 --RERrVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 163 KPEILLADEPTGALDSKSSAA----LLDVFDAInasGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKElrrwLRRLHDEL---GGTTVFVTHDQEEALElADRVVVMNQG 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-222 |
1.24e-47 |
|
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: 158.58 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 18 KGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRRERLGFVFQDFN 97
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 98 LLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092440915 178 SKSSAALLDVFDAINA-SGQTILMVTHSTAAASR-AQRVLFIKDGIL 222
Cdd:cd03294 193 PLIRREMQDELLRLQAeLQKTIVFITHDLDEALRlGDRIAIMKDGRL 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-215 |
3.32e-47 |
|
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: 159.06 E-value: 3.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKP---TAGRVYLNGMDTATIKNK 79
Cdd:COG0444 1 LLEVRNLKVYFPTR--RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 80 DASSFRRERLGFVFQD-FNLLD-TLSVKDNILLPLVLSRR-PLKQMMTQVEAISRQLGIH---SLLEKYPYEISGGQKQR 153
Cdd:COG0444 79 ELRKIRGREIQMIFQDpMTSLNpVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 154 VAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVL 215
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEiADRVA 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-234 |
3.41e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.45 E-value: 3.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 28 IHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMD-TATiknkdaSSFRRErLGFVFQDFNLLDTLSVKD 106
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDlTAL------PPAERP-VSMLFQENNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 107 NILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLD 186
Cdd:COG3840 91 NIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 187 VFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG-ILYN----QIFKGDKSEH 234
Cdd:COG3840 171 LVDELCRErGLTVLMVTHDPEDAARiADRVLLVADGrIAADgptaALLDGEPPPA 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-223 |
3.71e-47 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 156.19 E-value: 3.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 7 QHVKKIYktrFKGNQveALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRR 86
Cdd:PRK10908 5 EHVSKAY---LGGRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 ErLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEI 166
Cdd:PRK10908 80 Q-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 167 LLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTA-AASRAQRVLFIKDGILY 223
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHLH 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-225 |
4.77e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 165.78 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkDASSFRReRLGFVFQD 95
Cdd:COG2274 482 RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLRR-QIGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLDTlSVKDNILL--PLVlsrrplkqMMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIIT 162
Cdd:COG2274 558 VFLFSG-TIRENITLgdPDA--------TDEEIIEAARLAGLHDFIEALPmgYDtvvgeggsnLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINAsGQTILMVTHSTAAASRAQRVLFIKDGILYNQ 225
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-173 |
7.56e-47 |
|
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: 152.80 E-value: 7.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRReRLGFVFQDFNLLDTLSV 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRK-EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 105 KDNILLPLVLSRRPLKQMMTQVEAISRQLGI----HSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
8-233 |
2.45e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 154.96 E-value: 2.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 8 HVKKIYKtRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKD----ASS 83
Cdd:COG4598 10 EVRDLHK-SFGDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FR-----RERLGFVFQDFNLLDTLSVKDNILL-PLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVA 157
Cdd:COG4598 87 RRqlqriRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 158 RAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTA-AASRAQRVLFIKDGILYNQ-----IFKGDK 231
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGfARDVSSHVVFLHQGRIEEQgppaeVFGNPK 246
|
..
gi 1092440915 232 SE 233
Cdd:COG4598 247 SE 248
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-220 |
2.84e-46 |
|
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: 154.38 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAS 82
Cdd:TIGR02315 1 MLEVENLSKVY-----PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRReRLGFVFQDFNLLDTLSVKDNILLPLvLSRRPLKQMM-------TQVEAIS--RQLGIHSLLEKYPYEISGGQKQR 153
Cdd:TIGR02315 76 KLRR-RIGMIFQHYNLIERLTVLENVLHGR-LGYKPTWRSLlgrfseeDKERALSalERVGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 154 VAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKyADRIVGLKAG 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-220 |
3.81e-46 |
|
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: 154.00 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRFKgnqveALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkDASS 83
Cdd:cd03295 1 IEFENVTKRYGGGKK-----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQV-EAISR-QLGIHSLLEKYPYEISGGQKQRVAVARAII 161
Cdd:cd03295 73 LRR-KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERAdELLALvGLDPAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 162 TKPEILLADEPTGALDSKSSAALLDVFDAIN-ASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQqELGKTIVFVTHDIDEAFRlADRIAIMKNG 212
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-222 |
4.65e-46 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 153.25 E-value: 4.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASS 83
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQV--LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRR-PLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:TIGR02982 80 LRR-RIGYIFQAHNLLGFLTARQNVQMALELQPNlSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASRAQRVLFIKDGIL 222
Cdd:TIGR02982 159 HPKLVLADEPTAALDSKSGRDVVELMQKLAKeQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-220 |
5.08e-46 |
|
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: 156.80 E-value: 5.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 27 DIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGM---DTAtiKNKDASSFRReRLGFVFQDFNLLDTLS 103
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSA--RGIFLPPHRR-RIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 VKDNILLplVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAA 183
Cdd:COG4148 94 VRGNLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092440915 184 LLDVFDAINASGQT-ILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG4148 172 ILPYLERLRDELDIpILYVSHSLDEVARlADHVVLLEQG 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-222 |
6.08e-46 |
|
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: 152.79 E-value: 6.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTrfkgnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDass 83
Cdd:cd03301 1 VELENVTKRFGN------VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frrERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03301 72 ---RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHS-TAAASRAQRVLFIKDGIL 222
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-204 |
9.45e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 153.48 E-value: 9.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTRfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtATIKNKD 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGG--GQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG---VPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 AssfrrERlGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG4525 76 A-----DR-GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1092440915 161 ITKPEILLADEPTGALDS----KSSAALLDVFdaiNASGQTILMVTHS 204
Cdd:COG4525 150 AADPRFLLMDEPFGALDAltreQMQELLLDVW---QRTGKGVFLITHS 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-222 |
2.73e-45 |
|
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: 150.91 E-value: 2.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 27 DIHFTVDkGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNG---MDTAtiKNKDASSFRReRLGFVFQDFNLLDTLS 103
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSR--KKINLPPQQR-KIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 VKDNILLPL-VLSRRPLKQmmtQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSA 182
Cdd:cd03297 92 VRENLAFGLkRKRNREDRI---SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092440915 183 ALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDGIL 222
Cdd:cd03297 169 QLLPELKQIKKNlNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
25-220 |
2.89e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 152.12 E-value: 2.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDassfRRERLGFVFQDFNLLDTLSV 104
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDNILLplvlSRRPLKQMMTQ--------VEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGAL 176
Cdd:COG1120 93 RELVAL----GRYPHLGLFGRpsaedreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092440915 177 DSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG1120 169 DLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARyADRLVLLKDG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-203 |
3.01e-45 |
|
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: 151.24 E-value: 3.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkGNQVeALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdaSS 83
Cdd:cd03300 1 IELENVSKFY-----GGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03300 70 HKR-PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTH 203
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTH 189
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
9.05e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.62 E-value: 9.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVkkiyktRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATiknkd 80
Cdd:COG1121 4 MPAIELENL------TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 assfRRERLGFVFQDFNLLDT--LSVKDNILLPLV----LSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRV 154
Cdd:COG1121 73 ----ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 155 AVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGILY 223
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLNRGLVA 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
1.40e-44 |
|
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: 149.64 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAML-----DKPTAGRVYLNGMDTATIkN 78
Cdd:cd03260 1 IELRDLNVYY------GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDL-D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 79 KDASSFRReRLGFVFQDFNLLDtLSVKDNILLPLVLSR-RPLKQMMTQVEAISRQLGIHSLLEK--YPYEISGGQKQRVA 155
Cdd:cd03260 74 VDVLELRR-RVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 156 VARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASgQTILMVTHSTAAASR-AQRVLFIKDGIL 222
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARvADRTAFLLNGRL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-244 |
2.92e-44 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 149.24 E-value: 2.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKtrfkgnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdas 82
Cdd:COG4555 1 MIEVENLSKKYG------KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 sfRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:COG4555 72 --ARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGILYNQIFKGDKSEHQMFQEIS 241
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
...
gi 1092440915 242 DTL 244
Cdd:COG4555 230 DAF 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-226 |
4.13e-44 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 148.43 E-value: 4.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRRERLGFVFQDFNLLD 100
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 101 TLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKS 180
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092440915 181 SAALLDVFDAINAS-GQTILMVTHSTAAASRAQRVLFIKDGILYNQI 226
Cdd:PRK11629 181 ADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-220 |
7.04e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 149.14 E-value: 7.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 6 VQHVKKIY--KTRFkgnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASS 83
Cdd:TIGR04521 3 LKNVSYIYqpGTPF---EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQ--DFNLLDTLSVKDNILLP--LVLSRRPLKQmmtQVEAISRQLGI-HSLLEKYPYEISGGQKQRVAVAR 158
Cdd:TIGR04521 80 LRK-KVGLVFQfpEHQLFEETVYKDIAFGPknLGLSEEEAEE---RVKEALELVGLdEEYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 159 AIITKPEILLADEPTGALDSKSSAALLDVFDAIN-ASGQTILMVTHSTA-AASRAQRVLFIKDG 220
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEdVAEYADRVIVMHKG 219
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-203 |
9.85e-44 |
|
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: 150.96 E-value: 9.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKiyktRFkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkDASS 83
Cdd:TIGR03265 5 LSIDNIRK----RF--GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT-----RLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRErLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:TIGR03265 74 QKRD-YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTH 203
Cdd:TIGR03265 153 PGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTH 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-220 |
1.83e-43 |
|
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: 146.10 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 28 IHF--TVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkdASSFRRERLGFVFQDFNLLDTLSVK 105
Cdd:cd03298 15 MHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT------AAPPADRPVSMLFQENNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 106 DNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALL 185
Cdd:cd03298 89 QNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1092440915 186 DVFDAINA-SGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03298 169 DLVLDLHAeTKMTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-222 |
1.24e-42 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 152.22 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDassfRRERLGFVFQDFNLLDTl 102
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----WRRQIAWVPQNPYLFAG- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNILLPlvlsrRPlKQMMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIITKPEILLADE 171
Cdd:COG4988 426 TIRENLRLG-----RP-DASDEELEAALEAAGLDEFVAALPdgLDtplgeggrgLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 172 PTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDGIL 222
Cdd:COG4988 500 PTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-232 |
1.90e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.39 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 8 HVKKIYKtrFKGNQvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMD---TATIKNKDASSF 84
Cdd:COG4161 4 QLKNINC--FYGSH-QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 85 RRErLGFVFQDFNLLDTLSVKDNIL-LPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:COG4161 81 RQK-VGMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGILynqIFKGDKS 232
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRI---IEQGDAS 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-220 |
4.65e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 150.70 E-value: 4.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 19 GNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkDASSFRReRLGFVFQDFNL 98
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL---TLESLRR-QIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 99 LDTlSVKDNILLPlvlsrRPlKQMMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIITKPEIL 167
Cdd:COG1132 426 FSG-TIRENIRYG-----RP-DATDEEVEEAAKAAQAHEFIEALPdgYDtvvgergvnLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 168 LADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-203 |
1.05e-41 |
|
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: 142.19 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKiyktRFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKnkdasS 83
Cdd:cd03219 1 LEVRGLTK----RFGG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-----P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFV--FQDFNLLDTLSVKDNILLP----------LVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQK 151
Cdd:cd03219 70 HEIARLGIGrtFQIPRLFPELTVLENVMVAaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 152 QRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-220 |
1.19e-41 |
|
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: 141.96 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkDASSFRReRLGFVFQD 95
Cdd:cd03245 11 SYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLRR-NIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLDTlSVKDNILL--PLVLSRRplkqmmtqVEAISRQLGIHSLLEKYP-----------YEISGGQKQRVAVARAIIT 162
Cdd:cd03245 87 VTLFYG-TLRDNITLgaPLADDER--------ILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
1.40e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.58 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKiyktRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNG--MDTATIKN 78
Cdd:PRK11264 1 MSAIEVKNLVK----KFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 79 KDASSFR--RERLGFVFQDFNLLDTLSVKDNILL-PLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVA 155
Cdd:PRK11264 75 QQKGLIRqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 156 VARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTA-AASRAQRVLFIKDGILYNQ 225
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQ 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-220 |
2.03e-41 |
|
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: 141.91 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 5 DVQHVKKIYKTRfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdassF 84
Cdd:cd03249 2 EFKNVSFRYPSR---PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR----W 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 85 RRERLGFVFQDFNLLDTlSVKDNILLplvlSRRPLKqmMTQVEAISRQLGIHSLLEKYPY-----------EISGGQKQR 153
Cdd:cd03249 75 LRSQIGLVSQEPVLFDG-TIAENIRY----GKPDAT--DEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 154 VAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRNADLIAVLQNG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-220 |
3.42e-41 |
|
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: 140.08 E-value: 3.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 8 HVKKIYkTRFKGNQvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDassfRRE 87
Cdd:cd03226 1 RIENIS-FSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKE----RRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 88 RLGFVFQDFNL-LDTLSVKDNILLplvlSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEI 166
Cdd:cd03226 72 SIGYVMQDVDYqLFTDSVREELLL----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 167 LLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH-STAAASRAQRVLFIKDG 220
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHdYEFLAKVCDRVLLLANG 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-223 |
3.96e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.87 E-value: 3.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 29 HFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMD-TATIKNKDASSFrrerlgfVFQDFNLLDTLSVKDN 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPSRRPVSM-------LFQENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 108 ILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDV 187
Cdd:PRK10771 92 IGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092440915 188 FDAINASGQ-TILMVTHSTAAASR-AQRVLFIKDGILY 223
Cdd:PRK10771 172 VSQVCQERQlTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-220 |
3.96e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 147.99 E-value: 3.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDassfRRERLGFVFQD 95
Cdd:COG4987 342 RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD----LRRRIAVVPQR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLDTlSVKDNILLPlvlsrRP------LKQMMTQVeaisrqlGIHSLLEKYPY-----------EISGGQKQRVAVAR 158
Cdd:COG4987 418 PHLFDT-TLRENLRLA-----RPdatdeeLWAALERV-------GLGDWLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 159 AIITKPEILLADEPTGALDSKSSAALL-DVFDAinASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLaDLLEA--LAGRTVLLITHRLAGLERMDRILVLEDG 545
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
16-220 |
4.02e-41 |
|
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: 144.10 E-value: 4.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRRERLGFVFQD 95
Cdd:TIGR02142 4 RFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLDTLSVKDNILLPLVLSRRPLKQMmtQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGA 175
Cdd:TIGR02142 84 ARLFPHLSVRGNLRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092440915 176 LDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRlADRVVVLEDG 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-220 |
5.70e-41 |
|
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: 138.72 E-value: 5.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 20 NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDassfRRERLGFVFQdfnll 99
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 dtlsvkdnillplvlsrrplkqmmtqveaISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSK 179
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092440915 180 SSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03214 132 HQIELLELLRRLARErGKTVVMVLHDLNLAARyADRVILLKDG 174
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-220 |
6.95e-41 |
|
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: 140.55 E-value: 6.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 6 VQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknKDAS--S 83
Cdd:cd03296 5 VRNVSKRF------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG--------EDATdvP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFVFQDFNLLDTLSVKDNILLPL----VLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARA 159
Cdd:cd03296 71 VQERNVGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 160 IITKPEILLADEPTGALDSKS----SAALLDVFDAInasGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVrkelRRWLRRLHDEL---HVTTVFVTHDQEEALEvADRVVVMNKG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-220 |
1.50e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.99 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDassfRRERLGFVFQd 95
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE----LRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 fnlldtlsvkdnillplvlsrrplkqmmtqveaisrqlgihsllekypyeISGGQKQRVAVARAIITKPEILLADEPTGA 175
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092440915 176 LDSKSSAALLDVFDAINASGQTILMVTHSTAAASRA-QRVLFIKDG 220
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-220 |
1.72e-40 |
|
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: 137.35 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdASSFRRERLGFVFQD 95
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW----DPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLDTlSVKDNILlplvlsrrplkqmmtqveaisrqlgihsllekypyeiSGGQKQRVAVARAIITKPEILLADEPTGA 175
Cdd:cd03246 85 DELFSG-SIAENIL-------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092440915 176 LDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-220 |
3.17e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 138.69 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 10 KKIYKtRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtATIKNKDASSFRRERl 89
Cdd:PRK09493 5 KNVSK-HFGPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK-VNDPKVDERLIRQEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 90 GFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQmmtQVEAISRQL----GIHSLLEKYPYEISGGQKQRVAVARAIITKPE 165
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLRVRGASKE---EAEKQARELlakvGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKG 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-220 |
3.64e-40 |
|
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: 138.37 E-value: 3.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknKDASSFRRERLgFVFQDFNLLDTLSV 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG--------KQITEPGPDRM-VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDNILLPL--VLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSA 182
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092440915 183 ALLDVFDAI-NASGQTILMVTHST-AAASRAQRVLFIKDG 220
Cdd:TIGR01184 152 NLQEELMQIwEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-177 |
4.67e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 140.64 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTR---FKGN--QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIK 77
Cdd:COG4608 7 LLEVRDLKKHFPVRgglFGRTvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 78 NKDASSFRReRLGFVFQD-FNLLDT-LSVKDNILLPLVLSR-RPLKQMMTQVEAISRQLGIH-SLLEKYPYEISGGQKQR 153
Cdd:COG4608 87 GRELRPLRR-RMQMVFQDpYASLNPrMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQR 165
|
170 180
....*....|....*....|....
gi 1092440915 154 VAVARAIITKPEILLADEPTGALD 177
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-203 |
3.19e-39 |
|
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: 135.35 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 20 NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATiknkdassfRRERLGFVFQDFNLL 99
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 DT--LSVKDNILLPLVLSRRPLKQMMTQVEAISRQ----LGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:cd03235 81 RDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEalerVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190
....*....|....*....|....*....|
gi 1092440915 174 GALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-214 |
3.77e-39 |
|
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: 134.91 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatiKNKDAS 82
Cdd:COG4133 2 MLEAENLSCRR------GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP----IRDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRReRLGFVFQDFNLLDTLSVKDNILLplVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:COG4133 72 DYRR-RLAYLGHADGLKPELTVRENLRF--WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRV 214
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-232 |
4.72e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 135.91 E-value: 4.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYL--NGMD-TATIKNKDASSFRRErLGFVFQDFNLL 99
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDfSKTPSDKAIRELRRN-VGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 DTLSVKDN-ILLP---LVLSRrplKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGA 175
Cdd:PRK11124 95 PHLTVQQNlIEAPcrvLGLSK---DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 176 LDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGILYNQifkGDKS 232
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQ---GDAS 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-203 |
7.85e-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: 135.55 E-value: 7.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKiyktRFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkD 80
Cdd:COG0411 2 DPLLEVRGLTK----RFGG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-----G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASSFRRERLGFV--FQDFNLLDTLSVKDNI---------------LLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYP 143
Cdd:COG0411 71 LPPHRIARLGIArtFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 144 YEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTH 203
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEH 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
8.41e-39 |
|
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: 135.64 E-value: 8.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKtrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASs 83
Cdd:TIGR04520 1 IEVENVSFSYP----ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frRERLGFVFQ--DfNLLDTLSVKD-------NILLplvlsrrPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRV 154
Cdd:TIGR04520 76 --RKKVGMVFQnpD-NQFVGATVEDdvafgleNLGV-------PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 155 AVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVLADRVIVMNKG 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
1.66e-38 |
|
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: 133.78 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRfkgnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdass 83
Cdd:cd03263 1 LQIRNLTKTYKKG----TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 fRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03263 73 -ARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 164 PEILLADEPTGALDSKSSAallDVFDAINA--SGQTILMVTHSTAAASR-AQRVLFIKDGILY 223
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRR---AIWDLILEvrKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-228 |
1.90e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.14 E-value: 1.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKkiykTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGM--DTATIKNK 79
Cdd:PRK13635 4 EIIRVEHIS----FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 80 dassfrRERLGFVFQ--DFNLLDTlSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVA 157
Cdd:PRK13635 80 ------RRQVGMVFQnpDNQFVGA-TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 158 RAIITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASRAQRVLFIKDGILYN-----QIFK 228
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQADRVIVMNKGEILEegtpeEIFK 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-177 |
2.16e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 134.58 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTR---FKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMdtaTIK 77
Cdd:COG4167 2 SALLEVRNLSKTFKYRtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 78 NKDASsFRRERLGFVFQDFNllDTLSVKDNI--LL--PLVL-SRRPLKQMMTQVEAISRQLGI---HSLLekYPYEISGG 149
Cdd:COG4167 79 YGDYK-YRCKHIRMIFQDPN--TSLNPRLNIgqILeePLRLnTDLTAEEREERIFATLRLVGLlpeHANF--YPHMLSSG 153
|
170 180
....*....|....*....|....*...
gi 1092440915 150 QKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALD 181
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-220 |
2.35e-38 |
|
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: 133.77 E-value: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkDASSFRRErLGFVFQD 95
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ-VGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 fNLLDTLSVKDNILLPlvlsrRPlKQMMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIITKP 164
Cdd:cd03252 85 -NVLFNRSIRDNIALA-----DP-GMSMERVIEAAKLAGAHDFISELPegYDtivgeqgagLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 165 EILLADEPTGALDSKSSAALLDVFDAINAsGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-179 |
3.11e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 136.75 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDass 83
Cdd:PRK10851 3 IEIANIKKSF------GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frrERLGFVFQDFNLLDTLSVKDNILLPL-VLSR--RP----LKQMMTQV-EAIsrQLGiHsLLEKYPYEISGGQKQRVA 155
Cdd:PRK10851 74 ---RKVGFVFQHYALFRHMTVFDNIAFGLtVLPRreRPnaaaIKAKVTQLlEMV--QLA-H-LADRYPAQLSGGQKQRVA 146
|
170 180
....*....|....*....|....
gi 1092440915 156 VARAIITKPEILLADEPTGALDSK 179
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQ 170
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-220 |
7.97e-38 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 131.91 E-value: 7.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 31 TVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATiknkdASSFRRErLGFVFQDFNLLDTLSVKDNILL 110
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----LAPYQRP-VSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 111 PLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDA 190
Cdd:TIGR01277 94 GLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|..
gi 1092440915 191 INASGQ-TILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:TIGR01277 174 LCSERQrTLLMVTHHLSDARAiASQIAVVSQG 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-220 |
1.82e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 132.11 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVyLNGmdTATIKNKda 81
Cdd:PRK11247 11 TPLLLNAVSKRYGER------TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG--TAPLAEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 ssfrRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPlkQMMTQVEAIsrqlGIHSLLEKYPYEISGGQKQRVAVARAII 161
Cdd:PRK11247 80 ----REDTRLMFQDARLLPWKKVIDNVGLGLKGQWRD--AALQALAAV----GLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 162 TKPEILLADEPTGALDSKSSAALLDVFDAI-NASGQTILMVTHSTA-AASRAQRVLFIKDG 220
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-203 |
3.06e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 136.69 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKiyktRFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmDTATIKN-KDA 81
Cdd:COG1129 4 LLEMRGISK----SFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG-EPVRFRSpRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 ssfRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPL---KQMMTQVEAISRQLGIH----SLLEkypyEISGGQKQRV 154
Cdd:COG1129 77 ---QAAGIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDidpdTPVG----DLSVAQQQLV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092440915 155 AVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-220 |
4.42e-37 |
|
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: 130.43 E-value: 4.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 8 HVKKIYKTRFKgnqveALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRRe 87
Cdd:cd03253 5 NVTFAYDPGRP-----VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 88 RLGFVFQDFNLLDTlSVKDNILLPlvlsrRPlKQMMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAV 156
Cdd:cd03253 76 AIGVVPQDTVLFND-TIGYNIRYG-----RP-DATDEEVIEAAKAAQIHDKIMRFPdgYDtivgerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 157 ARAIITKPEILLADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDG 211
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-220 |
6.96e-37 |
|
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: 137.30 E-value: 6.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdASSFRRERLGFVFQD 95
Cdd:TIGR03375 472 AYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI----DPADLRRNIGYVPQD 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLdTLSVKDNILLplvlsRRPL--KQMMtqVEAIsRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIIT 162
Cdd:TIGR03375 548 PRLF-YGTLRDNIAL-----GAPYadDEEI--LRAA-ELAGVTEFVRRHPdgLDmqigergrsLSGGQRQAVALARALLR 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNG 675
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-177 |
1.81e-36 |
|
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: 134.81 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYKTRfKG------NQVEALKDIHFTVDKGDYVAIMGESGSGKSTL-LNILAMLdkPTAGRVYLNGMDTA 74
Cdd:COG4172 274 PLLEARDLKVWFPIK-RGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 75 TIKNKDASSFRReRLGFVFQD-FNLLDT-LSVKDNILLPLVLSRRPL--KQMMTQVEAISRQLGIH-SLLEKYPYEISGG 149
Cdd:COG4172 351 GLSRRALRPLRR-RMQVVFQDpFGSLSPrMTVGQIIAEGLRVHGPGLsaAERRARVAEALEEVGLDpAARHRYPHEFSGG 429
|
170 180
....*....|....*....|....*...
gi 1092440915 150 QKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-225 |
4.61e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.55 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAS---------SFRRERLGF 91
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 92 VFQDFNLLDTLSVKDNILlplvlsRRPLKQM-MTQVEAISR------QLGI-HSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVM------EAPIQVLgLSKQEARERavkylaKVGIdERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGILYNQ 225
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-220 |
5.15e-36 |
|
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: 127.17 E-value: 5.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKtrfkgnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkDASS 83
Cdd:cd03224 1 LEVENLNAGYG------KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-----GLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLG--FVFQDFNLLDTLSVKDNILLPL-VLSRRPLKQMMTQVEAI-------SRQLGihsllekypYEISGGQKQR 153
Cdd:cd03224 70 HERARAGigYVPEGRRIFPELTVEENLLLGAyARRRAKRKARLERVYELfprlkerRKQLA---------GTLSGGEQQM 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 154 VAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHS-TAAASRAQRVLFIKDG 220
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNaRFALEIADRAYVLERG 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-233 |
5.43e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.57 E-value: 5.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 6 VQHVKKIYKTRFKgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTatikNKDASSFR 85
Cdd:PRK13632 10 VENVSFSYPNSEN----NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 86 RERLGFVFQD-FNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKP 164
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 165 EILLADEPTGALDSKSSAALLDVFDAINASG-QTILMVTHSTAAASRAQRVLFIKDGILynqIFKGDKSE 233
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKL---IAQGKPKE 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-215 |
2.53e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 125.29 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLN-ILAMLDKP--TAGRVYLNGMDTATIKNkdassfRRERLGFVFQDFNLLDT 101
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPA------EQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNIL--LPLVLSRRPLKQmmtQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDsk 179
Cdd:COG4136 91 LSVGENLAfaLPPTIGRAQRRA---RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092440915 180 ssAALLD-----VFDAINASGQTILMVTHSTAAASRAQRVL 215
Cdd:COG4136 166 --AALRAqfrefVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-220 |
2.96e-35 |
|
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: 125.17 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 8 HVKKIYKT-RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiKNKDASsfrR 86
Cdd:cd03266 3 TADALTKRfRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--KEPAEA---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 ERLGFVFQDFNLLDTLSVKDNILL---PLVLSRRPLKQmmtQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYfagLYGLKGDELTA---RLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRG 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-203 |
3.31e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.92 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 9 VKKIYKtRFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmDTATIKN-KDAssfRRE 87
Cdd:COG3845 8 LRGITK-RFGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-KPVRIRSpRDA---IAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 88 RLGFVFQDFNLLDTLSVKDNILL---PLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKP 164
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092440915 165 EILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-188 |
4.87e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 127.39 E-value: 4.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTR---FKGN-QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATi 76
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKrglFKPErLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 77 KNKDASSFRRERLGFVFQdfNLLDTLS----VKDNILLPLV----LSRrplKQMMTQVEAISRQLGI---HSllEKYPYE 145
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQ--NPYGSLNprkkVGQILEEPLLintsLSA---AERREKALAMMAKVGLrpeHY--DRYPHM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092440915 146 ISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVF 188
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-247 |
6.38e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.29 E-value: 6.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKiYKTRFKGnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYL-NGMDTATIKNK 79
Cdd:PRK13634 3 ITFQKVEHRYQ-YKTPFER---RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 80 DASSFRReRLGFVFQ--DFNLLDTLSVKD------NILLPLVLSRRPLKQMMTQVeaisrqlGI-HSLLEKYPYEISGGQ 150
Cdd:PRK13634 79 KLKPLRK-KVGIVFQfpEHQLFEETVEKDicfgpmNFGVSEEDAKQKAREMIELV-------GLpEELLARSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 151 KQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAIN-ASGQTILMVTHSTA-AASRAQRVLFIKDGilynQIFK 228
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEdAARYADQIVVMHKG----TVFL 226
|
250
....*....|....*....
gi 1092440915 229 gDKSEHQMFQEiSDTLTAM 247
Cdd:PRK13634 227 -QGTPREIFAD-PDELEAI 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-220 |
7.18e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.03 E-value: 7.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRFkgnqveALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkDAS 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQH------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRRErLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:PRK11607 88 PYQRP-INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 163 KPEILLADEPTGALDSKSSAAL-LDVFDAINASGQTILMVTHSTAAA-SRAQRVLFIKDG 220
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRG 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-215 |
3.16e-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: 128.94 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKnkdaSSFRRERLGFVFQDFNLLDTl 102
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNILLPL-VLSRRPLKQMMTQVEAI----SRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:TIGR02857 411 TIAENIRLARpDASDAEIREALERAGLDefvaALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092440915 178 SKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVL 215
Cdd:TIGR02857 491 AETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIV 527
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-220 |
1.36e-33 |
|
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: 121.18 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 19 GNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAssfrRERLGFVFQDFNL 98
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 99 LDTlSVKDNILLplvlsRRPLKQmMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIITKPEIL 167
Cdd:cd03254 89 FSG-TIMENIRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKLPngYDtvlgenggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 168 LADEPTGALDSKSSAALLDVFDAINaSGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-220 |
3.12e-33 |
|
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: 126.40 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 19 GNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTatiknkdaSSFRRERL----GFVFQ 94
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL--------SQWDREELgrhiGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 95 DFNLLDTlSVKDNIllplvlSRrplkqmMTQV--EAI---SRQLGIHSLLEKYP--YE---------ISGGQKQRVAVAR 158
Cdd:COG4618 414 DVELFDG-TIAENI------AR------FGDAdpEKVvaaAKLAGVHEMILRLPdgYDtrigeggarLSGGQRQRIGLAR 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 159 AIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-227 |
5.07e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 120.53 E-value: 5.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNIL-AMLDK-PTA---GRVYLNGMDtatI--KNKDASSFRReRLGFVFQD 95
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLnRMNDLiPGArveGEILLDGED---IydPDVDVVELRR-RVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLdTLSVKDNILLPL----VLSRRPLKQMmtqVEAISRQLGihsL-------LEKYPYEISGGQKQRVAVARAIITKP 164
Cdd:COG1117 101 PNPF-PKSIYDNVAYGLrlhgIKSKSELDEI---VEESLRKAA---LwdevkdrLKKSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 165 EILLADEPTGALDSKSSAALLDVFDAInaSGQ-TILMVTHSTAAASR-AQRVLFIKDGIL--YN---QIF 227
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILEL--KKDyTIVIVTHNMQQAARvSDYTAFFYLGELveFGpteQIF 241
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-220 |
6.60e-33 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 119.64 E-value: 6.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKnkdASSFRRErLGFVFQD 95
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ-IGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLDTlSVKDNILlplvLSRRplKQMMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIITKP 164
Cdd:cd03251 85 VFLFND-TVAENIA----YGRP--GATREEVEEAARAANAHEFIMELPegYDtvigergvkLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 165 EILLADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDG 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-203 |
1.37e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 119.85 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYK--TRFKGnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMD-TATIKNKD 80
Cdd:PRK13649 3 INLQNVSYTYQagTPFEG---RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASSFRReRLGFVFQ--DFNLLDTLSVKDNILLPLVLSRRPlkqmmTQVEAISRQ----LGI-HSLLEKYPYEISGGQKQR 153
Cdd:PRK13649 80 IKQIRK-KVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-----EEAEALAREklalVGIsESLFEKNPFELSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1092440915 154 VAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-222 |
1.70e-32 |
|
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: 124.00 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRReRLGFVFQDFNLLDTlSV 104
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAD---LKQWDRETFGK-HIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDNIllplvlSRRPLKQMMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:TIGR01842 409 AENI------ARFGENADPEKIIEAAKLAGVHELILRLPdgYDtvigpggatLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092440915 174 GALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDGIL 222
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-234 |
2.16e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.96 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 6 VQHVKKIYKTRfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAML---DKPTAGRVYLNGmDTATIKNKDAS 82
Cdd:PRK09984 4 IIRVEKLAKTF---NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLG-RTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRRER--LGFVFQDFNLLDTLSVKDNILLPlVLSRRPL----------KQMMTQVEAISRqLGIHSLLEKYPYEISGGQ 150
Cdd:PRK09984 80 DIRKSRanTGYIFQQFNLVNRLSVLENVLIG-ALGSTPFwrtcfswftrEQKQRALQALTR-VGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 151 KQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDGILY----N 224
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRyCERIVALRQGHVFydgsS 237
|
250
....*....|
gi 1092440915 225 QIFKGDKSEH 234
Cdd:PRK09984 238 QQFDNERFDH 247
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-231 |
2.31e-32 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 119.14 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYKTR---FKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKN 78
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 79 KDASSFRRErLGFVFQD----FNllDTLSVKDNIllplvlsRRPLKQmMTQVEAISRQLGIHSLLE----------KYPY 144
Cdd:TIGR02769 81 KQRRAFRRD-VQLVFQDspsaVN--PRMTVRQII-------GEPLRH-LTSLDESEQKARIAELLDmvglrsedadKLPR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 145 EISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASR-AQRVLFIKDGIL 222
Cdd:TIGR02769 150 QLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQaFGTAYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
....*....
gi 1092440915 223 YNQIFKGDK 231
Cdd:TIGR02769 230 VEECDVAQL 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-220 |
2.71e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.04 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 13 YKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNK-DAssfrRERLGF 91
Cdd:PRK13633 14 YESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDI----RNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 92 VFQ--DFNLLDTLSVKDNILLPLVLSRRPlKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLA 169
Cdd:PRK13633 90 VFQnpDNQIVATIVEEDVAFGPENLGIPP-EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 170 DEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSG 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-220 |
2.89e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.81 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 9 VKKIYKTRFKGNQVE--ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDA----- 81
Cdd:PRK13651 5 VKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEkekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 -------SSFR--------RERLGFVFQ--DFNLLDTLSVKDNILLPLVLSrrplkqmMTQVEAISRQLGI-------HS 137
Cdd:PRK13651 85 eklviqkTRFKkikkikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMG-------VSKEEAKKRAAKYielvgldES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 138 LLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHS-TAAASRAQRVLF 216
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIF 237
|
....
gi 1092440915 217 IKDG 220
Cdd:PRK13651 238 FKDG 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
4.88e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.87 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKkiykTRFK--GNQVEALKDIHFTVDKGDYVAIMGESGSGKS-TLLNILAMLDKPTA---GRVYLNGMDTA 74
Cdd:COG4172 4 MPLLSVEDLS----VAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 75 TIKNKDASSFRRERLGFVFQD----FNLLDTlsVKDNILLPLVLsrrplKQMMTQVEAISR------QLGIH---SLLEK 141
Cdd:COG4172 80 GLSERELRRIRGNRIAMIFQEpmtsLNPLHT--IGKQIAEVLRL-----HRGLSGAAARARalelleRVGIPdpeRRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 142 YPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKD 219
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRfADRVAVMRQ 232
|
.
gi 1092440915 220 G 220
Cdd:COG4172 233 G 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-204 |
6.30e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.88 E-value: 6.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 9 VKKIYKTRFKG--NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdaSSFRR 86
Cdd:COG1101 4 LKNLSKTFNPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-----PEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 ERL-GFVFQDfNLLDT---LSVKDNILL------PLVLSRRPLKQMMTQVEAISRQLGIHslLEKYPYE----ISGGQKQ 152
Cdd:COG1101 79 AKYiGRVFQD-PMMGTapsMTIEENLALayrrgkRRGLRRGLTKKRRELFRELLATLGLG--LENRLDTkvglLSGGQRQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 153 RVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQ-TILMVTHS 204
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHN 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-215 |
9.50e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.41 E-value: 9.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknkdassfrRERLGFVFQDFNLLDTL- 102
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 -SVKDNILL----PLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:NF040873 72 lTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092440915 178 SKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVL 215
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-220 |
1.82e-31 |
|
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: 113.68 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAss 83
Cdd:cd03216 1 LELRGITKRF------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 fRRERLGFVFQdfnlldtlsvkdnillplvlsrrplkqmmtqveaisrqlgihsllekypyeISGGQKQRVAVARAIITK 163
Cdd:cd03216 73 -RRAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-205 |
2.70e-31 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 114.19 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTA--GRVYLNGmdtatiKNKDASSFRReRLGFVFQDFNLLDTL 102
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING------RPLDKRSFRK-IIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNILLPLVLSRrplkqmmtqveaisrqlgihsllekypyeISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSA 182
Cdd:cd03213 98 TVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180
....*....|....*....|...
gi 1092440915 183 ALLDVFDAINASGQTILMVTHST 205
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHQP 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-220 |
2.93e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.69 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDAS-SFRRERLGFVFQ--DFNLL 99
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD---ITDKKVKlSDIRKKVGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 DTLSVKDNILLP--LVLS----RRPLKQMMTQVeaisrQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:PRK13637 98 EETIEKDIAFGPinLGLSeeeiENRVKRAMNIV-----GLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092440915 174 GALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKlADRIIVMNKG 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-220 |
2.95e-31 |
|
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: 114.77 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknKDASS 83
Cdd:cd03265 1 IEVENLVKKY------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03265 71 VRR-RIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQlCDRVAIIDHG 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-220 |
5.97e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.55 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKT---RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIK 77
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 78 NKDASSFRRErLGFVFQD----FNllDTLSVKDNIllplvlsRRPLKQMMT--------QVEAISRQLGIH-SLLEKYPY 144
Cdd:PRK10419 81 RAQRKAFRRD-IQMVFQDsisaVN--PRKTVREII-------REPLRHLLSldkaerlaRASEMLRAVDLDdSVLDKRPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 145 EISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERfCQRVMVMDNG 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-220 |
7.49e-31 |
|
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: 114.07 E-value: 7.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKiyktRFK-----GNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLN----GMD 72
Cdd:COG4778 3 TLLEVENLSK----TFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 73 TATIKNKDASSFRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLL-EKYPYEISGGQK 151
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 152 QRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
8.12e-31 |
|
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: 114.41 E-value: 8.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVY------LNGMDTA 74
Cdd:COG1119 1 DPLLELRNVTVRR------GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 75 TIknkdassfrRERLGFVFQDF--NLLDTLSVKDnillpLVLS---------RRPLKQMMTQVEAISRQLGIHSLLEKYP 143
Cdd:COG1119 75 EL---------RKRIGLVSPALqlRFPRDETVLD-----VVLSgffdsiglyREPTDEQRERARELLELLGLAHLADRPF 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 144 YEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQ-TILMVTHSTAAASRA-QRVLFIKDG 220
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGiTHVLLLKDG 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-220 |
1.29e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.44 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRRERLGFVFQDFNLLDTLS 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 VKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAA 183
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092440915 184 LLDVFDAINASGQ-TILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK10070 203 MQDELVKLQAKHQrTIVFISHDLDEAMRiGDRIAIMQNG 241
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-220 |
1.78e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 116.13 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 39 AIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRRERLGFVFQDFNLLDTLSVKDNILLPLVlsrrp 118
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 119 lKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQT- 197
Cdd:PRK11144 103 -KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIp 181
|
170 180
....*....|....*....|....
gi 1092440915 198 ILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK11144 182 ILYVSHSLDEILRlADRVVVLEQG 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-220 |
2.26e-30 |
|
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: 115.28 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 40 IMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdaSSFRRErLGFVFQDFNLLDTLSVKDNILLPLVLSRRPL 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV-----PPHLRH-INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 120 KQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAAL-LDVFDAINASGQTI 198
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGITF 154
|
170 180
....*....|....*....|...
gi 1092440915 199 LMVTHSTAAA-SRAQRVLFIKDG 220
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKG 177
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-203 |
3.62e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.87 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMdtaTIKNKDAssfrrERlGFVFQDFNLLDTLS 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGA-----ER-GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 VKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDS----K 179
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftreQ 166
|
170 180
....*....|....*....|....
gi 1092440915 180 SSAALLDVFdaiNASGQTILMVTH 203
Cdd:PRK11248 167 MQTLLLKLW---QETGKQVLLITH 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-222 |
4.52e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 117.90 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 7 QHVKKIYKTRfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRR 86
Cdd:TIGR00958 482 QDVSFSYPNR---PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP---LVQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 eRLGFVFQDfNLLDTLSVKDNILLPLvlSRRPLKQMMtqveAISRQLGIHSLLEKYPYEI-----------SGGQKQRVA 155
Cdd:TIGR00958 556 -QVALVGQE-PVLFSGSVRENIAYGL--TDTPDEEIM----AAAKAANAHDFIMEFPNGYdtevgekgsqlSGGQKQRIA 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 156 VARAIITKPEILLADEPTGALDSKSSAALldvFDAINASGQTILMVTHSTAAASRAQRVLFIKDGIL 222
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLL---QESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-179 |
4.81e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.04 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkD 80
Cdd:PRK09452 12 SPLVELRGISKSFDGK------EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----H 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASSFRRErLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK09452 81 VPAENRH-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170
....*....|....*....
gi 1092440915 161 ITKPEILLADEPTGALDSK 179
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYK 178
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-232 |
7.25e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.52 E-value: 7.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTatikNKDASSFRRERLGFVFQD-FNLLDT 101
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV----NAENEKWVRSKVGLVFQDpDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNILL-PLVLSRRPlKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKS 180
Cdd:PRK13647 95 STVWDDVAFgPVNMGLDK-DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 181 SAALLDVFDAINASGQTILMVTHST-AAASRAQRVLFIKDGILYNQifkGDKS 232
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVdLAAEWADQVIVLKEGRVLAE---GDKS 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-180 |
8.73e-30 |
|
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: 111.48 E-value: 8.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdaSS 83
Cdd:cd03218 1 LRAENLSKRYGKR------KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-----PM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFVF--QDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAII 161
Cdd:cd03218 70 HKRARLGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170
....*....|....*....
gi 1092440915 162 TKPEILLADEPTGALDSKS 180
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIA 168
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-220 |
1.76e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 110.46 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkD 80
Cdd:COG0410 1 MPMLEVENLHAGY------GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-----G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASSFRRERLGFVF--QDFNLLDTLSVKDNILLPLVL--SRRPLKQMMTQVEAI-------SRQLGihSLLekypyeiSGG 149
Cdd:COG0410 70 LPPHRIARLGIGYvpEGRRIFPSLTVEENLLLGAYArrDRAEVRADLERVYELfprlkerRRQRA--GTL-------SGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 150 QKQRVAVARAIITKPEILLADEPTGALdskssAALL--DVFDAI---NASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGL-----APLIveEIFEIIrrlNREGVTILLVEQNARFALEiADRAYVLERG 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-203 |
2.50e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.75 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMD-TATIKNKDASSFRReRLGFVFQ--DFNLLD 100
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvSSTSKQKEIKPVRK-KVGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 101 TLSVKDNILLP--LVLSRRPLKQMMTQ---VEAISRQLgihslLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGA 175
Cdd:PRK13643 100 ETVLKDVAFGPqnFGIPKEKAEKIAAEkleMVGLADEF-----WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180
....*....|....*....|....*...
gi 1092440915 176 LDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-210 |
3.40e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.39 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAML-----DKPTAGRVYLNGMDtatIKNKDASSFRReRLGFVFQD 95
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQD---IFKMDVIELRR-RVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLLDTLSVKDNILLPLVLSR--RPLKQMMTQV-EAISR-QL--GIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLA 169
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNRlvKSKKELQERVrWALEKaQLwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092440915 170 DEPTGALDSKSSAALLDVFDAINASgQTILMVTHSTAAASR 210
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAAR 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-222 |
1.85e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.15 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMD-TATIKNKDASSFRReRLGFVFQ--DFN 97
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHiTPETGNKNLKKLRK-KVSLVFQfpEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 98 LLDTLSVKDNILLPLVLSRRPLKQMMTQVEAIsRQLGI-HSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGAL 176
Cdd:PRK13641 98 LFENTVLKDVEFGPKNFGFSEDEAKEKALKWL-KKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092440915 177 DSKSSAALLDVFDAINASGQTILMVTHST-AAASRAQRVLFIKDGIL 222
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKL 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-220 |
2.00e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.58 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 10 KKIYKtRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTA--TIKNKDassfrre 87
Cdd:PRK11432 10 KNITK-RFGSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRD------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 88 rLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEIL 167
Cdd:PRK11432 80 -ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 168 LADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTH-STAAASRAQRVLFIKDG 220
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHdQSEAFAVSDTVIVMNKG 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-220 |
2.80e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 105.86 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 17 FKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdassfRRERLGFVFQDF 96
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 NLLDTlSVKDNILLPLvlsrrplkqmmtqveaisrqlgihsllekypyeiSGGQKQRVAVARAIITKPEILLADEPTGAL 176
Cdd:cd03247 85 YLFDT-TLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092440915 177 DSKSSAALLD-VFDAinASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03247 130 DPITERQLLSlIFEV--LKDKTLIWITHHLTGIEHMDKILFLENG 172
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-204 |
3.33e-28 |
|
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: 112.07 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkDASSFRReRLGFVFQDFNLLDTl 102
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL---DQDEVRR-RVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNILLPlvlsrRPlKQMMTQVEAISRQLGIHSLLEKYPY-----------EISGGQKQRVAVARAIITKPEILLADE 171
Cdd:TIGR02868 424 TVRENLRLA-----RP-DATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 1092440915 172 PTGALDSKSSAALL-DVFDAInaSGQTILMVTHS 204
Cdd:TIGR02868 498 PTEHLDAETADELLeDLLAAL--SGRTVVLITHH 529
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-229 |
4.03e-28 |
|
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: 106.51 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYvAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknKDASS 83
Cdd:cd03264 1 LQLENLTKRYGKK------RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRReRLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03264 70 LRR-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTA-AASRAQRVLFIKDGILynqIFKG 229
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEdVESLCNQVAVLNKGKL---VFEG 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-224 |
4.36e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 107.03 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 6 VQHVKKIYKTRFKG---------------NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNG 70
Cdd:cd03267 3 VSNLSKSYRVYSKEpgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 71 MDTATIKNKdassFRReRLGFVF-QDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGG 149
Cdd:cd03267 83 LVPWKRRKK----FLR-RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 150 QKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTA-AASRAQRVLFIKDG-ILYN 224
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKdIEALARRVLVIDKGrLLYD 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-179 |
5.96e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.16 E-value: 5.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKD 80
Cdd:PRK11650 1 MAGLKLQAVRKSY-----DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 assfrRErLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK11650 76 -----RD-IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170
....*....|....*....
gi 1092440915 161 ITKPEILLADEPTGALDSK 179
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAK 168
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-220 |
6.84e-28 |
|
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: 105.63 E-value: 6.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLN-ILAMLDKpTAGRVYLNGmdtatiknkdassfrreRLGFVFQDFNLLDTl 102
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPG-----------------SIAYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNIL--LPL-------VLS----RRPLKQM----MTQV-EAisrqlGIhSLlekypyeiSGGQKQRVAVARAIITKP 164
Cdd:cd03250 81 TIRENILfgKPFdeeryekVIKacalEPDLEILpdgdLTEIgEK-----GI-NL--------SGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 165 EILLADEPTGALDSKSSAALLDvfDAIN---ASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFE--NCILgllLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-172 |
7.21e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 106.65 E-value: 7.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMD-Tatiknk 79
Cdd:COG1137 1 MMTLEAENLVKSYGKR------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDiT------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 80 DASSFRRERLGF--------VFQDfnlldtLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQK 151
Cdd:COG1137 69 HLPMHKRARLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGER 142
|
170 180
....*....|....*....|.
gi 1092440915 152 QRVAVARAIITKPEILLADEP 172
Cdd:COG1137 143 RRVEIARALATNPKFILLDEP 163
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-220 |
3.60e-27 |
|
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: 103.90 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTrfkgnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNG--MDTATiknkda 81
Cdd:cd03269 1 LEVENVTKRFGR------VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 ssfrRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAII 161
Cdd:cd03269 69 ----RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 162 TKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-220 |
3.61e-27 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 109.52 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRReRLGFVFQD---FNllDT 101
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD---IRDVTQASLRA-AIGIVPQDtvlFN--DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LsvKDNILLPlvlsrRPlKQMMTQVEAISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIITKPEILLAD 170
Cdd:COG5265 448 I--AYNIAYG-----RP-DASEEEVEAAARAAQIHDFIESLPdgYDtrvgerglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 171 EPTGALDSKSSAALLDVFDAInASGQTILMVTH--STAAasRAQRVLFIKDG 220
Cdd:COG5265 520 EATSALDSRTERAIQAALREV-ARGRTTLVIAHrlSTIV--DADEILVLEAG 568
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-220 |
4.07e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 109.28 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 19 GNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdasSFRRErLGFVFQDFNL 98
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA---SLRRN-IAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 99 LDTlSVKDNILLPlvlsrRP---LKQMMTQVEAISRQLGIHSLLEKYPYEI-------SGGQKQRVAVARAIITKPEILL 168
Cdd:PRK13657 421 FNR-SIEDNIRVG-----RPdatDEEMRAAAERAQAHDFIERKPDGYDTVVgergrqlSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 169 ADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-220 |
6.63e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 6.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtATIKNKDASSFR-RERLGFVFQdfNLLDT 101
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG---EPIKYDKKSLLEvRKTVGIVFQ--NPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 L---SVKDNILL-PLVLSRrPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK13639 91 LfapTVEEDVAFgPLNLGL-SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1092440915 178 SKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK13639 170 PMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDG 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-204 |
7.97e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 105.70 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRfKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYL-------------N 69
Cdd:PRK13631 21 ILRVKNLYCVFDEK-QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 70 GMDTATIKNKDASSFRReRLGFVFQ--DFNLLDTLSVKDNILLPLVLSrrplkqmMTQVEAISR------QLGI-HSLLE 140
Cdd:PRK13631 100 ITNPYSKKIKNFKELRR-RVSMVFQfpEYQLFKDTIEKDIMFGPVALG-------VKKSEAKKLakfylnKMGLdDSYLE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 141 KYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHS 204
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-220 |
8.91e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 104.24 E-value: 8.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAS 82
Cdd:PRK11701 6 LLSVRGLTKLYGPR------KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRRERL-----GFVFQdfNLLDTL----SVKDNILLPLVLS--------RRPLKQMMTQVE-AISRqlgihslLEKYPY 144
Cdd:PRK11701 80 EAERRRLlrtewGFVHQ--HPRDGLrmqvSAGGNIGERLMAVgarhygdiRATAGDWLERVEiDAAR-------IDDLPT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 145 EISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAAsR--AQRVLFIKDG 220
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVA-RllAHRLLVMKQG 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-203 |
1.02e-26 |
|
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: 103.12 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 18 KGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLD---KPTAGRVYLNGMDtatiknKDASSFRReRLGFVFQ 94
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQP------RKPDQFQK-CVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 95 DFNLLDTLSVKD------NILLPlVLSRRPLKQMMTQVEAIsRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILL 168
Cdd:cd03234 89 DDILLPGLTVREtltytaILRLP-RKSSDAIRKKRVEDVLL-RDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1092440915 169 ADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-220 |
1.40e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.91 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkDASSFR--RERLGFVFQDFNLL-- 99
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-----DFSKLQgiRKLVGIVFQNPETQfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 ------DTLSVKDNILLPLVLSRRPLKQMMTQVEaisrqlgihslLEKY----PYEISGGQKQRVAVARAIITKPEILLA 169
Cdd:PRK13644 92 grtveeDLAFGPENLCLPPIEIRKRVDRALAEIG-----------LEKYrhrsPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 170 DEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRG 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-203 |
1.98e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 105.50 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 26 KDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASsfrrerLGFVFQDFNLLDTLSVK 105
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------VGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 106 DNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDskssaALL 185
Cdd:PRK11000 94 ENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD-----AAL 168
|
170 180
....*....|....*....|....
gi 1092440915 186 DVFDAINAS------GQTILMVTH 203
Cdd:PRK11000 169 RVQMRIEISrlhkrlGRTMIYVTH 192
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-203 |
3.62e-26 |
|
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: 101.14 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiKNKDAss 83
Cdd:cd03268 1 LKTNDLTKTYGKK------RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEA-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKqmmtQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:cd03268 71 --LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH 184
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
4.43e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 101.70 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MT-LLDVQHVKKIYKTRFKGNQ----------------VEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTA 63
Cdd:COG1134 1 MSsMIEVENVSKSYRLYHEPSRslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 64 GRVYLNGmdtatiknkdassfrreRLGFvfqdfnLLDT-------LSVKDNILLP---LVLSRRPLKQMMTQVEAISrQL 133
Cdd:COG1134 81 GRVEVNG-----------------RVSA------LLELgagfhpeLTGRENIYLNgrlLGLSRKEIDEKFDEIVEFA-EL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 134 G--IHSLLEKYpyeiSGGQKQRVAVARAIITKPEILLADEPTGALDS----KSSAALLDVFDainaSGQTILMVTHSTAA 207
Cdd:COG1134 137 GdfIDQPVKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIRELRE----SGRTVIFVSHSMGA 208
|
250
....*....|....*.
gi 1092440915 208 ASR-AQRVLFIKDGIL 222
Cdd:COG1134 209 VRRlCDRAIWLEKGRL 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-220 |
5.11e-26 |
|
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: 101.39 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdas 82
Cdd:cd03248 11 IVKFQNVTFAYPTR---PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 sFRRERLGFVFQDfNLLDTLSVKDNILLPLvlsrrPLKQMMTQVEAISRQlGIHSLLEKYPYEI-----------SGGQK 151
Cdd:cd03248 85 -YLHSKVSLVGQE-PVLFARSLQDNIAYGL-----QSCSFECVKEAAQKA-HAHSFISELASGYdtevgekgsqlSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 152 QRVAVARAIITKPEILLADEPTGALDSKSSAAlldVFDAINA--SGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQ---VQQALYDwpERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-203 |
5.42e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 103.65 E-value: 5.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTRfKGNqVEALKDIHFTVDKGDYVAIMGESGSGKS-TLLNILAMLDKP--TAGRVYLNGMDTATIK 77
Cdd:PRK09473 10 DALLDVKDLRVTFSTP-DGD-VTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 78 NKDASSFRRERLGFVFQD--FNLLDTLSVKDNILLPLVLSRRPLKQ--------MMTQV---EAISRqlgihslLEKYPY 144
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAeafeesvrMLDAVkmpEARKR-------MKMYPH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 145 EISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQT-ILMVTH 203
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITH 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
5.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTrfkgNQVE-ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmDTATIKNk 79
Cdd:PRK13650 2 SNIIEVKNLTFKYKE----DQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEEN- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 80 daSSFRRERLGFVFQD-FNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVAR 158
Cdd:PRK13650 76 --VWDIRHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 159 AIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQ-TILMVTHSTAAASRAQRVLFIKDG 220
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQmTVISITHDLDEVALSDRVLVMKNG 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-225 |
8.78e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 8.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMdTATIKNKDaSSFR--RERLGFVFQdfnL 98
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDI-TITHKTKD-KYIRpvRKRIGMVFQ---F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 99 LDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIH-----SLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:PRK13646 94 PESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 174 GALDSKSSAALLDVFDAINA-SGQTILMVTHSTAAASR-AQRVLFIKDGILYNQ 225
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQ 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-240 |
1.19e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.80 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKST---LLNILAMLDKPTAGRVYLNGMDTatikNKD 80
Cdd:PRK13640 6 VEFKHVSFTYPD----SKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITL----TAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASSFRRERLGFVFQD-FNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK13640 78 TVWDIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 160 IITKPEILLADEPTGALDSKSSAALLDVF-DAINASGQTILMVTHSTAAASRAQRVLFIKDGILYNQ-----IFkgdkSE 233
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIrKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQgspveIF----SK 233
|
....*..
gi 1092440915 234 HQMFQEI 240
Cdd:PRK13640 234 VEMLKEI 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-233 |
1.76e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 5 DVQHVKKIYktrFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDK------PTAGRVYLNGMDTATIkn 78
Cdd:PRK14246 9 DVFNISRLY---LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 79 kDASSFRRErLGFVFQDFNLLDTLSVKDNILLPL----VLSRRPLKQMMtqvEAISRQLG----IHSLLEKYPYEISGGQ 150
Cdd:PRK14246 84 -DAIKLRKE-VGMVFQQPNPFPHLSIYDNIAYPLkshgIKEKREIKKIV---EECLRKVGlwkeVYDRLNSPASQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 151 KQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASgQTILMVTHSTAAASR-AQRVLFIKDGILY-----N 224
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARvADYVAFLYNGELVewgssN 237
|
....*....
gi 1092440915 225 QIFKGDKSE 233
Cdd:PRK14246 238 EIFTSPKNE 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-177 |
1.80e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 101.02 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYKTR---FKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATikn 78
Cdd:PRK15112 3 TLLEVRNLSKTFRYRtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 79 kDASSFRRERLGFVFQD-FNLLDTLSVKDNIL-LPLVLSrrplkqmmTQVEAISRQLGIHSLLEK----------YPYEI 146
Cdd:PRK15112 80 -GDYSYRSQRIRMIFQDpSTSLNPRQRISQILdFPLRLN--------TDLEPEQREKQIIETLRQvgllpdhasyYPHML 150
|
170 180 190
....*....|....*....|....*....|.
gi 1092440915 147 SGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-202 |
2.16e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 98.27 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRRERLGFVFQD---FNLLD 100
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP---VTRRSPRDAIRAGIAYVPEDrkrEGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 101 TLSVKDNILLPLVLSrrplkqmmtqveaisrqlgihsllekypyeisGGQKQRVAVARAIITKPEILLADEPTGALDSKS 180
Cdd:cd03215 92 DLSVAENIALSSLLS--------------------------------GGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180
....*....|....*....|..
gi 1092440915 181 SAALLDVFDAINASGQTILMVT 202
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLLIS 161
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-203 |
2.55e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 103.97 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKP---TAGRVYLNGMdtatiknKDASSFRRERLGFVFQDFNLLDT 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM-------PIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNILLP--LVLSRR-PLKQMMTQVEAISRQLGIHSL------LEKYPYEISGGQKQRVAVARAIITKPEILLADEP 172
Cdd:TIGR00955 114 LTVREHLMFQahLRMPRRvTKKEKRERVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|.
gi 1092440915 173 TGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-220 |
2.80e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 103.71 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 9 VKKIYKTrFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFrreR 88
Cdd:PRK09700 8 MAGIGKS-FGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 89 LGFVFQDFNLLDTLSVKDNILLPLVLSRRPL-------KQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAII 161
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKKVCgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 162 TKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-222 |
4.54e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.53 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAML-----DKPTAGRVYLNGMDtatIKNKDASSFR-RERLGFVFQDF 96
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRN---IYSPDVDPIEvRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 NLLDTLSVKDNILLPLVLSR--RPLKQMMTQVEAISRQLG----IHSLLEKYPYEISGGQKQRVAVARAIITKPEILLAD 170
Cdd:PRK14267 95 NPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAAlwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 171 EPTGALDSKSSAALLDVFDAINASgQTILMVTHSTAAASR-AQRVLFIKDGIL 222
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARvSDYVAFLYLGKL 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-245 |
5.40e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.08 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 20 NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLL-NILAMLD-KP---TAGRVYLNGMDTATiKNKDASSFRRErLGFVFQ 94
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrSINRMNDlNPevtITGSIVYNGHNIYS-PRTDTVDLRKE-IGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 95 DFNLLdTLSVKDNILLPLVLSRRPLKQMMTQ-VEAISRQLGIHSLLEKYPYE----ISGGQKQRVAVARAIITKPEILLA 169
Cdd:PRK14239 94 QPNPF-PMSIYENVVYGLRLKGIKDKQVLDEaVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 170 DEPTGALDSKSSAALLDVFDAINASgQTILMVTHSTAAASR-AQRVLFIKDG--ILYNQIfkgdkseHQMF-----QEIS 241
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRiSDRTGFFLDGdlIEYNDT-------KQMFmnpkhKETE 244
|
....
gi 1092440915 242 DTLT 245
Cdd:PRK14239 245 DYIS 248
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-223 |
7.52e-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: 97.99 E-value: 7.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 11 KIYKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdassfrreRLG 90
Cdd:cd03220 24 GILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----------GLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 91 FVFQdfnllDTLSVKDNILLPLVL---SRRPLKQMMTQVEAISrQLG--IHSLLEKYpyeiSGGQKQRVAVARAIITKPE 165
Cdd:cd03220 93 GGFN-----PELTGRENIYLNGRLlglSRKEIDEKIDEIIEFS-ELGdfIDLPVKTY----SSGMKARLAFAIATALEPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGILY 223
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-239 |
8.79e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 8.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiKNKDA 81
Cdd:PRK13636 4 YILKVEELNYNY-----SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG------KPIDY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 SSF----RRERLGFVFQD-FNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAV 156
Cdd:PRK13636 73 SRKglmkLRESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 157 ARAIITKPEILLADEPTGALDSKSSAALLD-VFDAINASGQTILMVTHST-AAASRAQRVLFIKDGILynqIFKGDKSEh 234
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKlLVEMQKELGLTIIIATHDIdIVPLYCDNVFVMKEGRV---ILQGNPKE- 228
|
....*
gi 1092440915 235 qMFQE 239
Cdd:PRK13636 229 -VFAE 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-225 |
1.41e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.85 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 28 IHFTVDKGDYVAIMGESGSGKSTLLN-ILAMLdkPTAGRVYLNGMDtatIKNKDASSFRRErLGFVFQDFNLLDTlSVKD 106
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIE---LRELDPESWRKH-LSWVGQNPQLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 107 NILLPlvlsrrplKQMMT--QVEAISRQLGIHSLLEKYP----YEI-------SGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:PRK11174 442 NVLLG--------NPDASdeQLQQALENAWVSEFLPLLPqgldTPIgdqaaglSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 174 GALDSKSSAAlldVFDAIN--ASGQTILMVTHSTAAASRAQRVLFIKDGILYNQ 225
Cdd:PRK11174 514 ASLDAHSEQL---VMQALNaaSRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-240 |
1.16e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.97 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMdtaTIKNKDASSFRrERLGFVFQD 95
Cdd:PRK13648 16 QYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLR-KHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 -FNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTG 174
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 175 ALDSKSSAALLDVFDAINASGQ-TILMVTHSTAAASRAQRVLFIKDGILYNQ-----IFKgdksEHQMFQEI 240
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEgtpteIFD----HAEELTRI 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-203 |
1.72e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNgmdtatiknkdassfRRERLGFVFQDFNLLDTLSV 104
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDNILlplvLSRRPLKQMMTQVEAISRQLG--------IHSLLEK--------YPYEI---------------------S 147
Cdd:COG0488 79 LDTVL----DGDAELRALEAELEELEAKLAepdedlerLAELQEEfealggweAEARAeeilsglgfpeedldrpvselS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 148 GGQKQRVAVARAIITKPEILLADEPTGALDskssaalldvFDAI-------NASGQTILMVTH 203
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD----------LESIewleeflKNYPGTVLVVSH 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-215 |
2.21e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKkiyktrFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDas 82
Cdd:PRK10247 7 LLQLQNVG------YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 sfRRERLGFVFQDFNLL-DTlsVKDNILLPLVLsrRPLKQMMTQVEAISRQLGI-HSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK10247 79 --YRQQVSYCAQTPTLFgDT--VYDNLIFPWQI--RNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 161 ITKPEILLADEPTGALDSKSSAALLDVFDAINASGQ-TILMVTHSTAAASRAQRVL 215
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNiAVLWVTHDKDEINHADKVI 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-220 |
2.59e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYktRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKS-TLLNILAMLDKP----TAGRVYLNGMDTAT 75
Cdd:PRK15134 3 QPLLAIENLSVAF--RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 76 IKNKDASSFRRERLGFVFQD----FNLLDTLSVKdnilLPLVLS-RRPLKQMMTQVEAIS--RQLGIH---SLLEKYPYE 145
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEpmvsLNPLHTLEKQ----LYEVLSlHRGMRREAARGEILNclDRVGIRqaaKRLTDYPHQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 146 ISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-203 |
2.91e-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: 97.95 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKTRFKGnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDT---ATIKNK 79
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRG-VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEwvdMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 80 DASSFRRERLGFVFQDFNLLDTLSVKDNIL------LPLVLSRRplKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQR 153
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNLTeaigleLPDELARM--KAVITLKMVGFDEEKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 154 VAVARAIITKPEILLADEPTGALDSKSSAALLD-VFDAINASGQTILMVTH 203
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSH 486
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-185 |
8.40e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTL-LNILAMLdkPTAGRVYLNGMDTATIKNKDASSFRReRLGFVFQDFN--LLD 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 101 TLSVKDNILLPLVLSRRPL--KQMMTQVEAISRQLGIH-SLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK15134 378 RLNVLQIIEEGLRVHQPTLsaAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
....*...
gi 1092440915 178 SKSSAALL 185
Cdd:PRK15134 458 KTVQAQIL 465
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-177 |
1.43e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.39 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVK-----KIYKTRF--KGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAT 75
Cdd:PRK15079 8 LLEVADLKvhfdiKDGKQWFwqPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 76 IKNKDASSFRRErLGFVFQD--FNLLDTLSVKDNILLPLV-----LSRRPLKQmmtQVEAISRQLGI-HSLLEKYPYEIS 147
Cdd:PRK15079 88 MKDDEWRAVRSD-IQMIFQDplASLNPRMTIGEIIAEPLRtyhpkLSRQEVKD---RVKAMMLKVGLlPNLINRYPHEFS 163
|
170 180 190
....*....|....*....|....*....|
gi 1092440915 148 GGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-203 |
3.27e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.17 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTrfkgnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtATIKNKD 80
Cdd:PRK13652 1 MHLIETRDLCYSYSG-----SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG---EPITKEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASSFRReRLGFVFQ--DFNLLDTLSVKDNILLP--LVLSRRPLKQmmtQVEAISRQLGIHSLLEKYPYEISGGQKQRVAV 156
Cdd:PRK13652 73 IREVRK-FVGLVFQnpDDQIFSPTVEQDIAFGPinLGLDEETVAH---RVSSALHMLGLEELRDRVPHHLSGGEKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1092440915 157 ARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTH 203
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTH 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-220 |
3.54e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.27 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIY---KTRFKgnqveALKDIHFTVDKGDYVAIMGESGSGKS-TLLNILAMLDKP---TAGRVYLNGMDT 73
Cdd:PRK11022 1 MALLNVDKLSVHFgdeSAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 74 ATIKNKDassfRRERLG----FVFQD------------FNLLDTLSVKDNillplvLSRRPLKQ----MMTQVeaisrql 133
Cdd:PRK11022 76 QRISEKE----RRNLVGaevaMIFQDpmtslnpcytvgFQIMEAIKVHQG------GNKKTRRQraidLLNQV------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 134 GI---HSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQ-TILMVTHSTA-AA 208
Cdd:PRK11022 139 GIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLAlVA 218
|
250
....*....|..
gi 1092440915 209 SRAQRVLFIKDG 220
Cdd:PRK11022 219 EAAHKIIVMYAG 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-220 |
3.61e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.46 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 18 KGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtATIKNKDASSFRReRLGFVFQD-F 96
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRR-KIGMVFQNpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 NLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGAL 176
Cdd:PRK13642 92 NQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092440915 177 DSKSSAALLDVFDAINASGQ-TILMVTHSTAAASRAQRVLFIKDG 220
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAG 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-220 |
2.16e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkGNQVeALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATiknkdASS 83
Cdd:PRK13537 8 IDFRNVEKRY-----GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-----RAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFVFQDFNLLDTLSVKDNILL---PLVLSRRPLKQMMTQVEAISRqlgIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLLVfgrYFGLSAAAARALVPPLLEFAK---LENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 161 ITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEG 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-173 |
2.45e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 89.12 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATiknkdASS 83
Cdd:TIGR03410 1 LEVSNLNVYY------GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK-----LPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRER--LGFVFQDFNLLDTLSVKDNILLplVLSRRP----------------LKQMMtqveaiSRQLGihsllekypyE 145
Cdd:TIGR03410 70 HERARagIAYVPQGREIFPRLTVEENLLT--GLAALPrrsrkipdeiyelfpvLKEML------GRRGG----------D 131
|
170 180
....*....|....*....|....*...
gi 1092440915 146 ISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:TIGR03410 132 LSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-204 |
2.49e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 20 NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiKNKDASSFRrERLGFV-FQDFnL 98
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVA-EACHYLgHRNA-M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 99 LDTLSVKDNillpLVLSRRPLKQMMTQVEAISRQLGIHSLLE-KYPYeISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK13539 85 KPALTVAEN----LEFWAAFLGGEELDIAAALEAVGLAPLAHlPFGY-LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*..
gi 1092440915 178 SKSSAALLDVFDAINASGQTILMVTHS 204
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-203 |
4.25e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.05 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 27 DIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRReRLGFVFQDFNLLDTLSVKD 106
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 107 NILLPLVLSRR---PLKQ--MMTQVEAIsrqlGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSS 181
Cdd:PRK11831 104 NVAYPLREHTQlpaPLLHstVMMKLEAV----GLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180
....*....|....*....|...
gi 1092440915 182 AALLDVFDAIN-ASGQTILMVTH 203
Cdd:PRK11831 180 GVLVKLISELNsALGVTCVVVSH 202
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-220 |
6.68e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 6.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 9 VKKIYKtRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASsfrrER 88
Cdd:COG4604 4 IKNVSK-RYGGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 89 LGFVFQDFNLLDTLSVKDnillpLVL------SR-RPLKQMMTQV-EAIsRQLGIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG4604 77 LAILRQENHINSRLTVRE-----LVAfgrfpySKgRLTAEDREIIdEAI-AYLDLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 161 ITKPEILLADEPTGALDSKSSAALLDVF-DAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLrRLADELGKTVVIVLHDINFASCyADHIVAMKDG 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-223 |
1.22e-20 |
|
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: 90.84 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATikNKDASsfrRERLGFVFQDFNLLDTLS 103
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--NLDAV---RQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 VKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAA 183
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092440915 184 LLDVFDAINaSGQTILMVTHSTAAAS-RAQRVLFIKDGILY 223
Cdd:TIGR01257 1100 IWDLLLKYR-SGRTIIMSTHHMDEADlLGDRIAIISQGRLY 1139
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-217 |
1.41e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.47 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 5 DVQHVKKIYKTRFKG--------NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNgmDTATI 76
Cdd:PTZ00265 373 DGKKLKDIKKIQFKNvrfhydtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 77 KNKDAsSFRRERLGFVFQDfNLLDTLSVKDNILLPLvLSRRPLKQMMTQVE----------------------------- 127
Cdd:PTZ00265 451 KDINL-KWWRSKIGVVSQD-PLLFSNSIKNNIKYSL-YSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndmsn 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 128 -----------------------AISRQLGIHSLLEKYP--YE---------ISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:PTZ00265 528 ttdsneliemrknyqtikdsevvDVSKKVLIHDFVSALPdkYEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEAT 607
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1092440915 174 GALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFI 217
Cdd:PTZ00265 608 SSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFV 651
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-230 |
2.39e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKiyktRFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNgmdtATIKnkda 81
Cdd:COG0488 314 KVLELEGLSK----SYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETVK---- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 ssfrrerLGFVFQDFNLLD-TLSVKDNIllplvlsrRPLKQMMTQVEAISRqLGihSLL------EKYPYEISGGQKQRV 154
Cdd:COG0488 380 -------IGYFDQHQEELDpDKTVLDEL--------RDGAPGGTEQEVRGY-LG--RFLfsgddaFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 155 AVARAIITKPEILLADEPTGALDSKSSAALLdvfDAINA-SGqTILMVTHSTAAASR-AQRVLFIKDGILYNqiFKGD 230
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALE---EALDDfPG-TVLLVSHDRYFLDRvATRILEFEDGGVRE--YPGG 513
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-220 |
2.84e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.48 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 17 FKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLD--KPTAGRVYLN-----------------------GM 71
Cdd:TIGR03269 10 FDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverpskvgepcpvcGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 72 DTATIK----NKDASSFR--RERLGFVFQ-DFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPY 144
Cdd:TIGR03269 88 TLEPEEvdfwNLSDKLRRriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 145 EISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVF-DAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-203 |
4.93e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 12 IYKTrFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSfrrERLGF 91
Cdd:PRK11288 10 IGKT-FPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA---AGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 92 VFQDFNLLDTLSVKDNILLPLVLSRRPL---KQMMTQVEAISRQLGIH---SLLEKYpyeISGGQKQRVAVARAIITKPE 165
Cdd:PRK11288 84 IYQELHLVPEMTVAENLYLGQLPHKGGIvnrRLLNYEAREQLEHLGVDidpDTPLKY---LSIGQRQMVEIAKALARNAR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-210 |
5.00e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.37 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDK--PTA---GRVYLNGMDTATiKNKDASSFRReRLGFVFQDFNL 98
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYA-PDVDPVEVRR-RIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 99 LDTlSVKDNILL-PLV---------LSRRPLKQ--MMTQVEAISRQLGIhsllekypyEISGGQKQRVAVARAIITKPEI 166
Cdd:PRK14243 103 FPK-SIYDNIAYgARIngykgdmdeLVERSLRQaaLWDEVKDKLKQSGL---------SLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092440915 167 LLADEPTGALDSKSSaalLDVFDAINASGQ--TILMVTHSTAAASR 210
Cdd:PRK14243 173 ILMDEPCSALDPIST---LRIEELMHELKEqyTIIIVTHNMQQAAR 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-210 |
6.32e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYktrfkGNQVeALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtiknkD 80
Cdd:PRK13536 39 TVAIDLAGVSKSY-----GDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-----A 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASSFRRERLGFVFQDFNLLDTLSVKDNILlplVLSRRpLKQMMTQVEAIsrqlgIHSLLEKYPYE---------ISGGQK 151
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENLL---VFGRY-FGMSTREIEAV-----IPSLLEFARLEskadarvsdLSGGMK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 152 QRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR 210
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAER 237
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-220 |
6.79e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.55 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFR-----RERLGFVFqdfnll 99
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSLAFPF------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 dtlSVKDNILL---PLVLSRRPLKQMMTQVEAisrQLGIHSLLEK-YPyEISGGQKQRVAVARAII-------TKPEILL 168
Cdd:COG4559 91 ---TVEEVVALgraPHGSSAAQDRQIVREALA---LVGLAHLAGRsYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 169 ADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:COG4559 164 LDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQG 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-225 |
1.53e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 39 AIMGESGSGKSTLLNILAMLDKPTAGRVYLNGM---DTATIKNKDASSFRReRLGFVFQDFNLLdTLSVKDNILLPLVLS 115
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllgGRSIFNYRDVLEFRR-RVGMLFQRPNPF-PMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 116 RR-PLKQMMTQVEAISRQLG----IHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDA 190
Cdd:PRK14271 129 KLvPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 1092440915 191 InASGQTILMVTHSTAAASR-AQRVLFIKDGILYNQ 225
Cdd:PRK14271 209 L-ADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEE 243
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-203 |
1.59e-19 |
|
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: 83.31 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 30 FTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNkdasSFRRERLGFVFQDfNLLDTLSVKDNIL 109
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD----SIARGLLYLGHAP-GIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 110 LPLVLSRRplkqmmTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFD 189
Cdd:cd03231 96 FWHADHSD------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....
gi 1092440915 190 AINASGQTILMVTH 203
Cdd:cd03231 170 GHCARGGMVVLTTH 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-220 |
1.76e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKS-TLLNILAMLDKpTAGRVYLNGM-------DTATIKNKDASSFRRER---L 89
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrQVIELSEQSAAQMRHVRgadM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 90 GFVFQD----FNLLDTL--SVKDNILLPLVLSR----RPLKQMMTQVeaisRQLGIHSLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK10261 107 AMIFQEpmtsLNPVFTVgeQIAESIRLHQGASReeamVEAKRMLDQV----RIPEAQTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 160 IITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTA-AASRAQRVLFIKDG 220
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGvVAEIADRVLVMYQG 245
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-220 |
1.83e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 87.10 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRRErLGFVFQDFNLLDTl 102
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS---LKDIDRHTLRQF-INYLPQEPYIFSG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNILLPlvlSRRPLKQ-MMTQVEAISR--------QLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:TIGR01193 563 SILENLLLG---AKENVSQdEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092440915 174 GALDSKSSAALLDvfDAINASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:TIGR01193 640 SNLDTITEKKIVN--NLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHG 684
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-222 |
2.42e-19 |
|
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: 83.31 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 13 YKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLN-ILAMLDkPTAGRVYLNGMDTATIKNKDAssfrRERLGF 91
Cdd:cd03244 8 VSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVE-LSSGSILIDGVDISKIGLHDL----RSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 92 VFQD---------FNlLDTLSVKDNILLPLVLSRRPLKQMmtqVEAISRQLGihSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:cd03244 83 IPQDpvlfsgtirSN-LDPFGEYSDEELWQALERVGLKEF---VESLPGGLD--TVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAiNASGQTILMVTH--STAAASraQRVLFIKDGIL 222
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHrlDTIIDS--DRILVLDKGRV 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-220 |
2.68e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 14 KTRFkgnQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDT-ATIKN-KDASSFRRErLGF 91
Cdd:PRK13645 19 KTPF---EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRKE-IGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 92 VFQ--DFNLLDTLSVKDNILLPLVLSRRplKQMMTQveAISRQLGIHSLLEKY----PYEISGGQKQRVAVARAIITKPE 165
Cdd:PRK13645 95 VFQfpEYQLFQETIEKDIAFGPVNLGEN--KQEAYK--KVPELLKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRiADEVIVMHEG 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-202 |
3.69e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtATIKNKDASSFRRERLGFVFQD---FNLL 99
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSPRDAIRAGIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 DTLSVKDNILLPLV--LSRRPL---KQMMTQVEAISRQLGIhslleKYPY------EISGGQKQRVAVARAIITKPEILL 168
Cdd:COG1129 343 LDLSIRENITLASLdrLSRGGLldrRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092440915 169 ADEPT-----GAldsKSsaallDVFDAIN---ASGQTILMVT 202
Cdd:COG1129 418 LDEPTrgidvGA---KA-----EIYRLIRelaAEGKAVIVIS 451
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-225 |
4.21e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFrRERLGFVFQD 95
Cdd:PRK11160 347 TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP---IADYSEAAL-RQAISVVSQR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 FNLL-DTLsvKDNILLPL-VLSRRPLKQMMTQVeaisrqlGIHSLLEKYP----------YEISGGQKQRVAVARAIITK 163
Cdd:PRK11160 423 VHLFsATL--RDNLLLAApNASDEALIEVLQQV-------GLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAInASGQTILMVTHSTAAASRAQRVLFIKDGILYNQ 225
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-220 |
4.44e-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: 82.46 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 13 YKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAssfrRERLGFV 92
Cdd:cd03369 12 LSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL----RSSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 93 FQDFNLLDTlSVKDNIllpLVLSRRPLKQMMtqvEAISRQLGIHSLlekypyeiSGGQKQRVAVARAIITKPEILLADEP 172
Cdd:cd03369 88 PQDPTLFSG-TIRSNL---DPFDEYSDEEIY---GALRVSEGGLNL--------SQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1092440915 173 TGALDSKSSAALLDVFDAiNASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03369 153 TASIDYATDALIQKTIRE-EFTNSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-225 |
5.27e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.21 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKStlLNILAMLD------KPTAGRVYLNGMDTAtiknkdASSFRRERLGFVFQ 94
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVA------PCALRGRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 95 D----FNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQlGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLAD 170
Cdd:PRK10418 87 NprsaFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLE-NAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 171 EPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIKDGILYNQ 225
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-214 |
5.75e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASSFRRErLGFVFQD-FNLL 99
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 DT-LSVKDNILLPLVLSRrplkqmMTQVEAISRQlgIHSLLEK----------YPYEISGGQKQRVAVARAIITKPEILL 168
Cdd:PRK10261 415 DPrQTVGDSIMEPLRVHG------LLPGKAAAAR--VAWLLERvgllpehawrYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1092440915 169 ADEPTGALDSKSSAALLDV-FDAINASGQTILMVTHSTAAASR-AQRV 214
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLlLDLQRDFGIAYLFISHDMAVVERiSHRV 534
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-220 |
5.81e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 15 TRFKGNQVE-------ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASsfrrE 87
Cdd:PRK10253 6 ARLRGEQLTlgygkytVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 88 RLGFVFQDFNLLDTLSVKDNIllplVLSRRPLKQMMTQ--------VEAISRQLGIHSLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK10253 82 RIGLLAQNATTPGDITVQELV----ARGRYPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 160 IITKPEILLADEPTGALDSKSSAALLDVFDAIN-ASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRyASHLIALREG 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-220 |
8.11e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNgmdtatiknkdassfRRERLGFVFQDFNL-LDTLs 103
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP---------------AGARVLFLPQRPYLpLGTL- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 vKDNILLPLVLSRRPLkqmmTQVEAISRQLGIHSLLEKY------PYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:COG4178 443 -REALLYPATAEAFSD----AELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092440915 178 SKSSAALLDVFDAINASGqTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:COG4178 518 EENEAALYQLLREELPGT-TVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-220 |
1.18e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 17 FKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRrERLGFVFQDF 96
Cdd:PRK11176 351 YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLR-NQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 NLL-DTlsVKDNILLPL--VLSRRPLKQ---MMTQVEAISR-QLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLA 169
Cdd:PRK11176 427 HLFnDT--IANNIAYARteQYSREQIEEaarMAYAMDFINKmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 170 DEPTGALDSKSSAALLDVFDAINASgQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDG 554
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-220 |
1.69e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknKDASSFRRE----RLGF 91
Cdd:PRK13548 11 RLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG--------RPLADWSPAelarRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 92 VFQDFNLLDTLSVKDNI---LLPLVLSRRPLKQMmtqVEAISRQLGIHSLLEK-YPyEISGGQKQRVAVARAI--ITKPE 165
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVamgRAPHGLSRAEDDAL---VAAALAQVDLAHLAGRdYP-QLSGGEQQRVQLARVLaqLWEPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 166 ----ILLADEPTGALDSKSSAALLD-VFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK13548 157 gpprWLLLDEPTSALDLAHQHHVLRlARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQG 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-203 |
1.72e-18 |
|
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: 80.48 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdassfRRERLGFVFQDFNLLDTL 102
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNillpLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSA 182
Cdd:TIGR01189 89 SALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 1092440915 183 ALLDVFDAINASGQTILMVTH 203
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-223 |
2.68e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.44 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 5 DVQHVKKIYKTR-----FKGN----------QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLN 69
Cdd:COG4586 3 EVENLSKTYRVYekepgLKGAlkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 70 GMDtatiKNKDASSFRReRLGFVF-------QDFNLLDTLSvkdniLLPLV--LSRRPLKQmmtQVEAISRQLGIHSLLE 140
Cdd:COG4586 83 GYV----PFKRRKEFAR-RIGVVFgqrsqlwWDLPAIDSFR-----LLKAIyrIPDAEYKK---RLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 141 KYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINAS-GQTILMVTHSTAAASR-AQRVLFIK 218
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEAlCDRVIVID 229
|
....*.
gi 1092440915 219 DG-ILY 223
Cdd:COG4586 230 HGrIIY 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-219 |
3.03e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.12 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNgmdtatiknkdassfRRERLGFvfqdfnlldtlsv 104
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------------EGEDLLF------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 kdnillplvLSRRPLkqmMTQV---EAISrqlgihsllekYPY--EISGGQKQRVAVARAIITKPEILLADEPTGALDSK 179
Cdd:cd03223 69 ---------LPQRPY---LPLGtlrEQLI-----------YPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092440915 180 SSAALLDVfdaINASGQTILMVTHSTAAASRAQRVLFIKD 219
Cdd:cd03223 126 SEDRLYQL---LKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-220 |
3.93e-18 |
|
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: 78.26 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 8 HVKKIYKTrFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVylngmdtatiknkdaSSFRRE 87
Cdd:cd03221 2 ELENLSKT-YGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------TWGSTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 88 RLGFVfqdfnlldtlsvkdnillplvlsrrplkqmmtqveaisRQLgihsllekypyeiSGGQKQRVAVARAIITKPEIL 167
Cdd:cd03221 64 KIGYF--------------------------------------EQL-------------SGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 168 LADEPTGALDSKSSAALLdvfDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:cd03221 93 LLDEPTNHLDLESIEALE---EALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-210 |
4.18e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASsfrrERLGFVFQDFNLLDTLSV 104
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDnillpLV-LSRRP---LKQMMTQ-----VEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGA 175
Cdd:PRK11231 94 RE-----LVaYGRSPwlsLWGRLSAednarVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1092440915 176 LDSKSSAALLDVFDAINASGQTILMVTHSTAAASR 210
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQGKTVVTVLHDLNQASR 203
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-173 |
5.42e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 80.16 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDasSFRRERLGFV--FQDFNLLDT 101
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTD---LTGLD--EHEIARLGIGrkFQKPTVFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNILLPL--------VLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:COG4674 100 LTVFENLELALkgdrgvfaSLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-215 |
1.01e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.38 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAML-DKPTAGRVYLNGMDTATIKN---- 78
Cdd:PTZ00265 1166 IEIMDVNFRYISR---PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNeqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 79 ----------KDASSFRRERLGFVFQD---FN-----LLDTLSVKDNILLPL-----VLSRRPLKQMMTQVEAIsrQLG- 134
Cdd:PTZ00265 1243 qgdeeqnvgmKNVNEFSLTKEGGSGEDstvFKnsgkiLLDGVDICDYNLKDLrnlfsIVSQEPMLFNMSIYENI--KFGk 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 135 --------------------IHSLLEKY-----PY--EISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAAL-LD 186
Cdd:PTZ00265 1321 edatredvkrackfaaidefIESLPNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIeKT 1400
|
250 260
....*....|....*....|....*....
gi 1092440915 187 VFDAINASGQTILMVTHSTAAASRAQRVL 215
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-203 |
1.26e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.85 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 35 GDYVAIMGESGSGKSTLLNILAmldkptaGRVYLNGMD-TATIKNKDASSFRRERLGFVFQDFNLLDTLSVKDNILLP-- 111
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALA-------GRIQGNNFTgTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 112 LVLSRRPLKQMMTQV-EAISRQLGIHS-----LLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALL 185
Cdd:PLN03211 167 LRLPKSLTKQEKILVaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170
....*....|....*...
gi 1092440915 186 DVFDAINASGQTILMVTH 203
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMH 264
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-203 |
1.58e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGrvylngmdtaTIKNKDASsfrreRLGFVFQDFNLLDTLsv 104
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKL-----RIGYVPQKLYLDTTL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 kdnillPLVLSR----RPLKQMMTQVEAISRQLGIHsLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKS 180
Cdd:PRK09544 83 ------PLTVNRflrlRPGTKKEDILPALKRVQAGH-LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....
gi 1092440915 181 SAALLDVFDAI-NASGQTILMVTH 203
Cdd:PRK09544 156 QVALYDLIDQLrRELDCAVLMVSH 179
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-203 |
2.10e-17 |
|
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: 81.13 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 7 QHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLngMDTATIknkdassfrr 86
Cdd:TIGR03719 8 NRVSKVV-----PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QPGIKV---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 erlGFVFQDFNLLDTLSVKDNILLPLvlsrRPLKQMMTQVEAISRQLG-----IHSLLEKY------------------- 142
Cdd:TIGR03719 71 ---GYLPQEPQLDPTKTVRENVEEGV----AEIKDALDRFNEISAKYAepdadFDKLAAEQaelqeiidaadawdldsql 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 143 ----------PYE-----ISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAAL---LDVFDAinasgqTILMVTH 203
Cdd:TIGR03719 144 eiamdalrcpPWDadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLerhLQEYPG------TVVAVTH 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-201 |
2.10e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVkkiykTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDA 81
Cdd:COG3845 256 VVLEVENL-----SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED---ITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 SSFRRERLGFVFQD---FNLLDTLSVKDNILLPLV----LSRRPL---KQMMTQVEAISRQLGI---------HSLleky 142
Cdd:COG3845 328 RERRRLGVAYIPEDrlgRGLVPDMSVAENLILGRYrrppFSRGGFldrKAIRAFAEELIEEFDVrtpgpdtpaRSL---- 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 143 pyeiSGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMV 201
Cdd:COG3845 404 ----SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-203 |
2.43e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKiyktRFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAs 82
Cdd:PRK15439 11 LLCARSISK----QYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 sfrrERLG--FVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMmtqvEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK15439 84 ----HQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQKM----KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092440915 161 ITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-220 |
2.84e-17 |
|
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: 77.28 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 13 YKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAmlDKPTAGRV----YLNGmdtatIKNKDasSFRReR 88
Cdd:cd03232 11 YTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVItgeiLING-----RPLDK--NFQR-S 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 89 LGFVFQDFNLLDTLSVKDNILLPLVLsrrplkqmmtqveaisRQLGIhsllekypyeisgGQKQRVAVARAIITKPEILL 168
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALL----------------RGLSV-------------EQRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 169 ADEPTGALDSKSSAALLDVFDAINASGQTILMVTH--STAAASRAQRVLFIKDG 220
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-215 |
3.59e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 27 DIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTatikNKDASSFRRerlgfvfqdfNLL------- 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQ----------DLLylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 --DTLSVKDN--ILLPL--VLSRRPLKQMMTQV------EAISRQLgihsllekypyeiSGGQKQRVAVARAIITKPEIL 167
Cdd:PRK13538 85 ikTELTALENlrFYQRLhgPGDDEALWEALAQVglagfeDVPVRQL-------------SAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092440915 168 LADEPTGALDSKSSAALLDVFDAINASGQTILMVTHST-AAASRAQRVL 215
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDlPVASDKVRKL 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-251 |
4.44e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.15 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKtrfKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNkdasS 83
Cdd:PRK10790 341 IDIDNVSFAYR---DDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH----S 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRRERLGFVFQDFNLLDTlSVKDNILLPLVLSRRPLKQMMTQVE--AISRQL--GIHSLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK10790 412 VLRQGVAMVQQDPVVLAD-TFLANVTLGRDISEEQVWQALETVQlaELARSLpdGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 160 IITKPEILLADEPTGALDSKSSAALLDVFDAINAsgQTILMV-THSTAAASRAQRVLFIKDGIL-----YNQIFKGDKSE 233
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVViAHRLSTIVEADTILVLHRGQAveqgtHQQLLAAQGRY 568
|
250 260
....*....|....*....|
gi 1092440915 234 HQMF--QEISDTLTAMASEV 251
Cdd:PRK10790 569 WQMYqlQLAGEELAASVREE 588
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-220 |
9.35e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 79.38 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 13 YKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAmlDKPTAGrvYLNGMDTATIKNKDASSFRReRLGFV 92
Cdd:TIGR00956 767 YEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG--VITGGDRLVNGRPLDSSFQR-SIGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 93 FQDFNLLDTLSVKDNILLPLVLsRRP----LKQMMTQVEAISRQLGihslLEKYPYEISG--------GQKQRVAVARAI 160
Cdd:TIGR00956 842 QQQDLHLPTSTVRESLRFSAYL-RQPksvsKSEKMEYVEEVIKLLE----MESYADAVVGvpgeglnvEQRKRLTIGVEL 916
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 161 ITKPEILL-ADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQ--RVLFIKDG 220
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-240 |
1.12e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 76.28 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTAtikNKDASS 83
Cdd:TIGR03740 1 LETKNLSKRFGKQ------TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDLHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frrerLGFVFQDFNLLDTLSVKDNILLPLVLSRRPlkqmMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITK 163
Cdd:TIGR03740 72 -----IGSLIESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNH 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGIL-YNQIFKGDKSEHQMFQEI 240
Cdd:TIGR03740 143 PKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQlADHIGIISEGVLgYQGKINKSENLEKLFVEV 221
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-203 |
1.57e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.64 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTRfKGNqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKP----TAGRVYLNGMDTATI 76
Cdd:COG4170 1 MPLLDIRNLTIEIDTP-QGR-VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 77 KNKDassfRRERLG----FVFQDfnlldTLSVKDnillplvlsrrPLKQMMTQ-VEAI-SRQLGIH-------------S 137
Cdd:COG4170 79 SPRE----RRKIIGreiaMIFQE-----PSSCLD-----------PSAKIGDQlIEAIpSWTFKGKwwqrfkwrkkraiE 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 138 LLEK------------YPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTH 203
Cdd:COG4170 139 LLHRvgikdhkdimnsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISH 217
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-225 |
2.22e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.03 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILA-MLdkPTAGRVYLNGMDTATIKNKDASSFR-----RERLGFVFQDFNL 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAgLL--PGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 99 LdTLSVKDNILLPLVLSRrplkqmmtqVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAII-TKPEI------LLADE 171
Cdd:COG4138 90 L-ALHQPAGASSEAVEQL---------LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 172 PTGALDSKSSAALLDVFDAINASGQTILMVTHS-TAAASRAQRVLFIKDGILYNQ 225
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKLVAS 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-203 |
2.30e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIknkdaSSFRRERLGFV--F 93
Cdd:PRK11300 14 RFGG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-----PGHQIARMGVVrtF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 94 QDFNLLDTLSVKDNIllpLVLSRRPLKQMM------------TQVEAISR------QLGIHSLLEKYPYEISGGQKQRVA 155
Cdd:PRK11300 87 QHVRLFREMTVIENL---LVAQHQQLKTGLfsgllktpafrrAESEALDRaatwleRVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092440915 156 VARAIITKPEILLADEPTGALDSKSSAALLDVFDAI-NASGQTILMVTH 203
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEH 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-220 |
2.95e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.56 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYktrfkgNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLdKPTA---GRVYLNGmdtATIKNK 79
Cdd:TIGR02633 1 LLEMKGIVKTF------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSG---SPLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 80 DASSFRRERLGFVFQDFNLLDTLSVKDNILLPLVLS----RRPLKQMMTQVEAISRQLGIHSLLEKYPY-EISGGQKQRV 154
Cdd:TIGR02633 71 NIRDTERAGIVIIHQELTLVPELSVAENIFLGNEITlpggRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 155 AVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHS-TAAASRAQRVLFIKDG 220
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDG 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-220 |
3.67e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 74.67 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 19 GNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLniLAMLD--KPTAGRVYLNGMDTATIKNKDASSFRRERLGFVFQDF 96
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGemQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 NLLDTlSVKDNILLPLVLSRRPLKQMmtqVEAISRQLGIHSLLEKYPYEI-------SGGQKQRVAVARAIITKPEILLA 169
Cdd:cd03290 89 WLLNA-TVEENITFGSPFNKQRYKAV---TDACSLQPDIDLLPFGDQTEIgerginlSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 170 DEPTGALDSKSSAALLD--VFDAINASGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-210 |
4.26e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.80 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 22 VEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASsfrrERLGFVFQDFNLLDT 101
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNILLPLVLSRRPLKQM----MTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK09536 92 FDVRQVVEMGRTPHRSRFDTWtetdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190
....*....|....*....|....*....|...
gi 1092440915 178 SKSSAALLDVFDAINASGQTILMVTHSTAAASR 210
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAIHDLDLAAR 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-218 |
4.47e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDK--PTAGRVYLNGMDtatIKNKDASsfrrER----LGFVFQD--- 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGED---ILELSPD----ERaragIFLAFQYpve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 ------FNLLDTlsVKDNILLPLVlsrrPLKQMMTQVEAISRQLGI-HSLLEKYPYE-ISGGQKQRVAVARAIITKPEIL 167
Cdd:COG0396 89 ipgvsvSNFLRT--ALNARRGEEL----SAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 168 LADEPTGALDsksSAALLDVFDAINA---SGQTILMVTHStaaasraQRVL-FIK 218
Cdd:COG0396 163 ILDETDSGLD---IDALRIVAEGVNKlrsPDRGILIITHY-------QRILdYIK 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-209 |
4.62e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDT--ATIKNKDASSFRRERLGFVFqdfnlldT 101
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrqALQKNLVAYVPQSEEVDWSF-------P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNILLP----LVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK15056 95 VLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190
....*....|....*....|....*....|..
gi 1092440915 178 SKSSAALLDVFDAINASGQTILMVTHSTAAAS 209
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVT 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-204 |
7.94e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTRfkgnqvEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKD 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGR------RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 81 ASsfrRERLGFVFQDFNLLDTLSVKDNILLPLVLsRRPL--KQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVAR 158
Cdd:PRK10895 75 RA---RRGIGYLPQEASIFRRLSVYDNLMAVLQI-RDDLsaEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092440915 159 AIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHS 204
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-203 |
8.84e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 8.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKiyktRFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAmldkptagRVYLNGMDTATI---- 76
Cdd:PRK13549 3 EYLLEMKNITK----TFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS--------GVYPHGTYEGEIifeg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 77 KNKDASSFR-RERLGFV--FQDFNLLDTLSVKDNILL---PLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQ 150
Cdd:PRK13549 69 EELQASNIRdTERAGIAiiHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 151 KQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-220 |
9.36e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 9.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAssfrRERLGFVFQD 95
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 -FNLLDTlsVKDNILLPlvlsrRPlKQMMTQVEAISRQLGIHS----LLEKYPYEI-------SGGQKQRVAVARAIITK 163
Cdd:PRK10789 398 pFLFSDT--VANNIALG-----RP-DATQQEIEHVARLASVHDdilrLPQGYDTEVgergvmlSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDvfdaiNAS----GQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILH-----NLRqwgeGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-220 |
1.11e-15 |
|
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: 72.94 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 20 NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILA--MLDKPTAGRVYLNGMDTatiknKDASSFRRERLGfVFQDFn 97
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDI-----TDLPPEERARLG-IFLAF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 98 lldtlsvkdnillplvlsrrplkQMMTQVEAISRQLGIHSLLEKYpyeiSGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:cd03217 84 -----------------------QYPPEIPGVKNADFLRYVNEGF----SGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092440915 178 SKSSAALLDVFDAINASGQTILMVTH--STAAASRAQRVLFIKDG 220
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDG 181
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-203 |
2.69e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVKKiyktRFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTaTIKNKDA 81
Cdd:PRK10762 3 ALLQLKGIDK----AFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 SsfRRERLGFVFQDFNLLDTLSVKDNILlplvLSRRPL--------KQMMTQVEAISRQLGI----HSLLEkypyEISGG 149
Cdd:PRK10762 76 S--QEAGIGIIHQELNLIPQLTIAENIF----LGREFVnrfgridwKKMYAEADKLLARLNLrfssDKLVG----ELSIG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 150 QKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-232 |
5.13e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 11 KIYKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDK-----PTAGRVYLNGMDTATiKNKDASSFR 85
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYE-RRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 86 RErLGFVFQDFNLLdTLSVKDNILLPL-VLSRRPLKQMMTQVEAISRQLG----IHSLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK14258 88 RQ-VSMVHPKPNLF-PMSVYDNVAYGVkIVGWRPKLEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 161 ITKPEILLADEPTGALDSKSSAALLDVFDAINASGQ-TILMVTHSTAAASRaqrvlfIKDgilYNQIFKGDKS 232
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSR------LSD---FTAFFKGNEN 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-211 |
5.37e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.13 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTatikNKDASSFRRErLGFVFQDFNLLDTLSV 104
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQ-LCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDNILLPLVLSRRPLkqmmtQVEAISRQLGIHSLLEkYPYEI-SGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAA 183
Cdd:PRK13540 92 RENCLYDIHFSPGAV-----GITELCRLFSLEHLID-YPCGLlSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*...
gi 1092440915 184 LLDVFDAINASGQTILMVTHSTAAASRA 211
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNKA 193
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-220 |
8.78e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.45 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 21 QVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDtatIKNKDASSFRRERLGFVFQDFNLLD 100
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 101 TLSVKDNILLPLVLSRRPLKQmmtqvEAISRQLGIHSLLEKYPYE----ISGGQKQRVAVARAIITKPEILLADEPTGAL 176
Cdd:PRK11614 94 RMTVEENLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092440915 177 DSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENG 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-233 |
1.62e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 71.29 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYktrfkGNQVeALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiKNKDASS 83
Cdd:COG4152 2 LELKGLTKRF-----GDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG------EPLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 FRR------ERlGfvfqdfnLLDTLSVKDNILLplvLSRrpLKQMmTQVEAISRqlgIHSLLEK-----YPY----EISG 148
Cdd:COG4152 70 RRRigylpeER-G-------LYPKMKVGEQLVY---LAR--LKGL-SKAEAKRR---ADEWLERlglgdRANkkveELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 149 GQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGilyNQIF 227
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKG---RKVL 209
|
....*.
gi 1092440915 228 KGDKSE 233
Cdd:COG4152 210 SGSVDE 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-202 |
9.98e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 2 TLLDVQHVkkiykTRFKGNQVealKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDA 81
Cdd:PRK09700 264 TVFEVRNV-----TSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 82 --------SSFRRERlGFvFQDFNLLDTLSVKDNI-------LLPLVLSRRPLKQMMTQVEAISrqLGIHSLlEKYPYEI 146
Cdd:PRK09700 336 vkkgmayiTESRRDN-GF-FPNFSIAQNMAISRSLkdggykgAMGLFHEVDEQRTAENQRELLA--LKCHSV-NQNITEL 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 147 SGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVT 202
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-203 |
1.75e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 7 QHVKKIYktrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLngMDTATIknkdassfrr 86
Cdd:PRK11819 10 NRVSKVV-----PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGIKV---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 erlGFVFQDFNLLDTLSVKDNILLPLvlsrRPLKQMMTQVEAISRQLG---------------------------IHSLL 139
Cdd:PRK11819 73 ---GYLPQEPQLDPEKTVRENVEEGV----AEVKAALDRFNEIYAAYAepdadfdalaaeqgelqeiidaadawdLDSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 140 EKY-------PYE-----ISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAAL---LDVFdainaSGqTILMVTH 203
Cdd:PRK11819 146 EIAmdalrcpPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLeqfLHDY-----PG-TVVAVTH 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-220 |
2.00e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 10 KKIYKTrFKGnqVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLdKPTA---GRVYLNGmDTATIKNKDASsfrr 86
Cdd:NF040905 5 RGITKT-FPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDG-EVCRFKDIRDS---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 ERLGFVF--QDFNLLDTLSVKDNILLPLVLSRRPL---KQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAII 161
Cdd:NF040905 76 EALGIVIihQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 162 TKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDG 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-225 |
2.18e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 30 FTVDKGDYVAIMGESGSGKSTLLNILAMLdKPTAGRVYLNGMDTATIknkDASSFRRERLGFVFQD--------FNLLdT 101
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAW---SAAELARHRAYLSQQQtppfampvFQYL-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNillplvlsrRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAII-TKPEI------LLADEPTG 174
Cdd:PRK03695 92 LHQPDK---------TRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqVWPDInpagqlLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 175 ALDSKSSAALLDVFDAINASGQTILMVTHS-TAAASRAQRVLFIKDGILYNQ 225
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLLAS 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-208 |
3.50e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.41 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 17 FKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknKDASSFRRER-------L 89
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG--------KTATRGDRSRfmaylghL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 90 GFVFQDFNLLDTLSvkdniLLPLVLSRRPlKQMMTQVEAIsrqLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLA 169
Cdd:PRK13543 91 PGLKADLSTLENLH-----FLCGLHGRRA-KQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092440915 170 DEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAA 208
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAA 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-177 |
4.03e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.78 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 19 GNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLdKPTAGRVYLNGM--DTATIKNkdassfRRERLGFVFQDF 96
Cdd:TIGR01271 1231 GRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVswNSVTLQT------WRKAFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 NLLdTLSVKDNIllplvlsrRPLKQMMTQ-VEAISRQLGIHSLLEKYP-----------YEISGGQKQRVAVARAIITKP 164
Cdd:TIGR01271 1302 FIF-SGTFRKNL--------DPYEQWSDEeIWKVAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCLARSILSKA 1372
|
170
....*....|...
gi 1092440915 165 EILLADEPTGALD 177
Cdd:TIGR01271 1373 KILLLDEPSAHLD 1385
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-203 |
4.40e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.52 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 1 MTLLDVQHVKKIYKTrfKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKP----TAGRVYLNGMDTATI 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKT--SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 77 KNKDASSFRRERLGFVFQDFNllDTLSVKDNILLPLVLS-----------RRPLKQMMTQVEAISRqLGI---HSLLEKY 142
Cdd:PRK15093 79 SPRERRKLVGHNVSMIFQEPQ--SCLDPSERVGRQLMQNipgwtykgrwwQRFGWRKRRAIELLHR-VGIkdhKDAMRSF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 143 PYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINA-SGQTILMVTH 203
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISH 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-203 |
4.95e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 22 VEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAssfRRERLGFVFQDFNLLDT 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA---LENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNILlplvLSRRPLK-------QMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTG 174
Cdd:PRK10982 88 RSVMDNMW----LGRYPTKgmfvdqdKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180
....*....|....*....|....*....
gi 1092440915 175 ALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-229 |
6.11e-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: 65.75 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 12 IYKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTA---GRVYLNGMDtatiKNKDASSFRREr 88
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIP----YKEFAEKYPGE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 89 LGFVFQDFNLLDTLSVKDniLLPLVLSrrplkqmmTQVEAISRQlgihsllekypyeISGGQKQRVAVARAIITKPEILL 168
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRE--TLDFALR--------CKGNEFVRG-------------ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 169 ADEPTGALDSKSSaalLDVFDAInasgQTILMVTHSTAAASRAQ----------RVLFIKDGilyNQIFKG 229
Cdd:cd03233 142 WDNSTRGLDSSTA---LEILKCI----RTMADVLKTTTFVSLYQasdeiydlfdKVLVLYEG---RQIYYG 202
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-220 |
1.58e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 65.65 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 19 GNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLN-ILAMLDkpTAGRVYLNGMDTATIKNKDAssfrRERLGFVFQDFN 97
Cdd:cd03289 16 GNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVPLQKW----RKAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 98 LLdTLSVKDNIllplvlsrRPLKQMMTQ-VEAISRQLGIHSLLEKYP-----------YEISGGQKQRVAVARAIITKPE 165
Cdd:cd03289 88 IF-SGTFRKNL--------DPYGKWSDEeIWKVAEEVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINAsGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-203 |
1.67e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNIL--AMLDKPTAGRVYLngmdtatiknkDASSFRRERlgfvfqdfNLLDTL 102
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDV-----------PDNQFGREA--------SLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNILLPL-VLSRRPLkqmmtqVEAISrqlgihsLLEKYPyEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSS 181
Cdd:COG2401 107 GRKGDFKDAVeLLNAVGL------SDAVL-------WLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|...
gi 1092440915 182 AAL-LDVFDAINASGQTILMVTH 203
Cdd:COG2401 173 KRVaRNLQKLARRAGITLVVATH 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-210 |
2.35e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdasSFRRErLGFVFQDFNLLDTLSV 104
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARK-VAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDnillpLV-LSRRPLKQMMTQVEAISRQ--------LGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGA 175
Cdd:PRK10575 103 RE-----LVaIGRYPWHGALGRFGAADREkveeaislVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092440915 176 LDsksSAALLDVFDAIN----ASGQTILMVTHSTAAASR 210
Cdd:PRK10575 178 LD---IAHQVDVLALVHrlsqERGLTVIAVLHDINMAAR 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-220 |
2.43e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.51 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLN-ILAMLDKpTAGRVYLNGmdtatiknkdassfrreRLGFVFQDfNLLDTLS 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG-----------------SVAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 VKDNILLPLVLSRRPLKQMMtQVEAISRQL-----GIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDS 178
Cdd:TIGR00957 715 LRENILFGKALNEKYYQQVL-EACALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092440915 179 KSSAallDVFDAINA-----SGQTILMVTHSTAAASRAQRVLFIKDG 220
Cdd:TIGR00957 794 HVGK---HIFEHVIGpegvlKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-203 |
2.78e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVeaLKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdTATIKNKDASSFRRERLGFVFQD 95
Cdd:PRK13638 10 RYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG--KPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 ------FNLLDT---LSVKdNILLPLVLSRRPLKQMMTQVEAIS-RQLGIHSLlekypyeiSGGQKQRVAVARAIITKPE 165
Cdd:PRK13638 86 peqqifYTDIDSdiaFSLR-NLGVPEAEITRRVDEALTLVDAQHfRHQPIQCL--------SHGQKKRVAIAGALVLQAR 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-222 |
1.02e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDA-------SSFRRERLGFVFQdfn 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivyISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 98 lldtLSVKDNILLPlvlSRRPLKQMMTQVEAISRQLGIHSLLE----KYPY------EISGGQKQRVAVARAIITKPEIL 167
Cdd:PRK10762 345 ----MSVKENMSLT---ALRYFSRAGGSLKHADEQQAVSDFIRlfniKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 168 LADEPTGALDsksSAALLDVFDAIN---ASGQTILMVThstaaaSRAQRVLFIKDGIL 222
Cdd:PRK10762 418 ILDEPTRGVD---VGAKKEIYQLINqfkAEGLSIILVS------SEMPEVLGMSDRIL 466
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-204 |
1.13e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.91 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 18 KGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKdassfrrerlgfvfqdfN 97
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISA-----------------G 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 98 LLDTLSVKDNI---LLPLVLSRRPLKQMMTQVEAISrQLG--IHSLLEKYpyeiSGGQKQRVAVARAIITKPEILLADEP 172
Cdd:PRK13546 96 LSGQLTGIENIefkMLCMGFKRKEIKAMTPKIIEFS-ELGefIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190
....*....|....*....|....*....|..
gi 1092440915 173 TGALDSKSSAALLDVFDAINASGQTILMVTHS 204
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHN 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-235 |
1.17e-11 |
|
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: 63.34 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknkdassfrreRLGFVFQdFNLLDTLSV 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQ-FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDNILLPLVLSRRPLKQMmtqVEAISRQLGIHSLLEKYP-------YEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:cd03291 115 KENIIFGVSYDEYRYKSV---VKACQLEEDITKFPEKDNtvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 178 SKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDGILYnqiFKGDKSEHQ 235
Cdd:cd03291 192 VFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSY---FYGTFSELQ 246
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-203 |
1.56e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.73 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 26 KDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVylngmdtatiknkdassFRRERLGFVFQDFNLLDTLSvk 105
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMAVFSQHHVDGLD-- 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 106 dnillplvLSRRPLKQMMTQVEAISRQ--------LGIHSLLEKYP-YEISGGQKQRVAVARAIITKPEILLADEPTGAL 176
Cdd:PLN03073 587 --------LSSNPLLYMMRCFPGVPEQklrahlgsFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190
....*....|....*....|....*....|
gi 1092440915 177 DSKSSAAL---LDVFDAinasgqTILMVTH 203
Cdd:PLN03073 659 DLDAVEALiqgLVLFQG------GVLMVSH 682
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-225 |
1.73e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLlnILAMLDK--PTAgrvylngmdtatiknkDASSFRRERLGFVFQ---DFNLl 99
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSL--ISAMLGElpPRS----------------DASVVIRGTVAYVPQvswIFNA- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 dtlSVKDNILLPLVLSRRPLKQMMtQVEAISRQLGI---HSLLE--KYPYEISGGQKQRVAVARAIITKPEILLADEPTG 174
Cdd:PLN03130 694 ---TVRDNILFGSPFDPERYERAI-DVTALQHDLDLlpgGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 175 ALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDGILYNQ 225
Cdd:PLN03130 770 ALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-235 |
2.07e-11 |
|
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: 63.78 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtatiknkdassfrreRLGFVFQdFNLLDTLSV 104
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQ-TSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDNILLPLVLSRRplkQMMTQVEAISRQLGIHSLLEKYP-------YEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:TIGR01271 504 KDNIIFGLSYDEY---RYTSVIKACQLEEDIALFPEKDKtvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 178 SKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDGILYnqiFKGDKSEHQ 235
Cdd:TIGR01271 581 VVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCY---FYGTFSELQ 635
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-239 |
2.41e-11 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 61.85 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTL-LNILAMLDKpTAGRVYLNGMDTATIKNKDAssfrRERLGFVFQ 94
Cdd:cd03288 28 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDI-FDGKIVIDGIDISKLPLHTL----RSRLSIILQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 95 D---------FNLLDTLSVKDNILLPlVLSRRPLKQMMTQVEAisrqlGIHSLLEKYPYEISGGQKQRVAVARAIITKPE 165
Cdd:cd03288 103 DpilfsgsirFNLDPECKCTDDRLWE-ALEIAQLKNMVKSLPG-----GLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINASgQTILMVTHSTAAASRAQRVLFIKDGILynqiFKGDKSEHQMFQE 239
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVSTILDADLVLVLSRGIL----VECDTPENLLAQE 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-222 |
2.57e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLlnILAMLDKptagrvyLNGMDTATIKNKDASSFRrERLGFVFQdfnlldtLSV 104
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSL--ISAMLGE-------LSHAETSSVVIRGSVAYV-PQVSWIFN-------ATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 105 KDNILLPLVL-SRRPLKQMmtQVEAISRQLGI---HSLLE--KYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDS 178
Cdd:PLN03232 696 RENILFGSDFeSERYWRAI--DVTALQHDLDLlpgRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1092440915 179 KSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKDGIL 222
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-214 |
3.47e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.66 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 40 IMGESGSGKSTLLNILAMLDKPTAGRVYlngmdtatIKNKDASSFRRERLGFVFQDFNLLDTLSVKDNILLplvlsRRPL 119
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIY--------YKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKF-----WSEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 120 KQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALdSKSSAALLDVFDAINA-SGQTI 198
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL-SKENRDLLNNLIVMKAnSGGIV 176
|
170
....*....|....*.
gi 1092440915 199 LMVTHSTAAASRAQRV 214
Cdd:PRK13541 177 LLSSHLESSIKSAQIL 192
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
20-203 |
3.81e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 61.12 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 20 NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDK--PTAGRVYLNGMDTATIKNKDassfrRERLG-FV-FQd 95
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKGQDLLELEPDE-----RARAGlFLaFQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 fNLLDTLSVKDNILLPLVL-SRR--------PLKQMMTQVEAISRQLGI-HSLLEKYPYE-ISGGQKQRVAVARAIITKP 164
Cdd:TIGR01978 85 -YPEEIPGVSNLEFLRSALnARRsargeeplDLLDFEKLLKEKLALLDMdEEFLNRSVNEgFSGGEKKRNEILQMALLEP 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092440915 165 EILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:TIGR01978 164 KLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-234 |
3.82e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMdTATIKNKDASsfrRERLGFVFQDFNLLDTLS 103
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-PVTAEQPEDY---RKLFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 VKDNILLPLVLSRRPLK--QMMTQVEAISRQLGIHSLlekypyeiSGGQKQRVAVARAIITKPEILLADEptgaldsksS 181
Cdd:PRK10522 414 GPEGKPANPALVEKWLErlKMAHKLELEDGRISNLKL--------SKGQKKRLALLLALAEERDILLLDE---------W 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 182 AALLD-----VF-----DAINASGQTILMVTHSTAAASRAQRVLFIKDGILYNqiFKGDKSEH 234
Cdd:PRK10522 477 AADQDphfrrEFyqvllPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE--LTGEERDA 537
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-246 |
4.62e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.66 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 13 YKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAssfrRERLGFV 92
Cdd:TIGR00957 1290 YCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 93 FQDfNLLDTLSVKDNiLLPlvLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYE-------ISGGQKQRVAVARAIITKPE 165
Cdd:TIGR00957 1366 PQD-PVLFSGSLRMN-LDP--FSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 166 ILLADEPTGALDskssaalLDVFDAINAsgqTILMVTHSTAAASRAQRVLFIKDgilYNQIFKGDKSEHQMFQEISDTLT 245
Cdd:TIGR00957 1442 ILVLDEATAAVD-------LETDNLIQS---TIRTQFEDCTVLTIAHRLNTIMD---YTRVIVLDKGEVAEFGAPSNLLQ 1508
|
.
gi 1092440915 246 A 246
Cdd:TIGR00957 1509 Q 1509
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-220 |
6.86e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILA-MLDKPTA-------GRVYLNGMDTATIknkDASSFRRERL------- 89
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAI---DAPRLARLRAvlpqaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 90 -GFVFqdfnlldtlSVKDNILL---PLVlsRRPLKQMMTQVEAISRQL---GIHSLLEKYPYEISGGQKQRVAVARAI-- 160
Cdd:PRK13547 94 pAFAF---------SAREIVLLgryPHA--RRAGALTHRDGEIAWQALalaGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092440915 161 -------ITKPEILLADEPTGALDSKSSAALLDVFDAINASGQT-ILMVTHSTAAASR-AQRVLFIKDG 220
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARhADRIAMLADG 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-173 |
7.30e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYL-------NGMDTatiknkdassfrRERLGFVFQDF 96
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdaGDIAT------------RRRVGYMSQAF 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 97 NLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPT 173
Cdd:NF033858 349 SLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-204 |
9.36e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 9 VKKIYKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdTATIKNKDASsfrrer 88
Cdd:PRK13545 24 LKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--SAALIAISSG------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 89 lgfvfqdfnLLDTLSVKDNILLP---LVLSRRPLKQMMTQVEAISrQLG--IHSLLEKYpyeiSGGQKQRVAVARAIITK 163
Cdd:PRK13545 96 ---------LNGQLTGIENIELKglmMGLTKEKIKEIIPEIIEFA-DIGkfIYQPVKTY----SSGMKSRLGFAISVHIN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHS 204
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHS 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-182 |
1.01e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAssfrRERLGFVFQD 95
Cdd:PLN03130 1246 RYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQA 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 ---------FNlLDTLSVKDNILLPLVLSRRPLKqmmtqvEAISRQ-LGIHSLLEKYPYEISGGQKQRVAVARAIITKPE 165
Cdd:PLN03130 1322 pvlfsgtvrFN-LDPFNEHNDADLWESLERAHLK------DVIRRNsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170
....*....|....*..
gi 1092440915 166 ILLADEPTGALDSKSSA 182
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDA 1411
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-246 |
1.02e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYlngmdtatiknkdassfrRER-LGFVFQDFNLLDTlS 103
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------------------AERsIAYVPQQAWIMNA-T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 104 VKDNILL--PLVLSRRPLKQMMTQVEAISRQL--GIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSK 179
Cdd:PTZ00243 737 VRGNILFfdEEDAARLADAVRVSQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 180 SSAALL-DVFDAINAsGQTILMVTHSTAAASRAQRVLFIKDGILynqIFKGDkSEHQMFQEISDTLTA 246
Cdd:PTZ00243 817 VGERVVeECFLGALA-GKTRVLATHQVHVVPRADYVVALGDGRV---EFSGS-SADFMRTSLYATLAA 879
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-178 |
1.88e-10 |
|
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: 59.34 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 22 VEALKDIHFTVDKGDY-----VAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTA----TIKNKDASSFRrerlgfv 92
Cdd:cd03237 7 KKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVR------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 93 fqdfnllDTLSVKDNILLplvlsrrplKQMMTQVEaISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEP 172
Cdd:cd03237 80 -------DLLSSITKDFY---------THPYFKTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
....*.
gi 1092440915 173 TGALDS 178
Cdd:cd03237 143 SAYLDV 148
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-203 |
2.51e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 20 NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAmlDKP----TAGRVYLNGMDtatIKNKDASsfRRERLGfVFQD 95
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGES---ILDLEPE--ERAHLG-IFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 F-NLLDTLSVKDNILLPLVLSRRPLKQMMTQVEA------ISRQLGI----HSLLEKYPYE-ISGGQKQRVAVARAIITK 163
Cdd:CHL00131 90 FqYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPlefleiINEKLKLvgmdPSFLSRNVNEgFSGGEKKRNEILQMALLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092440915 164 PEILLADEPTGALDSKssaALLDVFDAINA---SGQTILMVTH 203
Cdd:CHL00131 170 SELAILDETDSGLDID---ALKIIAEGINKlmtSENSIILITH 209
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-201 |
4.33e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 11 KIYKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYlngmdtatiknkdaSSFRR-ERL 89
Cdd:PRK10938 5 QISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ--------------SQFSHiTRL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 90 GF---------VFQDFN--LL-----DT---------LSVKDNILlplvlsrrplkqmmtqVEAISRQLGIHSLLEKYPY 144
Cdd:PRK10938 71 SFeqlqklvsdEWQRNNtdMLspgedDTgrttaeiiqDEVKDPAR----------------CEQLAQQFGITALLDRRFK 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 145 EISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMV 201
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-178 |
8.64e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 31 TVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLngmdTATIknkdasSFRRERLGfvfQDFNLldtlSVKDNIll 110
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE----DLKI------SYKPQYIS---PDYDG----TVEEFL-- 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 111 plvlsRRPLKQMMT----QVEaISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDS 178
Cdd:COG1245 423 -----RSANTDDFGssyyKTE-IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-239 |
9.28e-10 |
|
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: 58.30 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 27 DIHFTVDKGDYVAIMGESGSGKSTLLN-ILAMLDKPTAGRVYLNGMDTATIKNKDASsfrRERLGFVFQD---FNLLDTL 102
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAI---RAGIAMVPEDrkrHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 103 SVKDNILLPLVLSRRPLKQMMTQVE--AISRQLGIHSLLEKYPY----EISGGQKQRVAVARAIITKPEILLADEPTGAL 176
Cdd:TIGR02633 355 GVGKNITLSVLKSFCFKMRIDAAAElqIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 177 DSKSSAALLDVFDAINASGQTILMVTHSTAAA-SRAQRVLFIKDGILynqifKGDKSEHQMFQE 239
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVVSSELAEVlGLSDRVLVIGEGKL-----KGDFVNHALTQE 493
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-222 |
1.37e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDassfrRERLGFVF-----QDFN 97
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 98 LLDTLSVKDNILlPLVLSRRPLKQMMTQ----VEAISRQLGIH-SLLEKYPYEISGGQKQRVAVARAIITKPEILLADEP 172
Cdd:PRK15439 352 LYLDAPLAWNVC-ALTHNRRGFWIKPARenavLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 173 TGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR-AQRVLFIKDGIL 222
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-229 |
1.55e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGrvylngmdtaTIKNKDASSfrrerLGFVFQD--------F 96
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSENAN-----IGYYAQDhaydfendL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 NLLDTLS----VKDNILLplvlSRRPLKQMMTQVEAISRQLGIhsllekypyeISGGQKQRVAVARAIITKPEILLADEP 172
Cdd:PRK15064 400 TLFDWMSqwrqEGDDEQA----VRGTLGRLLFSQDDIKKSVKV----------LSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092440915 173 TGALDSKSSAAL---LDVFDAinasgqTILMVTHSTA-AASRAQRVLFIKDGILYNqiFKG 229
Cdd:PRK15064 466 TNHMDMESIESLnmaLEKYEG------TLIFVSHDREfVSSLATRIIEITPDGVVD--FSG 518
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-204 |
1.62e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 3 LLDVQHVKKIYKtrfkGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATiknkdAS 82
Cdd:TIGR01257 1937 ILRLNELTKVYS----GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----NI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 83 SFRRERLGFVFQDFNLLDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092440915 163 KPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHS 204
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2129
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-249 |
2.86e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 11 KIYKTRFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAM----LDKPTAGRVYLNGMDTATIKNkdassFRR 86
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKK-----HYR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 87 ERLGFVFQDFNLLDTLSVKDNillpLVLSRRpLKQMMTQVEAISRQLGIHSLLEKYPYE------------------ISG 148
Cdd:TIGR00956 138 GDVVYNAETDVHFPHLTVGET----LDFAAR-CKTPQNRPDGVSREEYAKHIADVYMATyglshtrntkvgndfvrgVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 149 GQKQRVAVARAIITKPEILLADEPTGALDsksSAALLDVFDAInasgQTILMVTHSTA-----AASRAQRVLFIKDGILY 223
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLD---SATALEFIRAL----KTSANILDTTPlvaiyQCSQDAYELFDKVIVLY 285
|
250 260 270
....*....|....*....|....*....|....*....
gi 1092440915 224 N--QIFKGDKSEHQMF-----------QEISDTLTAMAS 249
Cdd:TIGR00956 286 EgyQIYFGPADKAKQYfekmgfkcpdrQTTADFLTSLTS 324
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-241 |
4.09e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDAssfrRERLGFVFQD 95
Cdd:PLN03232 1243 RYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 96 ---------FNlLDTLSVKDNILLPLVLSRRPLKqmmtqvEAISRQ-LGIHSLLEKYPYEISGGQKQRVAVARAIITKPE 165
Cdd:PLN03232 1319 pvlfsgtvrFN-IDPFSEHNDADLWEALERAHIK------DVIDRNpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 166 ILLADEPTGALDSKSSAALLDVFDAINASGqTILMVTHSTAAASRAQRVLFIKDGilynQIFKGDKSEHQMFQEIS 241
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSC-TMLVIAHRLNTIIDCDKILVLSSG----QVLEYDSPQELLSRDTS 1462
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-217 |
4.86e-09 |
|
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: 54.25 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 17 FKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNilAMLDKPTAGRVylngmdtatikNKDASSFRRERLGFVFQDF 96
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARL-----------ISFLPKFSRNKLIFIDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 NLLDtlsvkdnillpLVLSRRPLKQMMTQveaisrqlgihsllekypyeISGGQKQRVAVARAII--TKPEILLADEPTG 174
Cdd:cd03238 70 FLID-----------VGLGYLTLGQKLST--------------------LSGGELQRVKLASELFsePPGTLFILDEPST 118
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092440915 175 ALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFI 217
Cdd:cd03238 119 GLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-206 |
2.44e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.14 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 35 GDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNkdassFRRERLGFVFQDFnLLDTLSVkdnILLPLVL 114
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDE-----FRGSELQNYFTKL-LEGDVKV---IVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 115 SRRP----------LKQM--MTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSA 182
Cdd:cd03236 97 DLIPkavkgkvgelLKKKdeRGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|....
gi 1092440915 183 ALLDVFDAINASGQTILMVTHSTA 206
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-177 |
5.40e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAmldkptaGRVYLNgmDTATIKNKDASSFR------RERLGFVFqDF-- 96
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLD--DGRIIYEQDLIVARlqqdppRNVEGTVY-DFva 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 97 ----NLLDTLSVKDNILLpLVL---SRRPLKQMMTQVEAISRQLG------IHSLLEKYPY-------EISGGQKQRVAV 156
Cdd:PRK11147 89 egieEQAEYLKRYHDISH-LVEtdpSEKNLNELAKLQEQLDHHNLwqlenrINEVLAQLGLdpdaalsSLSGGWLRKAAL 167
|
170 180
....*....|....*....|.
gi 1092440915 157 ARAIITKPEILLADEPTGALD 177
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-177 |
6.62e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 31 TVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVylngmdTATIKnkdaSSFRRErlgFVFQDFNLldtlSVKDNill 110
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELK----ISYKPQ---YIKPDYDG----TVEDL--- 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 111 plvlsrrpLKQMMTQVEA------ISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK13409 421 --------LRSITDDLGSsyykseIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-203 |
1.36e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNIlaMLD--KPTAGRVYL---------------------------NGMDTAT 75
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGqlQADSGRIHCgtklevayfdqhraeldpektvmdnlaEGKQEVM 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 76 IKNKDassfrRERLGFVfQDFnlldtlsvkdniLLPlvlsrrPlKQMMTQVEAisrqlgihsllekypyeISGGQKQRVA 155
Cdd:PRK11147 413 VNGRP-----RHVLGYL-QDF------------LFH------P-KRAMTPVKA-----------------LSGGERNRLL 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1092440915 156 VARaIITKPEILLA-DEPTGALDSKSsaalLDVFDAINASGQ-TILMVTH 203
Cdd:PRK11147 451 LAR-LFLKPSNLLIlDEPTNDLDVET----LELLEELLDSYQgTVLLVSH 495
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-220 |
1.76e-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: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 38 VAIMGESGSGKSTLLNILA-MLDKPTAGRVYLNGmdtatiknkdassfrrerlgfvfqdfnlldtlsvkdnillplvlsr 116
Cdd:smart00382 5 ILIVGPPGSGKTTLARALArELGPPGGGVIYIDG---------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 117 rplkqmmTQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLD------VFDA 190
Cdd:smart00382 39 -------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLL 111
|
170 180 190
....*....|....*....|....*....|....*.
gi 1092440915 191 INASGQTILMVTH------STAAASRAQRVLFIKDG 220
Cdd:smart00382 112 KSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLI 147
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-177 |
2.04e-07 |
|
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: 51.32 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 34 KGDYVAIMGESGSGKSTLLNILAMLDKPTAGRvYLNGMDTATIKNKdassFRRERLGFVFQDfnLLD---TLSVK----D 106
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGD-YDEEPSWDEVLKR----FRGTELQDYFKK--LANgeiKVAHKpqyvD 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092440915 107 NIllPLVLSRRPlKQMMTQV------EAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:COG1245 171 LI--PKVFKGTV-RELLEKVdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-102 |
2.89e-07 |
|
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: 50.95 E-value: 2.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092440915 28 IHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtATIKNKDASSFrRERLGFVFQDFNLLDTL 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG---QPVTADNREAY-RQLFSAVFSDFHLFDRL 421
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-203 |
6.84e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 20 NQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAmlDKPTAGrvYLNGMDTATIKNKDASSFRRERlGFVFQDFNLL 99
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--GRKTGG--YIEGDIRISGFPKKQETFARIS-GYCEQNDIHS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 100 DTLSVKDNIL------LPLVLSR----RPLKQMMTQVE------AISRQLGIHSLlekypyeiSGGQKQRVAVARAIITK 163
Cdd:PLN03140 966 PQVTVRESLIysaflrLPKEVSKeekmMFVDEVMELVEldnlkdAIVGLPGVTGL--------STEQRKRLTIAVELVAN 1037
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
16-214 |
7.95e-07 |
|
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: 48.41 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 16 RFKGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLL--NILAMLDK------PTAGRVYLNGMD------------TAT 75
Cdd:cd03270 2 IVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdTIYAEGQRryveslSAYARQFLGQMDkpdvdsieglspAIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 76 IKNKDASSFRRERLGFVFQDFNLLDTLSVKDNIllplvlsRRPLKQMmtqveaisRQLGIHSL-LEKYPYEISGGQKQRV 154
Cdd:cd03270 82 IDQKTTSRNPRSTVGTVTEIYDYLRLLFARVGI-------RERLGFL--------VDVGLGYLtLSRSAPTLSGGEAQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 155 AVARAIITKPE--ILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRV 214
Cdd:cd03270 147 RLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHV 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-203 |
9.48e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.16 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 4 LDVQHVKKIYKTRFkgnqveALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNgmdtATIKnkdass 83
Cdd:TIGR03719 323 IEAENLTKAFGDKL------LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVK------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 84 frrerLGFVFQdfnlldtlsvkdnillplvlSRRPLKQMMTQVEAISR-----QLGIHSL---------------LEKYP 143
Cdd:TIGR03719 387 -----LAYVDQ--------------------SRDALDPNKTVWEEISGgldiiKLGKREIpsrayvgrfnfkgsdQQKKV 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 144 YEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLdvfDAINASGQTILMVTH 203
Cdd:TIGR03719 442 GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALE---EALLNFAGCAVVISH 498
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-223 |
1.00e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMlDKPTAgrvYLNgmdtatiknkDASSFRRER------------LGFV 92
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG---YSN----------DLTLFGRRRgsgetiwdikkhIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 93 FQDFNLlD---TLSVKDNILLPL-----VLSRRPLKQMMTQVEAISRqLGIHSLLEKYPYE-ISGGQKQRVAVARAIITK 163
Cdd:PRK10938 342 SSSLHL-DyrvSTSVRNVILSGFfdsigIYQAVSDRQQKLAQQWLDI-LGIDKRTADAPFHsLSWGQQRLALIVRALVKH 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 164 PEILLADEPTGALDSKSSAALLDVFDAINASGQT-ILMVTHSTAAASR--AQRVLFIKDGILY 223
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAciTHRLEFVPDGDIY 482
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-238 |
1.71e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 28 IHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMDTATIKNKDASsfrreRLGFVF------QDfNLLDT 101
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAI-----RAGIMLcpedrkAE-GIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNILLPlvlSRR---PLKQMMTQV-EAISRQLGIHSLLEKYPY------EISGGQKQRVAVARAIITKPEILLADE 171
Cdd:PRK11288 346 HSVADNINIS---ARRhhlRAGCLINNRwEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092440915 172 PTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAA-SRAQRVLFIKDGILYNQIFKGDKSEHQMFQ 238
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVlGVADRIVVMREGRIAGELAREQATERQALS 490
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-205 |
3.68e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.44 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 27 DIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYlngmdtatiknKDassfRRERLGFVFQD-FNLLDTLsvK 105
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT-----------KP----AKGKLFYVPQRpYMTLGTL--R 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 106 DNILLPLV--------LSRRPLKQMM--TQVEAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTga 175
Cdd:TIGR00954 533 DQIIYPDSsedmkrrgLSDKDLEQILdnVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT-- 610
|
170 180 190
....*....|....*....|....*....|....
gi 1092440915 176 ldsksSAALLDVFDAI----NASGQTILMVTHST 205
Cdd:TIGR00954 611 -----SAVSVDVEGYMyrlcREFGITLFSVSHRK 639
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-177 |
4.19e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLlnilAM------LDKPTAGRVYLNG--MDTAT----IKNKDA-SSFRRERLGF 91
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTEL----AMsvfgrsYGRNISGTVFKDGkeVDVSTvsdaIDAGLAyVTEDRKGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 92 vfqdfNLLDTlsVKDNILLPLV--LSRRPL--KQMMTQV-EAISRQLGI--HSLLEKYPyEISGGQKQRVAVARAIITKP 164
Cdd:NF040905 352 -----NLIDD--IKRNITLANLgkVSRRGVidENEEIKVaEEYRKKMNIktPSVFQKVG-NLSGGNQQKVVLSKWLFTDP 423
|
170
....*....|...
gi 1092440915 165 EILLADEPTGALD 177
Cdd:NF040905 424 DVLILDEPTRGID 436
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-203 |
5.06e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 42 GESGSGKSTLLNILAMLDKPTAGRVYLNgmdtatiknkdassfRRERLG------FVFQDFNLLDTLsvkdnillplVLS 115
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLD---------------PNERLGklrqdqFAFEEFTVLDTV----------IMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 116 RRPLKQMMTQVEAI------------------------------SR------QLGI----HSLLEKypyEISGGQKQRVA 155
Cdd:PRK15064 89 HTELWEVKQERDRIyalpemseedgmkvadlevkfaemdgytaeARagelllGVGIpeeqHYGLMS---EVAPGWKLRVL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1092440915 156 VARAIITKPEILLADEPTGALDSKSSAALLDVfdaINASGQTILMVTH 203
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMIIISH 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-177 |
6.02e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 31 TVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRvYLNGMDTATIKNKdassFRRERLGFVFQDfnLLD---TLSVK-- 105
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWDEVLKR----FRGTELQNYFKK--LYNgeiKVVHKpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 106 --DniLLPLVLSRRpLKQMMTQV------EAISRQLGIHSLLEKYPYEISGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PRK13409 168 yvD--LIPKVFKGK-VRELLKKVdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-239 |
7.17e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 27 DIHFTVDKGDYVAIMGESGSGKSTLLN-ILAMLDKPTAGRVYLNGmDTATIKN-KDASsfrRERLGFVFQD---FNLLDT 101
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDG-KPVKIRNpQQAI---AQGIAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 102 LSVKDNILLPlVLSR-----------------RPLKQMmtQVEAISRQLGIHSLlekypyeiSGGQKQRVAVARAIITKP 164
Cdd:PRK13549 356 MGVGKNITLA-ALDRftggsriddaaelktilESIQRL--KVKTASPELAIARL--------SGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092440915 165 EILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAA-SRAQRVLFIKDGILynqifKGDKSEHQMFQE 239
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVlGLSDRVLVMHEGKL-----KGDLINHNLTQE 495
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-177 |
9.73e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 24 ALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGmdtATIKNKDA-----------SSFRRERLGFV 92
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNAneainhgfalvTEERRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 93 FQDFNLLDTLSVKDNILLPL-VLSRRPLKQMmTQ-------VEAISRQLGIHSLlekypyeiSGGQKQRVAVARAIITKP 164
Cdd:PRK10982 340 YLDIGFNSLISNIRNYKNKVgLLDNSRMKSD-TQwvidsmrVKTPGHRTQIGSL--------SGGNQQKVIIGRWLLTQP 410
|
170
....*....|...
gi 1092440915 165 EILLADEPTGALD 177
Cdd:PRK10982 411 EILMLDEPTRGID 423
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
147-219 |
2.17e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 2.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 147 SGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFIKD 219
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVID 218
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
90-246 |
2.27e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 90 GFVFQDFNL--LDTLSVKDNILLPLVLSRRPLKQMMTQVEAISRQLGIHSL-LEKYPYEISGGQKQRVAVARAI------ 160
Cdd:PRK00635 418 GKTFAEFQQmsLQELFIFLSQLPSKSLSIEEVLQGLKSRLSILIDLGLPYLtPERALATLSGGEQERTALAKHLgaelig 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 161 ITKpeILlaDEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRAQRVLFI--KDGILYNQI-FKGDKSEhqmF 237
Cdd:PRK00635 498 ITY--IL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIgpGAGIFGGEVlFNGSPRE---F 570
|
....*....
gi 1092440915 238 QEISDTLTA 246
Cdd:PRK00635 571 LAKSDSLTA 579
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
146-210 |
3.12e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 3.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 146 ISGGQKQRVAVARAII--------TKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASR 210
Cdd:PRK10246 950 LSGGESFLVSLALALAlsdlvshkTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKER 1022
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-203 |
5.56e-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: 42.98 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 39 AIMGESGSGKSTLLNILAML---DKPTAGRVYLNGMDTATIKNKDASSfrrerlgfvfqdfnlldTLSVKDNILLPLVLS 115
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEVRAQV-----------------KLAFENANGKKYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 116 RRPlkQMMTQVeAISRQLGIHSLLEKYPYEISGGQKQ------RVAVARAIITKPEILLADEPTGALDSKS-SAALLDVF 188
Cdd:cd03240 89 RSL--AILENV-IFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEII 165
|
170
....*....|....*..
gi 1092440915 189 DAINASG--QTILmVTH 203
Cdd:cd03240 166 EERKSQKnfQLIV-ITH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
25-215 |
8.20e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 25 LKDIHFTVDKGDYVAIMGESGSGKSTLLN---ILAM-------------LDKPTAGRV------------------YLNG 70
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSSLINdtlVPAVeefieqgfcsnlsIQWGAISRLvhitrdlpgrsqrsipltYIKA 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 71 MDTatIKNKDASSFRRERLGFV---FQdFNL----------LDTLSVKDN---ILLPLVLSRRPLKQM------------ 122
Cdd:PRK00635 691 FDD--LRELFAEQPRSKRLGLTkshFS-FNTplgacaecqgLGSITTTDNrtsIPCPSCLGKRFLPQVlevrykgkniad 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 123 ---MTQVEAISRQLG-------IHSL----LEKYP-----YEISGGQKQRVAVARAIIT---KPEILLADEPTGALDSKS 180
Cdd:PRK00635 768 ileMTAYEAEKFFLDepsihekIHALcslgLDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHD 847
|
250 260 270
....*....|....*....|....*....|....*
gi 1092440915 181 SAALLDVFDAINASGQTILMVTHSTAAASRAQRVL 215
Cdd:PRK00635 848 IKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
147-177 |
1.84e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.84e-04
10 20 30
....*....|....*....|....*....|.
gi 1092440915 147 SGGQKQRVAVARAIITKPEILLADEPTGALD 177
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-70 |
1.11e-03 |
|
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: 40.00 E-value: 1.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1092440915 18 KGNQVEALKDIHFTVDKGDYVAIMGESGSGKSTLLN-ILAmldkPTAGRvYLNG 70
Cdd:TIGR00630 617 KGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINdTLY----PALAN-RLNG 665
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-203 |
1.11e-03 |
|
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: 39.52 E-value: 1.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 144 YEISGGQKQRVAVARAII---TKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEH 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-208 |
1.44e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.32 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 32 VDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRVYLNGMdtatiknkdassfrrerlgfvfqdfnlldTLSVKDNILlp 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI-----------------------------TPVYKPQYI-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 112 lvlsrrplkqmmtqveaisrqlgihsllekypyEISGGQKQRVAVARAIITKPEILLADEPTGALDSKSSAALLDVFDAI 191
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*...
gi 1092440915 192 NASG-QTILMVTHSTAAA 208
Cdd:cd03222 118 SEEGkKTALVVEHDLAVL 135
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
39-213 |
1.91e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 38.52 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 39 AIMGESGSGKSTLLNILAM----------LDKPTAGRV-YLNGMDtatiknkDASSFRReRLGFVFQDFNLLDTLSVKDN 107
Cdd:cd01125 5 MLVGPPGSGKSFLALDLAVavatgrdwlgERRVKQGRVvYLAAED-------PRDGLRR-RLKAIGAHLGDEDAALAENL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 108 ILLPLVLSRRPLKQMMTQVEAIsrqlgihsllekypyeisggqKQRVAVARAIITKP--EILL-ADEPtgalDSKSSAAL 184
Cdd:cd01125 77 VIENLRGKPVSIDAEAPELERI---------------------IEELEGVRLIIIDTlaRVLHgGDEN----DAADMGAF 131
|
170 180 190
....*....|....*....|....*....|
gi 1092440915 185 LDVFDAI-NASGQTILMVTHSTAAASRAQR 213
Cdd:cd01125 132 VAGLDRIaRETGAAVLLVHHTGKDAAGDSQ 161
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-66 |
2.81e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 2.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 4 LDVQHVKKIYktrfkGNQVeALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLDKPTAGRV 66
Cdd:PRK11819 325 IEAENLSKSF-----GDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
143-218 |
3.21e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.80 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092440915 143 PYE-ISGGQKQRVAVARAII----------TKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTHSTAAASRA 211
Cdd:TIGR00618 947 PSAtLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERI 1026
|
....*..
gi 1092440915 212 QRVLFIK 218
Cdd:TIGR00618 1027 PHRILVK 1033
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-72 |
6.18e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 37.08 E-value: 6.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1092440915 23 EALKDIHFTVDKGDYVAIMGESGSGKSTLLNILAMLD--KPTAGRVYLNGMD 72
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKD 66
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-203 |
8.92e-03 |
|
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: 37.30 E-value: 8.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092440915 144 YEISGGQKQRVAVARAI---ITKPEILLADEPTGALDSKSSAALLDVFDAINASGQTILMVTH 203
Cdd:TIGR00630 828 TTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| |
