|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-226 |
2.80e-112 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 321.99 E-value: 2.80e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA 81
Cdd:COG1136 3 PLLELRNLTKSYGTG--EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 SSFRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAII 161
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 162 TSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAARAKRVLFIKDGILYNQI 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 |
2.92e-101 |
|
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: 293.63 E-value: 2.92e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTrfQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASS 83
Cdd:cd03255 1 IELKNLSKTYGG--GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03255 79 FRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAARAKRVLFIKDG 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 |
8.12e-92 |
|
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: 269.49 E-value: 8.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 6 VQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFR 85
Cdd:TIGR03608 1 LKNISKKFGDK------VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 86 REKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPE 165
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFI 217
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-230 |
7.30e-82 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 244.58 E-value: 7.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 7 QHVKKIYktrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRR 86
Cdd:COG2884 5 ENVSKRY-----PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 eKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEI 166
Cdd:COG2884 80 -RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 167 LLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTA-AAARAKRVLFIKDGILYNQIFRGE 230
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-222 |
7.25e-75 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 226.91 E-value: 7.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAS 82
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKV--LNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:NF038007 79 ILRRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDGIL 222
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-222 |
8.55e-68 |
|
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: 209.21 E-value: 8.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIkNKDA 81
Cdd:COG4181 7 PIIELRGLTKTVGTG--AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 -SSFRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRP-----VKEMMSKVdsvsrelGIHQLLEKYPYEISGGQKQRVA 155
Cdd:COG4181 84 rARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRdararARALLERV-------GLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 156 VARAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAARAKRVLFIKDGIL 222
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-203 |
2.00e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 206.47 E-value: 2.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 6 VQHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFR 85
Cdd:COG1135 4 LENLSKTFPTK--GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 86 ReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSvsrelgihqLLE---------KYPYEISGGQKQRVAV 156
Cdd:COG1135 82 R-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAE---------LLElvglsdkadAYPSQLSGGQKQRVGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 552782194 157 ARAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTH 203
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINReLGLTIVLITH 199
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
4.44e-65 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 203.01 E-value: 4.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtSTIKNKD 80
Cdd:COG1116 5 APALELRGVSKRFPTG--GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG---KPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 AssfrreKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG1116 80 P------DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 161 ITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAAR-AKRVL 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 |
1.75e-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: 200.17 E-value: 1.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYktrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAS 82
Cdd:TIGR02673 1 MIEFHNVSKAY-----PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:TIGR02673 76 LLRR-RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTA-AAARAKRVLFIKDGI 221
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-203 |
1.82e-62 |
|
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: 195.49 E-value: 1.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 6 VQHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFR 85
Cdd:cd03258 4 LKNVSKVFGDT--GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 86 ReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPE 165
Cdd:cd03258 82 R-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTH 203
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINrELGLTIVLITH 199
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-220 |
1.82e-62 |
|
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: 203.98 E-value: 1.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRFQGTqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAS 82
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGG-VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRReKLGFVFQD-FNLLD-TLSVKDNILLPLVLSRR-PVKEMMSKVDSVSRELGIH-QLLEKYPYEISGGQKQRVAVAR 158
Cdd:COG1123 339 ELRR-RVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552782194 159 AIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQrELGLTYLFISHDLAVVRYiADRVAVMYDG 481
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-222 |
3.56e-62 |
|
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: 195.41 E-value: 3.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDAS 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPV--LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP---VTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRReKLGFVFQD----FNLLdtLSVKDNILLPLVLSRRPvkEMMSKVDSVSRELGIH-QLLEKYPYEISGGQKQRVAVA 157
Cdd:COG1124 76 AFRR-RVQMVFQDpyasLHPR--HTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 158 RAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDGIL 222
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
9.33e-62 |
|
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: 193.49 E-value: 9.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAS 82
Cdd:cd03257 1 LLEVKNLSVSFPTG--GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRREkLGFVFQD-FNLLD-TLSVKDNILLPLVLSRRPVKEMMSK--VDSVSRELGIH-QLLEKYPYEISGGQKQRVAVA 157
Cdd:cd03257 79 IRRKE-IQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSKKEARKeaVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 158 RAIITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
9.88e-62 |
|
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: 193.46 E-value: 9.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiknkdass 83
Cdd:cd03293 1 LEVRNVSKTYGGG--GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 fRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03293 71 -PGPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAAR-AKRVL 215
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFlADRVV 203
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
2.35e-60 |
|
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: 189.65 E-value: 2.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKtrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdasS 83
Cdd:cd03259 1 LELKGLSKTYG------SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03259 69 PERRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALAlADRIAVMNEG 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-220 |
2.14e-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: 187.54 E-value: 2.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 21 QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRReKLGFVFQD----- 95
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELRR-KVGLVFQNpddql 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLldtlSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGA 175
Cdd:COG1122 89 FAP----TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552782194 176 LDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG1122 165 LDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDG 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-234 |
5.40e-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: 186.74 E-value: 5.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKiyktRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTsTIKNKDAS 82
Cdd:COG1126 1 MIEIENLHK----SFGDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRpvkemMSK--VDSVSREL----GIHQLLEKYPYEISGGQKQRVAV 156
Cdd:COG1126 74 KLRR-KVGMVFQQFNLFPHLTVLENVTLAPIKVKK-----MSKaeAEERAMELlervGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 157 ARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILY-----NQIFRGE 230
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVeegppEEFFENP 227
|
....
gi 552782194 231 KTER 234
Cdd:COG1126 228 QHER 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-220 |
6.43e-58 |
|
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: 184.41 E-value: 6.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKiyktRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA 81
Cdd:COG1127 4 PMIEVRNLTK----SFGDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 SSFRReKLGFVFQDFNLLDTLSVKDNILLPLV-LSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG1127 78 YELRR-RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782194 161 ITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAiADRVAVLADG 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-222 |
2.87e-57 |
|
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: 181.84 E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 10 KKIYKTrfQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRReKL 89
Cdd:cd03292 4 INVTKT--YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 90 GFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLA 169
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552782194 170 DEPTGALDSKSSAALLDVFEDINSMGQTILMVTH-STAAAARAKRVLFIKDGIL 222
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-220 |
1.33e-56 |
|
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: 179.97 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfRREKLGFVFQD 95
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNL-LDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:cd03225 84 PDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552782194 175 ALDSKSSAALLDVFEDINSMGQTILMVTHSTA-AAARAKRVLFIKDG 220
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-220 |
4.10e-56 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 189.93 E-value: 4.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKIYKTRFQgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEE--QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 SSFRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAII 161
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 162 TSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-222 |
4.91e-56 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 182.97 E-value: 4.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKtrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKD 80
Cdd:COG3839 1 MASLELENVSKSYG------GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 assfRRekLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG3839 75 ----RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 161 ITSPEILLADEPTGALDskssAAL-LDVFEDI----NSMGQTILMVTHS-TAAAARAKRVLFIKDGIL 222
Cdd:COG3839 149 VREPKVFLLDEPLSNLD----AKLrVEMRAEIkrlhRRLGTTTIYVTHDqVEAMTLADRIAVMNDGRI 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-220 |
1.65e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 178.33 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKIYktrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA 81
Cdd:COG3638 1 PMLELRNLSKRY-----PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 SSFRREkLGFVFQDFNLLDTLSVKDNILLPLvLSRRP-VKEMMSKVDSVSRELGIHQL----LEKYPY----EISGGQKQ 152
Cdd:COG3638 76 RRLRRR-IGMIFQQFNLVPRLSVLTNVLAGR-LGRTStWRSLLGLFPPEDRERALEALervgLADKAYqradQLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 153 RVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRyADRIIGLRDG 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-240 |
2.57e-55 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 180.77 E-value: 2.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 7 QHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRR 86
Cdd:PRK11153 5 KNISKVFPQG--GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 eKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDsvsrEL----GIHQLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:PRK11153 83 -QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVT----ELlelvGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQ-----IFRGEKTE-- 233
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINReLGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQgtvseVFSHPKHPlt 237
|
....*..
gi 552782194 234 RQMFQEI 240
Cdd:PRK11153 238 REFIQST 244
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-220 |
4.37e-54 |
|
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: 174.68 E-value: 4.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYktrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASS 83
Cdd:cd03256 1 IEVENLSKTY-----PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQL----LEKYPY----EISGGQKQRVA 155
Cdd:cd03256 76 LRR-QIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALervgLLDKAYqradQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 156 VARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREyADRIVGLKDG 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-220 |
1.70e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.92 E-value: 1.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVkkiyktRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkDASS 83
Cdd:COG4619 1 LELEGL------SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTlSVKDNILLPLVLSRRPVKemMSKVDSVSRELGI-HQLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:COG4619 72 WRR-QVAYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFED-INSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
2.65e-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: 170.45 E-value: 2.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKtrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTsTIKNKDASS 83
Cdd:cd03229 1 LELKNVSKRYG------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTLSVKDNILLPLvlsrrpvkemmskvdsvsrelgihqllekypyeiSGGQKQRVAVARAIITS 163
Cdd:cd03229 74 LRR-RIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-220 |
8.10e-53 |
|
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: 168.72 E-value: 8.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfRREKLGFVFQD 95
Cdd:cd03228 9 SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES----LRKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTlSVKDNILlplvlsrrpvkemmskvdsvsrelgihqllekypyeiSGGQKQRVAVARAIITSPEILLADEPTGA 175
Cdd:cd03228 85 PFLFSG-TIRENIL-------------------------------------SGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552782194 176 LDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03228 127 LDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-222 |
8.62e-53 |
|
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: 170.40 E-value: 8.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiKNKDASS 83
Cdd:cd03262 1 IEIKNLHKSFGDF------HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT--DDKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRpvkemMSKVDSVSRELgihQLLEK---------YPYEISGGQKQRV 154
Cdd:cd03262 73 ELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKG-----MSKAEAEERAL---ELLEKvgladkadaYPAQLSGGQQQRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 155 AVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTA-AAARAKRVLFIKDGIL 222
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-203 |
2.01e-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: 2.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKtrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstiknKD 80
Cdd:COG3842 3 MPALELENVSKRYG------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--------RD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRREK--LGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVAR 158
Cdd:COG3842 69 VTGLPPEKrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552782194 159 AIITSPEILLADEPTGALDSKSSAAL-LDVFEDINSMGQTILMVTH 203
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTH 194
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-220 |
3.03e-52 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 169.60 E-value: 3.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKtRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRReK 88
Cdd:cd03261 3 LRGLTK-SFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 89 LGFVFQDFNLLDTLSVKDNILLPL-VLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEIL 167
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 168 LADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTH--STAAAArAKRVLFIKDG 220
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKkELGLTSIMVTHdlDTAFAI-ADRIAVLYDG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-220 |
1.44e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.93 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTrfqgtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknKDASS 83
Cdd:COG1131 1 IEVRGLTKRYGD------KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:COG1131 71 VRR-RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKG 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-220 |
1.87e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 168.40 E-value: 1.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKiyktRFQGTQveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTikNKDAss 83
Cdd:COG1118 3 IEVRNISK----RFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT--NLPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 fRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:COG1118 73 -RERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782194 164 PEILLADEPTGALDSKSSAA----LLDVFEDInsmGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKElrrwLRRLHDEL---GGTTVFVTHDQEEALElADRVVVMNQG 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-222 |
7.08e-50 |
|
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: 162.81 E-value: 7.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTrfqgtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDass 83
Cdd:cd03301 1 VELENVTKRFGN------VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frrEKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03301 72 ---RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552782194 164 PEILLADEPTGALDSKSSAALLdvfEDINSM----GQTILMVTHS-TAAAARAKRVLFIKDGIL 222
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMR---AELKRLqqrlGTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
1.55e-49 |
|
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: 170.08 E-value: 1.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKkiykTRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPT---EGRVYLNGMDTSTIKN 78
Cdd:COG1123 3 PLLEVRDLS----VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 79 KDassfRREKLGFVFQDF-NLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVA 157
Cdd:COG1123 79 AL----RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 158 RAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEiADRVVVMDDG 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-215 |
2.74e-49 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 164.46 E-value: 2.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQP---TEGRVYLNGMDTSTIKNK 79
Cdd:COG0444 1 LLEVRNLKVYFPTR--RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 80 DASSFRREKLGFVFQD-FNLLD-TLSVKDNILLPLVLSRR-PVKEMMSKVDSVSRELGIH---QLLEKYPYEISGGQKQR 153
Cdd:COG0444 79 ELRKIRGREIQMIFQDpMTSLNpVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552782194 154 VAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVL 215
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQrELGLAILFITHDLGVVAEiADRVA 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-222 |
7.81e-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: 7.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstikNKDASS 83
Cdd:cd03230 1 IEVRNLSKRYGKK------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD-----IKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLGFVFQDFNLLDTLSVKDNILLplvlsrrpvkemmskvdsvsrelgihqllekypyeiSGGQKQRVAVARAIITS 163
Cdd:cd03230 70 EVKRRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTA-AAARAKRVLFIKDGIL 222
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-220 |
2.20e-48 |
|
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: 159.77 E-value: 2.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRFQgtqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkDASS 83
Cdd:cd03295 1 IEFENVTKRYGGGKK-----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTLSVKDNI-LLPLVLS------RRPVKEMMSKVDsvsreLGIHQLLEKYPYEISGGQKQRVAV 156
Cdd:cd03295 73 LRR-KIGYVIQQIGLFPHMTVEENIaLVPKLLKwpkekiRERADELLALVG-----LDPAEFADRYPHELSGGQQQRVGV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 157 ARAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHDIDEAFRlADRIAIMKNG 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-173 |
3.28e-48 |
|
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: 156.27 E-value: 3.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRREkLGFVFQDFNLLDTLSV 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 105 KDNILLPLVLSRRPVKEMMSKVDSVSRELGI----HQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-225 |
4.24e-48 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 158.79 E-value: 4.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKtrfQGT-QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA 81
Cdd:PRK10584 6 IVEVHHLKKSVG---QGEhELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 SSFRREKLGFVFQDFNLLDTLSVKDNILLPLVLsrRPVKEMMSKVDSVS--RELGIHQLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK10584 83 AKLRAKHVGFVFQSFMLIPTLNALENVELPALL--RGESSRQSRNGAKAllEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 160 IITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAARAKRVLFIKDGILYNQ 225
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-220 |
5.66e-48 |
|
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: 159.00 E-value: 5.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYktrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAS 82
Cdd:TIGR02315 1 MLEVENLSKVY-----PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRReKLGFVFQDFNLLDTLSVKDNIL---------LPLVLSRRPVKEMMSKVDSVSReLGIHQLLEKYPYEISGGQKQR 153
Cdd:TIGR02315 76 KLRR-RIGMIFQHYNLIERLTVLENVLhgrlgykptWRSLLGRFSEEDKERALSALER-VGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 154 VAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKyADRIVGLKAG 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-222 |
8.04e-48 |
|
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: 159.35 E-value: 8.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 21 QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRREKLGFVFQDFNLLD 100
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 TLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKS 180
Cdd:cd03294 116 HRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 552782194 181 SAALLDVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDGIL 222
Cdd:cd03294 196 RREMQDELLRLQAeLQKTIVFITHDLDEALRlGDRIAIMKDGRL 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-223 |
1.20e-47 |
|
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: 157.88 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKtRFQgtqveaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdass 83
Cdd:cd03299 1 LKVENLSKDWK-EFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03299 70 --KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHS-TAAAARAKRVLFIKDGILY 223
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLI 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-223 |
1.90e-47 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 156.96 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 7 QHVKKIYktrFQGTQveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRR 86
Cdd:PRK10908 5 EHVSKAY---LGGRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 EkLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEI 166
Cdd:PRK10908 80 Q-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 167 LLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAK-RVLFIKDGILY 223
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-203 |
5.51e-47 |
|
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: 159.43 E-value: 5.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKiyktRFQGTQveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkD 80
Cdd:TIGR03265 2 SPYLSIDNIRK----RFGAFT--ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT-----R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRREkLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:TIGR03265 71 LPPQKRD-YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 552782194 161 ITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTH 203
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDARVREHLRTEIRQLQRrLGVTTIMVTH 193
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-225 |
6.17e-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: 6.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkDASSFRReKLGFVFQD 95
Cdd:COG2274 482 RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLRR-QIGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTlSVKDNILlplvLSRRPVKemMSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSP 164
Cdd:COG2274 558 VFLFSG-TIRENIT----LGDPDAT--DEEIIEAARLAGLHDFIEALPmgYDtvvgeggsnLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 165 EILLADEPTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDGILYNQ 225
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-226 |
6.56e-47 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 155.74 E-value: 6.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQV--EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRREKLGFVF 93
Cdd:PRK11629 14 RYQEGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 94 QDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:PRK11629 94 QFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552782194 174 GALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAARAKRVLFIKDGILYNQI 226
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
8.33e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 155.42 E-value: 8.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAML-----DQPTEGRVYLNGMDTSTIkN 78
Cdd:cd03260 1 IELRDLNVYYGDK------HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDL-D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 79 KDASSFRReKLGFVFQDFNLLDtLSVKDNILLPL---------VLSRRpVKEMMSKV---DSVSRELGIHQLlekypyei 146
Cdd:cd03260 74 VDVLELRR-RVGMVFQKPNPFP-GSIYDNVAYGLrlhgiklkeELDER-VEEALRKAalwDEVKDRLHALGL-------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 147 SGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINsMGQTILMVTHSTAAAAR-AKRVLFIKDGIL 222
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK-KEYTIVIVTHNMQQAARvADRTAFLLNGRL 218
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-222 |
1.70e-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: 154.41 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASS 83
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQV--LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRR-PVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:TIGR02982 80 LRR-RIGYIFQAHNLLGFLTARQNVQMALELQPNlSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAARAKRVLFIKDGIL 222
Cdd:TIGR02982 159 HPKLVLADEPTAALDSKSGRDVVELMQKLaKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-233 |
1.99e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 154.53 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 28 IHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkDASSFRReKLGFVFQDFNLLDTLSVKDN 107
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-----ALPPAER-PVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 108 ILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDV 187
Cdd:COG3840 92 IGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552782194 188 FEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG-ILYN----QIFRGEKTE 233
Cdd:COG3840 172 VDELCrERGLTVLMVTHDPEDAARiADRVLLVADGrIAADgptaALLDGEPPP 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-220 |
4.89e-46 |
|
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: 154.92 E-value: 4.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 6 VQHVKKIY--KTRFQGTqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASS 83
Cdd:TIGR04521 3 LKNVSYIYqpGTPFEKK---ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQ--DFNLLDTLSVKD------NILLPLVLSRRPVKEMMSKVdsvsrelGI-HQLLEKYPYEISGGQKQRV 154
Cdd:TIGR04521 80 LRK-KVGLVFQfpEHQLFEETVYKDiafgpkNLGLSEEEAEERVKEALELV-------GLdEEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 155 AVARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTA-AAARAKRVLFIKDG 220
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEdVAEYADRVIVMHKG 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-220 |
6.02e-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: 6.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 27 DIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGM---DTStiKNKDASSFRReKLGFVFQDFNLLDTLS 103
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSA--RGIFLPPHRR-RIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNILLplVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAA 183
Cdd:COG4148 94 VRGNLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 552782194 184 LLDVFEDINSMGQT-ILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG4148 172 ILPYLERLRDELDIpILYVSHSLDEVARlADHVVLLEQG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-220 |
1.37e-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: 152.89 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfRREKLGFVFQD 95
Cdd:COG1120 10 GYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTLSVKDNILL---P-LVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADE 171
Cdd:COG1120 84 PPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 172 PTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARyADRLVLLKDG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-203 |
3.27e-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: 151.62 E-value: 3.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYktrfqGTQVeALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDAss 83
Cdd:cd03300 1 IELENVSKFY-----GGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD---ITNLPP-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03300 70 HKR-PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTH 203
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQkELGITFVFVTH 189
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-252 |
1.74e-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: 150.01 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKtrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdas 82
Cdd:COG4555 1 MIEVENLSKKYG------KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 sfRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:COG4555 72 --ARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQIFRGEKTERQMFQEIS 241
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
250
....*....|.
gi 552782194 242 DTLTVMAGKED 252
Cdd:COG4555 230 DAFVALIGSEE 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-234 |
1.16e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 147.85 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 8 HVKKIYKtrFQGTQvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMD---TSTIKNKDASSF 84
Cdd:COG4161 4 QLKNINC--FYGSH-QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 85 RReKLGFVFQDFNLLDTLSVKDNIL-LPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:COG4161 81 RQ-KVGMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQ----IFRGEKTER 234
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQgdasHFTQPQTEA 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-220 |
1.16e-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: 146.87 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 28 IHF--TVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkdASSFRREKLGFVFQDFNLLDTLSVK 105
Cdd:cd03298 15 MHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT------AAPPADRPVSMLFQENNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 106 DNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALL 185
Cdd:cd03298 89 QNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 552782194 186 DVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03298 169 DLVLDLHAeTKMTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
1.35e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 1.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiknkd 80
Cdd:COG1121 4 MPAIELENLTVSYGGR------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 assfRREKLGFVFQDFNLLDT--LSVKDNILLPLV----LSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRV 154
Cdd:COG1121 73 ----ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 155 AVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILY 223
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLNRGLVA 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-222 |
1.74e-43 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 146.29 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 27 DIHFTVEkGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNG---MDTStiKNKDASSFRReKLGFVFQDFNLLDTLS 103
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSR--KKINLPPQQR-KIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNILLplVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAA 183
Cdd:cd03297 92 VRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552782194 184 LLDVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDGIL 222
Cdd:cd03297 170 LLPELKQIKKnLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-222 |
2.66e-43 |
|
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: 154.15 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfRREKLGFVFQDFNLLDTl 102
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----WRRQIAWVPQNPYLFAG- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNILlplvLSRRPVKEmmSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSPEILLADE 171
Cdd:COG4988 426 TIRENLR----LGRPDASD--EELEAALEAAGLDEFVAALPdgLDtplgeggrgLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 172 PTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDGIL 222
Cdd:COG4988 500 PTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
2.81e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 147.58 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYktrfQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASs 83
Cdd:TIGR04520 1 IEVENVSFSY----PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frREKLGFVFQ--DfNLLDTLSVKD-------NILLPLvlsrrpvKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRV 154
Cdd:TIGR04520 76 --RKKVGMVFQnpD-NQFVGATVEDdvafgleNLGVPR-------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 155 AVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLADRVIVMNKG 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-203 |
4.02e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 148.73 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTR---FQGT--QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIK 77
Cdd:COG4608 7 LLEVRDLKKHFPVRgglFGRTvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 78 NKDASSFRReKLGFVFQD-FNLLDT-LSVKDNILLPLVLS--------RRPVKEMMSKVDsVSRElgiHqlLEKYPYEIS 147
Cdd:COG4608 87 GRELRPLRR-RMQMVFQDpYASLNPrMTVGDIIAEPLRIHglaskaerRERVAELLELVG-LRPE---H--ADRYPHEFS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 148 GGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTH 203
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTYLFISH 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-220 |
5.33e-43 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 145.94 E-value: 5.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 6 VQHVKKIYKtRFQgtqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdasSFR 85
Cdd:cd03296 5 VRNVSKRFG-DFV-----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 86 REKLGFVFQDFNLLDTLSVKDNILLPL----VLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAII 161
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 162 TSPEILLADEPTGALDSKSSAAL---LDVFEDinSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELrrwLRRLHD--ELHVTTVFVTHDQEEALEvADRVVVMNKG 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
8-234 |
1.48e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 145.33 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 8 HVKKIYKtRFqgTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKD----ASS 83
Cdd:COG4598 10 EVRDLHK-SF--GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FR-----REKLGFVFQDFNLLDTLSVKDNILL-PLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVA 157
Cdd:COG4598 87 RRqlqriRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 158 RAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQ-----IFRGEK 231
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDvSSHVVFLHQGRIEEQgppaeVFGNPK 246
|
...
gi 552782194 232 TER 234
Cdd:COG4598 247 SER 249
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
16-220 |
1.54e-42 |
|
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: 147.95 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRREKLGFVFQD 95
Cdd:TIGR02142 4 RFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTLSVKDNILLPLvlSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGA 175
Cdd:TIGR02142 84 ARLFPHLSVRGNLRYGM--KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552782194 176 LDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHaEFGIPILYVSHSLQEVLRlADRVVVLEDG 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-204 |
2.21e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 145.00 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTRFQgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkd 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQ--PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRReklGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:COG4525 73 GPGADR---GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 552782194 161 ITSPEILLADEPTGALDS----KSSAALLDVFEDinsMGQTILMVTHS 204
Cdd:COG4525 150 AADPRFLLMDEPFGALDAltreQMQELLLDVWQR---TGKGVFLITHS 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-220 |
4.34e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.09 E-value: 4.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkDASSFRReKLGFVFQDFNLLDTl 102
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL---TLESLRR-QIGVVPQDTFLFSG- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNILlplvLSRRPVKEmmSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSPEILLADE 171
Cdd:COG1132 429 TIRENIR----YGRPDATD--EEVEEAAKAAQAHEFIEALPdgYDtvvgergvnLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552782194 172 PTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:COG1132 503 ATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-220 |
5.82e-42 |
|
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: 141.20 E-value: 5.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdASSFRREKLGFVFQD 95
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW----DPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTlSVKDNILlplvlsrrpvkemmskvdsvsrelgihqllekypyeiSGGQKQRVAVARAIITSPEILLADEPTGA 175
Cdd:cd03246 85 DELFSG-SIAENIL-------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552782194 176 LDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-223 |
1.33e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 142.03 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 29 HFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkdASSFRREKLGFVFQDFNLLDTLSVKDNI 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT------TTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 109 LLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVF 188
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 552782194 189 EDINSMGQ-TILMVTHSTAAAAR-AKRVLFIKDGILY 223
Cdd:PRK10771 173 SQVCQERQlTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-220 |
2.17e-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: 139.88 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfRREKLGFVFQd 95
Cdd:cd03214 8 GYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 fnlldtlsvkdnillplvlsrrpvkemmskvdsVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGA 175
Cdd:cd03214 81 ---------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552782194 176 LDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03214 128 LDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARyADRVILLKDG 174
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-220 |
5.03e-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: 140.75 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 5 DVQHVKKIYKTRfqgTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdassF 84
Cdd:cd03249 2 EFKNVSFRYPSR---PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR----W 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 85 RREKLGFVFQDFNLLDTlSVKDNILLplvlSRRPVKEMMskVDSVSRELGIHQLLEKYPY-----------EISGGQKQR 153
Cdd:cd03249 75 LRSQIGLVSQEPVLFDG-TIAENIRY----GKPDATDEE--VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 154 VAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 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 ... |
23-220 |
5.34e-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: 139.70 E-value: 5.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDassfRREKLGFVFQDFNL-LDT 101
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKE----RRKSIGYVMQDVDYqLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LSVKDNILLplvlSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSS 181
Cdd:cd03226 87 DSVREELLL----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552782194 182 AALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANG 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-179 |
6.57e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 143.69 E-value: 6.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKTrFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfrrEK 88
Cdd:PRK10851 5 IANIKKS-FGRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD------RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 89 LGFVFQDFNLLDTLSVKDNILLPL-VLSR--RPVKEMMSKvdSVSRELGIHQL---LEKYPYEISGGQKQRVAVARAIIT 162
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAFGLtVLPRreRPNAAAIKA--KVTQLLEMVQLahlADRYPAQLSGGQKQRVALARALAV 153
|
170
....*....|....*..
gi 552782194 163 SPEILLADEPTGALDSK 179
Cdd:PRK10851 154 EPQILLLDEPFGALDAQ 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-220 |
9.68e-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: 139.65 E-value: 9.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkDASSFRReKLGFVFQD 95
Cdd:cd03245 11 SYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLRR-NIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTlSVKDNILL--PLVLSRRPVKemmskvdsVSRELGIHQLLEKYP-----------YEISGGQKQRVAVARAIIT 162
Cdd:cd03245 87 VTLFYG-TLRDNITLgaPLADDERILR--------AAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 163 SPEILLADEPTGALDSKSSAALldvFEDINSM--GQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERL---KERLRQLlgDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-203 |
1.02e-40 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 139.88 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKiyktRFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKnkdasS 83
Cdd:cd03219 1 LEVRGLTK----RFGG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-----P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLGFV--FQDFNLLDTLSVKDNILLP----------LVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQK 151
Cdd:cd03219 70 HEIARLGIGrtFQIPRLFPELTVLENVMVAaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552782194 152 QRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-220 |
1.80e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 139.46 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 10 KKIYKtRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiKNKDASSFRREKl 89
Cdd:PRK09493 5 KNVSK-HFGPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 90 GFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEmmsKVDSVSREL----GIHQLLEKYPYEISGGQKQRVAVARAIITSPE 165
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLRVRGASKE---EAEKQARELlakvGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKG 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
2.07e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.50 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKiyktRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNG--MDTSTIKN 78
Cdd:PRK11264 1 MSAIEVKNLVK----KFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 79 KDASSFR--REKLGFVFQDFNLLDTLSVKDNILL-PLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVA 155
Cdd:PRK11264 75 QQKGLIRqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 156 VARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQ 225
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-220 |
2.42e-40 |
|
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: 146.06 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfRREKLGFVFQD 95
Cdd:COG4987 342 RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD----LRRRIAVVPQR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTlSVKDNILLPlvlsrRP------VKEMMSKVdsvsrelGIHQLLEKYPY-----------EISGGQKQRVAVAR 158
Cdd:COG4987 418 PHLFDT-TLRENLRLA-----RPdatdeeLWAALERV-------GLGDWLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 159 AIITSPEILLADEPTGALDSKSSAALL-DVFEdiNSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLaDLLE--ALAGRTVLLITHRLAGLERMDRILVLEDG 545
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-220 |
3.37e-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: 136.22 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 6 VQHVKKIYKTRFqgtqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfR 85
Cdd:cd00267 2 IENLSFRYGGRT------ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 86 REKLGFVFQdfnlldtlsvkdnillplvlsrrpvkemmskvdsvsrelgihqllekypyeISGGQKQRVAVARAIITSPE 165
Cdd:cd00267 72 RRRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAK-RVLFIKDG 220
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAAdRVIVLKDG 156
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-220 |
3.42e-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: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstiKNKDASSFRREklgFVFQDFNLLDTLSV 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG------KQITEPGPDRM---VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNILLPL--VLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSA 182
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552782194 183 ALLDVFEDI-NSMGQTILMVTHST-AAAARAKRVLFIKDG 220
Cdd:TIGR01184 152 NLQEELMQIwEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-234 |
3.68e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.77 E-value: 3.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKtrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAs 82
Cdd:PRK13635 5 IIRVEHISFRYP----DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 sfrREKLGFVFQ--DFNLLDTlSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK13635 80 ---RRQVGMVFQnpDNQFVGA-TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 161 ITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQ-TILMVTHSTAAAARAKRVLFIKDGILYN-----QIFR-GEKTE 233
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEegtpeEIFKsGHMLQ 235
|
.
gi 552782194 234 R 234
Cdd:PRK13635 236 E 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
24-220 |
1.46e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.20 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTstikNKDASSFRREKLGFVFQD-FNLLDTL 102
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKENLKEIRKKIGIIFQNpDNQFIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSA 182
Cdd:PRK13632 100 TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 552782194 183 ALLDVFEDI-NSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PRK13632 180 EIKKIMVDLrKTRKKTLISITHDMDEAILADKVIVFSEG 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-220 |
1.79e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 137.07 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYL--NGMDTSTIKNKDASSFRREKLGFVFQDFNLLD 100
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPSDKAIRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 TLSVKDN-ILLP---LVLSRrpvKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGAL 176
Cdd:PRK11124 96 HLTVQQNlIEAPcrvLGLSK---DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552782194 177 DSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENG 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-223 |
2.78e-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: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 21 QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiknkdassfRREKLGFVFQDFNLLD 100
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 T--LSVKDNILLPLV----LSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:cd03235 82 DfpISVRDVVLMGLYghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 552782194 175 ALDSKSSAALLDVFEDINSMGQTILMVTHS-TAAAARAKRVLFIKDGILY 223
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYFDRVLLLNRTVVA 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-220 |
8.57e-39 |
|
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: 134.22 E-value: 8.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 31 TVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiknkdaSSFRREKLGFVFQDFNLLDTLSVKDNILL 110
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG------LAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 111 PLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFED 190
Cdd:TIGR01277 94 GLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|..
gi 552782194 191 INSMGQ-TILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:TIGR01277 174 LCSERQrTLLMVTHHLSDARAiASQIAVVSQG 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
1.54e-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: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdass 83
Cdd:cd03263 1 LQIRNLTKTYKKG----TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 fRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03263 73 -ARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSmGQTILMVTHSTA-AAARAKRVLFIKDGILY 223
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDeAEALCDRIAIMSDGKLR 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-203 |
3.17e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.38 E-value: 3.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKiyktRFQGTQveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStIKN-K 79
Cdd:COG1129 2 EPLLEMRGISK----SFGGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSpR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 80 DAssfRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPV---KEMMSKVDSVSRELGIH----QLLEkypyEISGGQKQ 152
Cdd:COG1129 75 DA---QAAGIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDidpdTPVG----DLSVAQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 153 RVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-220 |
4.20e-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: 133.38 E-value: 4.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkDASSFRREkLGFVFQD 95
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ-VGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 fNLLDTLSVKDNILLPlvlsrRPVKEmMSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSP 164
Cdd:cd03252 85 -NVLFNRSIRDNIALA-----DPGMS-MERVIEAAKLAGAHDFISELPegYDtivgeqgagLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 165 EILLADEPTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-220 |
6.21e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 133.26 E-value: 6.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdass 83
Cdd:PRK11247 13 LLLNAVSKRYGER------TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPvkEMMSKVDSVsrelGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:PRK11247 80 --REDTRLMFQDARLLPWKKVIDNVGLGLKGQWRD--AALQALAAV----GLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTA-AAARAKRVLFIKDG 220
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-214 |
6.57e-38 |
|
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: 131.83 E-value: 6.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKiyktRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstiKNKDA 81
Cdd:COG4133 1 MMLEAENLSC----RRGERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP----IRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 SSFRREkLGFVFQDFNLLDTLSVKDNI-----LLPLVLSRRPVKEMMSKVdsvsrelGIHQLLEKYPYEISGGQKQRVAV 156
Cdd:COG4133 71 EDYRRR-LAYLGHADGLKPELTVRENLrfwaaLYGLRADREAIDEALEAV-------GLAGLADLPVRQLSAGQKRRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 157 ARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRV 214
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
7.37e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.99 E-value: 7.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 5 DVQHVKKiYKTRFQGtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYL-NGMDTSTIKNKDASS 83
Cdd:PRK13634 7 KVEHRYQ-YKTPFER---RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQ--DFNLLDTLSVKD------NILLPLVLSRRPVKEMMSKVdsvsrelGI-HQLLEKYPYEISGGQKQRV 154
Cdd:PRK13634 83 LRK-KVGIVFQfpEHQLFEETVEKDicfgpmNFGVSEEDAKQKAREMIELV-------GLpEELLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 155 AVARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDGilynQIFRgEKT 232
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARyADQIVVMHKG----TVFL-QGT 229
|
....*..
gi 552782194 233 ERQMFQE 239
Cdd:PRK13634 230 PREIFAD 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-203 |
7.66e-38 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 133.24 E-value: 7.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKiyktRFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkD 80
Cdd:COG0411 2 DPLLEVRGLTK----RFGG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-----G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRREKLGFV--FQDFNLLDTLSVKDNI---------------LLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYP 143
Cdd:COG0411 71 LPPHRIARLGIArtFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 144 YEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTH 203
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEH 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-177 |
1.70e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 132.27 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTR---FQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMdtsTIK 77
Cdd:COG4167 2 SALLEVRNLSKTFKYRtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 78 NKDASsFRREKLGFVFQDFNllDTLSVKDNI--LL--PLVLSrrpvkemmSKVDSVSRELGIHQLLEK----------YP 143
Cdd:COG4167 79 YGDYK-YRCKHIRMIFQDPN--TSLNPRLNIgqILeePLRLN--------TDLTAEEREERIFATLRLvgllpehanfYP 147
|
170 180 190
....*....|....*....|....*....|....
gi 552782194 144 YEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-220 |
3.28e-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: 130.81 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 8 HVKKIYKTRFQgtqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRRe 87
Cdd:cd03253 5 NVTFAYDPGRP-----VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 88 KLGFVFQDFNLLDTlSVKDNILLplvlSRRPVKEmmSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAV 156
Cdd:cd03253 76 AIGVVPQDTVLFND-TIGYNIRY----GRPDATD--EEVIEAAKAAQIHDKIMRFPdgYDtivgerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552782194 157 ARAIITSPEILLADEPTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-241 |
6.27e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 131.36 E-value: 6.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 13 YKTRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNK-DAssfrREKLGF 91
Cdd:PRK13633 14 YESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDI----RNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 92 VFQ--DFNLLDTLSVKDNILLPLVLSRRPvKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLA 169
Cdd:PRK13633 90 VFQnpDNQIVATIVEEDVAFGPENLGIPP-EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 170 DEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAARAKRVLFIKDGILYNqifrgEKTERQMFQEIS 241
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSGKVVM-----EGTPKEIFKEVE 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-177 |
7.27e-37 |
|
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: 135.97 E-value: 7.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTR---FQGT--QVEALKDIHFTVEKGEYVAIMGESGSGKSTL-LNILAMLdqPTEGRVYLNGMDTSTI 76
Cdd:COG4172 275 LLEARDLKVWFPIKrglFRRTvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 77 KNKDASSFRREkLGFVFQD-FNLLDT-LSVKDNILLPLVLSRRPV--KEMMSKVDSVSRELGIH-QLLEKYPYEISGGQK 151
Cdd:COG4172 353 SRRALRPLRRR-MQVVFQDpFGSLSPrMTVGQIIAEGLRVHGPGLsaAERRARVAEALEEVGLDpAARHRYPHEFSGGQR 431
|
170 180
....*....|....*....|....*.
gi 552782194 152 QRVAVARAIITSPEILLADEPTGALD 177
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALD 457
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-220 |
7.47e-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: 7.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdASSFRREKLGFVFQD 95
Cdd:TIGR03375 472 AYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI----DPADLRRNIGYVPQD 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLdTLSVKDNILLplvlsRRPV---KEMMSKVDSVsrelGIHQLLEKYP--YE---------ISGGQKQRVAVARAII 161
Cdd:TIGR03375 548 PRLF-YGTLRDNIAL-----GAPYaddEEILRAAELA----GVTEFVRRHPdgLDmqigergrsLSGGQRQAVALARALL 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 162 TSPEILLADEPTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNG 675
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-203 |
1.16e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 132.01 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTR---FQGT-QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTsTI 76
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKrglFKPErLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-LK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 77 KNKDASSFRREKLGFVFQdfNLLDTLS----VKDNILLPLV----LS----RRPVKEMMSKVdsvsrelGI---HqlLEK 141
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQ--NPYGSLNprkkVGQILEEPLLintsLSaaerREKALAMMAKV-------GLrpeH--YDR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 142 YPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTH 203
Cdd:PRK11308 151 YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLqQELGLSYVFISH 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-229 |
1.29e-36 |
|
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: 129.02 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 8 HVKKIYKtRFQ--GTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiKNKDASsfr 85
Cdd:cd03266 3 TADALTK-RFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--KEPAEA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 86 REKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPE 165
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILynqIFRG 229
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRV---VYEG 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-208 |
4.68e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.50 E-value: 4.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRFqgtqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkDAS 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQH------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:PRK11607 88 PYQR-PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552782194 163 SPEILLADEPTGALDSKSSAAL-LDVFEDINSMGQTILMVTHSTAAA 208
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEA 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-245 |
1.23e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.46 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNIL-AMLD-QP---TEGRVYLNGMDTSTiKNKDASSFRReKLGFVFQDFN 97
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLnRMNDlIPgarVEGEILLDGEDIYD-PDVDVVELRR-RVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 98 LLdTLSVKDNILLPL-VLSRRPVKEMMSKVDSVSRELGihqL-------LEKYPYEISGGQKQRVAVARAIITSPEILLA 169
Cdd:COG1117 103 PF-PKSIYDNVAYGLrLHGIKSKSELDEIVEESLRKAA---LwdevkdrLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 170 DEPTGALDSKSSAALldvfED-INSMGQ--TILMVTHSTAAAAR-AKRVLFIKDGIL--YNqifrgeKTErQMFQEISDT 243
Cdd:COG1117 179 DEPTSALDPISTAKI----EElILELKKdyTIVIVTHNMQQAARvSDYTAFFYLGELveFG------PTE-QIFTNPKDK 247
|
..
gi 552782194 244 LT 245
Cdd:COG1117 248 RT 249
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-215 |
2.69e-35 |
|
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: 131.64 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKnkdaSSFRREKLGFVFQDFNLLDTl 102
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNILlplvLSRRPVKEMMSK-------VDSVSREL--GIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:TIGR02857 411 TIAENIR----LARPDASDAEIRealeragLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552782194 174 GALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAARAKRVL 215
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIV 527
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-220 |
3.24e-35 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 125.24 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKtrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkDASS 83
Cdd:cd03224 1 LEVENLNAGYG------KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-----GLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLG--FVFQDFNLLDTLSVKDNILLPL-VLSRRPVKEMMSKVDSVSRELgiHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:cd03224 70 HERARAGigYVPEGRRIFPELTVEENLLLGAyARRRAKRKARLERVYELFPRL--KERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 161 ITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERG 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-225 |
4.94e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 125.85 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 21 QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAS---------SFRREKLGF 91
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 92 VFQDFNLLDTLSVKDNILlplvlsRRPVKEM-MSKVDSVSR------ELGIHQLLE-KYPYEISGGQKQRVAVARAIITS 163
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVM------EAPIQVLgLSKQEARERavkylaKVGIDERAQgKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQ 225
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-220 |
5.09e-35 |
|
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: 125.03 E-value: 5.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQDFNLLDTlS 103
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNILlplvLSRRPVKEmmSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSPEILLADEP 172
Cdd:cd03254 93 IMENIR----LGRPNATD--EEVIEAAKEAGAHDFIMKLPngYDtvlgenggnLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 552782194 173 TGALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-215 |
5.39e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.52 E-value: 5.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLN-ILAMLDQP--TEGRVYLNGMDTSTIKNkdassfRREKLGFVFQDFNLLDT 101
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPA------EQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LSVKDNIL--LPLVLSRRPVKEMmskVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDsk 179
Cdd:COG4136 91 LSVGENLAfaLPPTIGRAQRRAR---VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552782194 180 ssAALLD-----VFEDINSMGQTILMVTHSTAAAARAKRVL 215
Cdd:COG4136 166 --AALRAqfrefVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-203 |
1.69e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.38 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKtRFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTsTIKN-KDAssfRRE 87
Cdd:COG3845 8 LRGITK-RFGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSpRDA---IAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 88 KLGFVFQDFNLLDTLSVKDNILL---PLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSP 164
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 552782194 165 EILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-220 |
2.92e-34 |
|
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: 129.10 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 19 GTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIkNKDAssfRREKLGFVFQDFNL 98
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-DREE---LGRHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 99 LDTlSVKDNIllplvlSRrpvkemMSKVDSVS-----RELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIIT 162
Cdd:COG4618 418 FDG-TIAENI------AR------FGDADPEKvvaaaKLAGVHEMILRLPdgYDtrigeggarLSGGQRQRIGLARALYG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-244 |
5.40e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.00 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 6 VQHVKKIYktrFQGTQVE--ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDAS- 82
Cdd:PRK13637 5 IENLTHIY---MEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD---ITDKKVKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRREKLGFVFQ--DFNLLDTLSVKDNILLP--LVLS----RRPVKEMMSKVDsvsreLGIHQLLEKYPYEISGGQKQRV 154
Cdd:PRK13637 79 SDIRKKVGLVFQypEYQLFEETIEKDIAFGPinLGLSeeeiENRVKRAMNIVG-----LDYEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 155 AVARAIITSPEILLADEPTGALDSKSSAallDVFEDINSMGQ----TILMVTHSTAAAAR-AKRVLFIKDGILynqIFRG 229
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRD---EILNKIKELHKeynmTIILVSHSMEDVAKlADRIIVMNKGKC---ELQG 227
|
250
....*....|....*
gi 552782194 230 ekTERQMFQEIsDTL 244
Cdd:PRK13637 228 --TPREVFKEV-ETL 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-205 |
6.64e-34 |
|
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: 121.12 E-value: 6.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAML--DQPTEGRVYLNGmdtstiKNKDASSFRREkLGFVFQDFNLLDTL 102
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLING------RPLDKRSFRKI-IGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNILLPLVLSRrpvkemmskvdsvsrelgihqllekypyeISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSA 182
Cdd:cd03213 98 TVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180
....*....|....*....|...
gi 552782194 183 ALLDVFEDINSMGQTILMVTHST 205
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHQP 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-220 |
1.00e-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: 121.95 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKnkdASSFRReKLGFVFQD 95
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRR-QIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTlSVKDNILlplvLSRRpvKEMMSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSP 164
Cdd:cd03251 85 VFLFND-TVAENIA----YGRP--GATREEVEEAARAANAHEFIMELPegYDtvigergvkLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 165 EILLADEPTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDG 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-220 |
1.74e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 122.89 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKTRFQGTQVE--ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA----- 81
Cdd:PRK13651 5 VKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEkekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 -------SSFR--------REKLGFVFQ--DFNLLDTLSVKDNILLPLVLSrrpvkemMSKVDSVSRELGIHQL------ 138
Cdd:PRK13651 85 eklviqkTRFKkikkikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMG-------VSKEEAKKRAAKYIELvgldes 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 139 -LEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHS-TAAAARAKRVLF 216
Cdd:PRK13651 158 yLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIF 237
|
....
gi 552782194 217 IKDG 220
Cdd:PRK13651 238 FKDG 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-220 |
3.45e-33 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 118.30 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKtRFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkdassfrrek 88
Cdd:cd03216 3 LRGITK-RFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 89 lgfvfqdfnlldTLSVKDnillplvlsrrpvkemmskvdsvSRELGI---HQLlekypyeiSGGQKQRVAVARAIITSPE 165
Cdd:cd03216 66 ------------FASPRD-----------------------ARRAGIamvYQL--------SVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-235 |
4.23e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 126.76 E-value: 4.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 7 QHVKKIYKTRfqgTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdassFRR 86
Cdd:TIGR00958 482 QDVSFSYPNR---PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH----YLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 EKLGFVFQDfNLLDTLSVKDNILLPlvLSRRPVKEMMskvdSVSRELGIHQLLEKYPYEI-----------SGGQKQRVA 155
Cdd:TIGR00958 555 RQVALVGQE-PVLFSGSVRENIAYG--LTDTPDEEIM----AAAKAANAHDFIMEFPNGYdtevgekgsqlSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 156 VARAIITSPEILLADEPTGALDSKSSAALldvFEDINSMGQTILMVTHSTAAAARAKRVLFIKDGILYNQIFRGEKTERQ 235
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLL---QESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-203 |
1.34e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 120.23 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYK--TRFQGtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMD-TSTIKNKD 80
Cdd:PRK13649 3 INLQNVSYTYQagTPFEG---RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRReKLGFVFQ--DFNLLDTLSVKDNILLPLVLSRRPvkemmSKVDSVSRE----LGIHQ-LLEKYPYEISGGQKQR 153
Cdd:PRK13649 80 IKQIRK-KVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-----EEAEALAREklalVGISEsLFEKNPFELSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 552782194 154 VAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-220 |
4.87e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 121.29 E-value: 4.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRREKLGFVFQDFNLLDTLS 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAA 183
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 552782194 184 LLDVFEDINSMGQ-TILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK10070 203 MQDELVKLQAKHQrTIVFISHDLDEAMRiGDRIAIMQNG 241
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-222 |
6.02e-32 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 116.70 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKtrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknKDASS 83
Cdd:cd03265 1 IEVENLVKKYG------DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03265 71 VRR-RIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAA-ARAKRVLFIKDGIL 222
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAeQLCDRVAIIDHGRI 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-180 |
7.84e-32 |
|
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: 116.87 E-value: 7.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdaSS 83
Cdd:cd03218 1 LRAENLSKRYGKR------KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-----PM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLGFVF--QDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAII 161
Cdd:cd03218 70 HKRARLGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170
....*....|....*....
gi 552782194 162 TSPEILLADEPTGALDSKS 180
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIA 168
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-203 |
8.99e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 118.30 E-value: 8.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMD-TSTIKNKDASSFRReKLGFVFQ--DFNLLD 100
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvSSTSKQKEIKPVRK-KVGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 TLSVKDNILLPLVLSRRpvKEMMSKVDSVSREL-GI-HQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDS 178
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIP--KEKAEKIAAEKLEMvGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180
....*....|....*....|....*
gi 552782194 179 KSSAALLDVFEDINSMGQTILMVTH 203
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
9.56e-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: 122.10 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKkiykTRFQ--GTQVEALKDIHFTVEKGEYVAIMGESGSGKS-TLLNILAMLDQP---TEGRVYLNGMDTS 74
Cdd:COG4172 4 MPLLSVEDLS----VAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 75 TIKNKDASSFRREKLGFVFQD----FNLLDTlsVKDNILLPLVLSRRpvkemMSKVDSVSR--EL----GIH---QLLEK 141
Cdd:COG4172 80 GLSERELRRIRGNRIAMIFQEpmtsLNPLHT--IGKQIAEVLRLHRG-----LSGAAARARalELlervGIPdpeRRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 142 YPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAAR-AKRVLFIKD 219
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
.
gi 552782194 220 G 220
Cdd:COG4172 233 G 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-220 |
9.70e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 119.59 E-value: 9.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 39 AIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRREKLGFVFQDFNLLDTLSVKDNILLPLVlsrrp 118
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 119 vKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFE----DINSm 194
Cdd:PRK11144 103 -KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLErlarEINI- 180
|
170 180
....*....|....*....|....*..
gi 552782194 195 gqTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK11144 181 --PILYVSHSLDEILRlADRVVVLEQG 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-220 |
1.73e-31 |
|
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: 118.37 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 40 IMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdassfrREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPV 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 120 KEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTI 198
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIqEQLGITF 154
|
170 180
....*....|....*....|...
gi 552782194 199 LMVTHSTAAA-ARAKRVLFIKDG 220
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKG 177
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-220 |
3.19e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.32 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKT-----RFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTST 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgKHQHQTV--LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 76 IKNKDASSFRREkLGFVFQD----FNllDTLSVKDNILLPL----VLSRRpvkEMMSKVDSVSRELGIH-QLLEKYPYEI 146
Cdd:PRK10419 79 LNRAQRKAFRRD-IQMVFQDsisaVN--PRKTVREIIREPLrhllSLDKA---ERLARASEMLRAVDLDdSVLDKRPPQL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 147 SGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERfCQRVMVMDNG 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-220 |
4.16e-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: 114.84 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKiyktRF-----QGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLN----GMD 72
Cdd:COG4778 3 TLLEVENLSK----TFtlhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 73 TSTIKNKDASSFRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLL-EKYPYEISGGQK 151
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 152 QRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
4.52e-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: 115.18 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKkiykTRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVY------LNGMDTS 74
Cdd:COG1119 1 DPLLELRNVT----VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 75 TIknkdassfrREKLGFVFQDF--NLLDTLSVKDnillpLVLS---------RRPVKEMMSKVDSVSRELGIHQLLEKYP 143
Cdd:COG1119 75 EL---------RKRIGLVSPALqlRFPRDETVLD-----VVLSgffdsiglyREPTDEQRERARELLELLGLAHLADRPF 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 144 YEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQ-TILMVTHSTAAAARA-KRVLFIKDG 220
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGiTHVLLLKDG 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-231 |
9.26e-31 |
|
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: 114.90 E-value: 9.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKIYKT-----RFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTI 76
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPV--LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 77 KNKDASSFRREkLGFVFQD----FNllDTLSVKDNILLPLV-LSRRPVKEMMSKVDSVSRELGIH-QLLEKYPYEISGGQ 150
Cdd:TIGR02769 79 DRKQRRAFRRD-VQLVFQDspsaVN--PRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 151 KQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQIFR 228
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQaFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDV 235
|
...
gi 552782194 229 GEK 231
Cdd:TIGR02769 236 AQL 238
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-222 |
1.79e-30 |
|
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: 118.60 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRReKLGFVFQDFNLLDTlSV 104
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAD---LKQWDRETFGK-HIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNIllplvlSRRPVKEMMSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:TIGR01842 409 AENI------ARFGENADPEKIIEAAKLAGVHELILRLPdgYDtvigpggatLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552782194 174 GALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDGIL 222
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-203 |
1.88e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 116.10 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTRFQgtqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKD 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ-----VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 assfrREkLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK11650 76 -----RD-IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 552782194 161 ITSPEILLADEPTGALDSKSSAAL-LDVFEDINSMGQTILMVTH 203
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMrLEIQRLHRRLKTTSLYVTH 193
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-215 |
2.06e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.94 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstiknkdassfrREKLGFVFQDFNLLDTL- 102
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 -SVKDNILL----PLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:NF040873 72 lTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 552782194 178 SKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVL 215
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-220 |
2.11e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 113.95 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 6 VQHVKKIYKTrFQgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAML---DQPTEGRVYLNGmDTSTIKNKDAS 82
Cdd:PRK09984 4 IIRVEKLAKT-FN--QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLG-RTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFR--REKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQL----LEKYPYE----ISGGQKQ 152
Cdd:PRK09984 80 DIRksRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALtrvgMVHFAHQrvstLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 153 RVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSM-GQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-204 |
3.25e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 113.26 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKTRFQGT--QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdaSSFRR 86
Cdd:COG1101 4 LKNLSKTFNPGTvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-----PEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 EKL-GFVFQDfNLLDT---LSVKDNILL--------PLVLS-----RRPVKEMMSKVDsvsreLGihqlLEKYPYE---- 145
Cdd:COG1101 79 AKYiGRVFQD-PMMGTapsMTIEENLALayrrgkrrGLRRGltkkrRELFRELLATLG-----LG----LENRLDTkvgl 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 146 ISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQ-TILMVTHS 204
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHN 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-179 |
4.37e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.43 E-value: 4.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 12 IYKTrFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkDASSFRREkLGF 91
Cdd:PRK09452 20 ISKS-FDGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVPAENRH-VNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 92 VFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADE 171
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
....*...
gi 552782194 172 PTGALDSK 179
Cdd:PRK09452 171 SLSALDYK 178
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-203 |
9.91e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.10 E-value: 9.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKkiykTRFQGTqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstIKNKDAS 82
Cdd:PRK11248 1 MLQISHLY----ADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRreklGFVFQDFNLLDTLSVKDNILLPLVLS------RRPV-KEMMSKVDSVSRElgihqllEKYPYEISGGQKQRVA 155
Cdd:PRK11248 70 AER----GVVFQNEGLLPWRNVQDNVAFGLQLAgvekmqRLEIaHQMLKKVGLEGAE-------KRYIWQLSGGQRQRVG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552782194 156 VARAIITSPEILLADEPTGALDS----KSSAALLDVFEDinsMGQTILMVTH 203
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAftreQMQTLLLKLWQE---TGKQVLLITH 187
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-220 |
1.01e-29 |
|
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: 110.75 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYvAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknKDASS 83
Cdd:cd03264 1 LQLENLTKRYGKK------RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRReKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03264 70 LRR-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDInSMGQTILMVTHSTA-AAARAKRVLFIKDG 220
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEdVESLCNQVAVLNKG 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-172 |
1.02e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 111.27 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkD 80
Cdd:COG1137 1 MMTLEAENLVKSYGKR------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-----H 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRREKLGF--------VFQDfnlldtLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQ 152
Cdd:COG1137 70 LPMHKRARLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180
....*....|....*....|
gi 552782194 153 RVAVARAIITSPEILLADEP 172
Cdd:COG1137 144 RVEIARALATNPKFILLDEP 163
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-224 |
1.09e-29 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 111.27 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKTRFQgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdassFRReK 88
Cdd:cd03267 23 LKSLFKRKYR--EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK----FLR-R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 89 LGFVF-QDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEIL 167
Cdd:cd03267 96 IGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 168 LADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTHSTA-AAARAKRVLFIKDG-ILYN 224
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKdIEALARRVLVIDKGrLLYD 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-220 |
1.61e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 113.66 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 10 KKIYKtRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDT--STIKNKDassfrre 87
Cdd:PRK11432 10 KNITK-RFGSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 88 kLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEIL 167
Cdd:PRK11432 80 -ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 168 LADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTH-STAAAARAKRVLFIKDG 220
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQqQFNITSLYVTHdQSEAFAVSDTVIVMNKG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-220 |
2.29e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 111.37 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTstikNKDASSFRREKLGFVFQD-FNLLDT 101
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV----NAENEKWVRSKVGLVFQDpDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LSVKDNILL-PLVLSRRPvKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKS 180
Cdd:PRK13647 95 STVWDDVAFgPVNMGLDK-DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552782194 181 SAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-235 |
3.20e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.94 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtSTIKNKDASSFR-REKLGFVFQdfNLLDT 101
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG---EPIKYDKKSLLEvRKTVGIVFQ--NPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 L---SVKDNILL-PLVLSRrPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:PRK13639 91 LfapTVEEDVAFgPLNLGL-SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552782194 178 SKSSAALLDVFEDINSMGQTILMVTHST-AAAARAKRVLFIKDG-ILYN----QIFRGEKTERQ 235
Cdd:PRK13639 170 PMGASQIMKLLYDLNKEGITIIISTHDVdLVPVYADKVYVMSDGkIIKEgtpkEVFSDIETIRK 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-220 |
4.47e-29 |
|
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: 109.48 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRfQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdas 82
Cdd:cd03248 11 IVKFQNVTFAYPTR-PDTLV--LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 sFRREKLGFVFQDfNLLDTLSVKDNILLPLvlsrrPVKEMMsKVDSVSRELGIH---QLLEKYPYE--------ISGGQK 151
Cdd:cd03248 85 -YLHSKVSLVGQE-PVLFARSLQDNIAYGL-----QSCSFE-CVKEAAQKAHAHsfiSELASGYDTevgekgsqLSGGQK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 152 QRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-220 |
8.01e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.08 E-value: 8.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkDASSFR--REKLGFVFQ--DFNLL 99
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-----DFSKLQgiRKLVGIVFQnpETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 DTLSVKDNILLPLVLSRRPVkEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSK 179
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPI-EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552782194 180 SSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PRK13644 171 SGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-210 |
8.36e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 109.23 E-value: 8.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAML-----DQPTEGRVYLNGMDtstIKNKDASSFRReKLG 90
Cdd:PRK14247 10 KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQD---IFKMDVIELRR-RVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 91 FVFQDFNLLDTLSVKDNILLPLVLSRRpVKEMMSKVDSVSRELGIHQLLEKY-------PYEISGGQKQRVAVARAIITS 163
Cdd:PRK14247 86 MVFQIPNPIPNLSIFENVALGLKLNRL-VKSKKELQERVRWALEKAQLWDEVkdrldapAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAAR 210
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAAR 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-220 |
9.17e-29 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 107.40 E-value: 9.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdassfRREKLGFVFQDFNLLDTlS 103
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQRPYLFDT-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNILLPLvlsrrpvkemmskvdsvsrelgihqllekypyeiSGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAA 183
Cdd:cd03247 91 LRNNLGRRF----------------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 552782194 184 LLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03247 137 LLSLIFEV-LKDKTLIWITHHLTGIEHMDKILFLENG 172
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-222 |
1.80e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.53 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 19 GTQVEA--LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMD-TSTIKNKDASSFRReKLGFVFQ- 94
Cdd:PRK13641 15 GTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHiTPETGNKNLKKLRK-KVSLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 95 -DFNLLDTLSVKDNILLPLVLSRRPvKEMMSKVDSVSRELGI-HQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEP 172
Cdd:PRK13641 94 pEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 173 TGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGIL 222
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-225 |
1.93e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.07 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNgmdTSTIKNKDASSFRrEKLGFVFQD 95
Cdd:PRK13648 16 QYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN---NQAITDDNFEKLR-KHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 -FNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552782194 175 ALDSKSSAALLDVFEDINSMGQ-TILMVTHSTAAAARAKRVLFIKDGILYNQ 225
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-240 |
2.03e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTrfqgTQVEALKDIHFTVEKGEYVAIMGESGSGKST---LLNILAMLDQPTEGRVYLNGMDTSTIKNKD 80
Cdd:PRK13640 6 VEFKHVSFTYPD----SKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 AssfrREKLGFVFQD-FNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK13640 82 I----REKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 160 IITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAARAKRVLFIKDGILYNQ-----IFrgEKTE 233
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQgspveIF--SKVE 235
|
....*..
gi 552782194 234 rqMFQEI 240
Cdd:PRK13640 236 --MLKEI 240
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-203 |
2.45e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.50 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 26 KDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASsfrrekLGFVFQDFNLLDTLSVK 105
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------VGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 106 DNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDskssaALL 185
Cdd:PRK11000 94 ENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD-----AAL 168
|
170 180
....*....|....*....|....
gi 552782194 186 DVFEDI------NSMGQTILMVTH 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 |
2.96e-28 |
|
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: 106.92 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiKNKDAss 83
Cdd:cd03268 1 LKTNDLTKTYGKK------RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEA-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEmmskVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03268 71 --LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH 184
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-246 |
3.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.28 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKtrfQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmDTSTIKNkd 80
Cdd:PRK13650 2 SNIIEVKNLTFKYK---EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEEN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 aSSFRREKLGFVFQD-FNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK13650 76 -VWDIRHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 160 IITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAARAKRVLFIKDGilynQIfRGEKTERQMFQ 238
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEVALSDRVLVMKNG----QV-ESTSTPRELFS 229
|
....*...
gi 552782194 239 EISDTLTV 246
Cdd:PRK13650 230 RGNDLLQL 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-203 |
4.25e-28 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 106.97 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 18 QGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQP---TEGRVYLNGMDTSTIKNKDASSFrreklgfVFQ 94
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAY-------VRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 95 DFNLLDTLSVKD------NILLPlVLSRRPVKEMMSkVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILL 168
Cdd:cd03234 89 DDILLPGLTVREtltytaILRLP-RKSSDAIRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 552782194 169 ADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-204 |
5.62e-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: 111.30 E-value: 5.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkDASSFRReKLGFVFQDFNLLDTl 102
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL---DQDEVRR-RVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNILLPlvlsrRPV---KEMMSKVDSV-------SRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEP 172
Cdd:TIGR02868 424 TVRENLRLA-----RPDatdEELWAALERVgladwlrALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|..
gi 552782194 173 TGALDSKSSAALLDVFEDINSmGQTILMVTHS 204
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALS-GRTVVLITHH 529
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-223 |
6.32e-28 |
|
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: 106.46 E-value: 6.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 22 VEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdassfrreKLGFVFQdfnllDT 101
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----------GLGGGFN-----PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LSVKDNILLPLVLSRRPVKEMMSKVDSVSR--ELG--IHQLLEKYpyeiSGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEfsELGdfIDLPVKTY----SSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552782194 178 SKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILY 223
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
1.32e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.93 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MA-LLDVQHVKKIYKTRFQGTQ----------------VEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTE 63
Cdd:COG1134 1 MSsMIEVENVSKSYRLYHEPSRslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 64 GRVYLNG-----MDTSTiknkdassfrreklGFVFQdfnlldtLSVKDNILLP---LVLSRRPVKEMMSKVDSVSrELG- 134
Cdd:COG1134 81 GRVEVNGrvsalLELGA--------------GFHPE-------LTGRENIYLNgrlLGLSRKEIDEKFDEIVEFA-ELGd 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 135 -IHQLLEKYpyeiSGGQKQRVAVARAIITSPEILLADEPTGALDS----KSSAALLDVFEDinsmGQTILMVTHSTAAAA 209
Cdd:COG1134 139 fIDQPVKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIRELRES----GRTVIFVSHSMGAVR 210
|
250
....*....|....
gi 552782194 210 R-AKRVLFIKDGIL 222
Cdd:COG1134 211 RlCDRAIWLEKGRL 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-220 |
1.51e-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: 105.06 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTrfqgtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstiKNKDASS 83
Cdd:cd03269 1 LEVENVTKRFGR------VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:cd03269 69 --RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-201 |
1.54e-27 |
|
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: 105.45 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKtrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkD 80
Cdd:COG0410 1 MPMLEVENLHAGYG------GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-----G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRREKLGFVF--QDFNLLDTLSVKDNILLPLVL--SRRPVKEMMSKVdsvsrelgihqllekypYEI---------- 146
Cdd:COG0410 70 LPPHRIARLGIGYvpEGRRIFPSLTVEENLLLGAYArrDRAEVRADLERV-----------------YELfprlkerrrq 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 147 -----SGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMV 201
Cdd:COG0410 133 ragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLV 192
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-220 |
2.85e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 109.67 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdasSFRReKLGFVFQDFNLLDTlS 103
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA---SLRR-NIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNIL----------LPLVLSRRPVKEMMSKvdsvsRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:PRK13657 425 IEDNIRvgrpdatdeeMRAAAERAQAHDFIER-----KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552782194 174 GALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PRK13657 500 SALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-239 |
6.28e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.25 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKtrfQGT--QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMdTSTIKNKDaSSFR- 85
Cdd:PRK13646 8 VSYTYQ---KGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDI-TITHKTKD-KYIRp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 86 -REKLGFVFQ--DFNLLDTlSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQ-LLEKYPYEISGGQKQRVAVARAII 161
Cdd:PRK13646 83 vRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 162 TSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQIfrgekTERQMFQE 239
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQT-----SPKELFKD 236
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-225 |
8.61e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.39 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 18 QGTQveALKDIHFTVEKGEYVAIMGESGSGKSTLLN-ILAMLdqPTEGRVYLNGMDTSTIknkDASSFRReKLGFVFQDF 96
Cdd:PRK11174 361 DGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELREL---DPESWRK-HLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 NLLDTlSVKDNILLPlvlsrrpvKEMMS--KVDSVSRELGIHQLLEKYP----YEI-------SGGQKQRVAVARAIITS 163
Cdd:PRK11174 433 QLPHG-TLRDNVLLG--------NPDASdeQLQQALENAWVSEFLPLLPqgldTPIgdqaaglSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDiNSMGQTILMVTHSTAAAARAKRVLFIKDGILYNQ 225
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-203 |
8.98e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.58 E-value: 8.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTrfQGTQVEALKDIHFTVEKGEYVAIMGESGSGKS----TLLNILAMlDQPTEGRVYLNGMDTSTI 76
Cdd:PRK09473 10 DALLDVKDLRVTFST--PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 77 KNKDASSFRREKLGFVFQD--FNLLDTLSVKDNILLPLVLSRRpvkemMSKVDSVSRELGI---------HQLLEKYPYE 145
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKG-----MSKAEAFEESVRMldavkmpeaRKRMKMYPHE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 146 ISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTH 203
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITH 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-220 |
1.19e-26 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 102.55 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstiknkdassfrreKLGFVFQDFNLLDTlS 103
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------------SIAYVSQEPWIQNG-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNILLPLVLSrrpvKEMMSKVdsvsrelgIH--QL---LEKYP----YEI-------SGGQKQRVAVARAIITSPEIL 167
Cdd:cd03250 82 IRENILFGKPFD----EERYEKV--------IKacALepdLEILPdgdlTEIgekginlSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 168 LADEPTGALDSKSSAALldvFED-INSMGQ---TILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03250 150 LLDDPLSAVDAHVGRHI---FENcILGLLLnnkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-220 |
1.64e-26 |
|
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: 107.60 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRREkLGFVFQD---FNllDT 101
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD---IRDVTQASLRAA-IGIVPQDtvlFN--DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LsvKDNILLPlvlsrRPvKEMMSKVDSVSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSPEILLAD 170
Cdd:COG5265 448 I--AYNIAYG-----RP-DASEEEVEAAARAAQIHDFIESLPdgYDtrvgerglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552782194 171 EPTGALDSKSSAALLDVFEDInSMGQTILMVTH--STaaAARAKRVLFIKDG 220
Cdd:COG5265 520 EATSALDSRTERAIQAALREV-ARGRTTLVIAHrlST--IVDADEILVLEAG 568
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-215 |
1.73e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.48 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKkiyktrFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDa 81
Cdd:PRK10247 6 PLLQLQNVG------YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 ssfRREKLGFVFQDFNLL-DTlsVKDNILLPLVLsRRPVKEMMSKVDSVSR-ELGIHqLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK10247 79 ---YRQQVSYCAQTPTLFgDT--VYDNLIFPWQI-RNQQPDPAIFLDDLERfALPDT-ILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 160 IITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQ-TILMVTHSTAAAARAKRVL 215
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNiAVLWVTHDKDEINHADKVI 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
1.81e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKtrfQGTqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNG--MDTStiknKD 80
Cdd:PRK13636 5 ILKVEELNYNYS---DGT--HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYS----RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRREKLGFVFQD-FNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK13636 76 GLMKLRESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 160 IITSPEILLADEPTGALDSKSSAALLD-VFEDINSMGQTILMVTHST-AAAARAKRVLFIKDGILynqIFRGekTERQMF 237
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKlLVEMQKELGLTIIIATHDIdIVPLYCDNVFVMKEGRV---ILQG--NPKEVF 230
|
..
gi 552782194 238 QE 239
Cdd:PRK13636 231 AE 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-220 |
2.19e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 103.08 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAS 82
Cdd:PRK11701 6 LLSVRGLTKLYGPR------KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRREKL-----GFVFQdfNLLDTL----SVKDNILLPLVLS--------RRPVKEMMSKVD-SVSRelgihqlLEKYPY 144
Cdd:PRK11701 80 EAERRRLlrtewGFVHQ--HPRDGLrmqvSAGGNIGERLMAVgarhygdiRATAGDWLERVEiDAAR-------IDDLPT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 145 EISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFED-INSMGQTILMVTHSTaAAAR--AKRVLFIKDG 220
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDL-AVARllAHRLLVMKQG 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-204 |
3.00e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.16 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRfQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYL-------------N 69
Cdd:PRK13631 21 ILRVKNLYCVFDEK-QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 70 GMDTSTIKNKDASSFRReKLGFVFQ--DFNLLDTLSVKDNILLPLVLSRrPVKEMMSKVDSVSRELGI-HQLLEKYPYEI 146
Cdd:PRK13631 100 ITNPYSKKIKNFKELRR-RVSMVFQfpEYQLFKDTIEKDIMFGPVALGV-KKSEAKKLAKFYLNKMGLdDSYLERSPFGL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 147 SGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHS 204
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-203 |
3.27e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYktRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKS-TLLNILAMLdqPTEGRVYLNG---MDTSTI 76
Cdd:PRK15134 3 QPLLAIENLSVAF--RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSGdirFHGESL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 77 KNKDASSFRR---EKLGFVFQD----FNLLDTLSVKdnilLPLVLS------RRPVK-EMMSKVDSVsrelGIHQL---L 139
Cdd:PRK15134 79 LHASEQTLRGvrgNKIAMIFQEpmvsLNPLHTLEKQ----LYEVLSlhrgmrREAARgEILNCLDRV----GIRQAakrL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 140 EKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINS-MGQTILMVTH 203
Cdd:PRK15134 151 TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQeLNMGLLFITH 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-251 |
3.44e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.41 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 22 VEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFrreKLGFVFQDFNLLDT 101
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LSVKDNILLPLVLSRR----PV---KEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:PRK09700 95 LTVLENLYIGRHLTKKvcgvNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 175 ALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGilyNQIFRGekterqMFQEIS--DTLTVMAGKE 251
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG---SSVCSG------MVSDVSndDIVRLMVGRE 245
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-206 |
4.94e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.63 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTR------FQGTQ-VEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTST 75
Cdd:PRK15079 8 LLEVADLKVHFDIKdgkqwfWQPPKtLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 76 IKNKDASSFRREkLGFVFQD--FNLLDTLSVKDNILLPLV-----LSRRPVKE----MMSKVDSVSrelgihQLLEKYPY 144
Cdd:PRK15079 88 MKDDEWRAVRSD-IQMIFQDplASLNPRMTIGEIIAEPLRtyhpkLSRQEVKDrvkaMMLKVGLLP------NLINRYPH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 145 EISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTA 206
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLA 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-222 |
1.49e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAML-----DQPTEGRVYLNGMDtstIKNKDASSFR-REKLGFVFQDF 96
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRN---IYSPDVDPIEvRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 NLLDTLSVKDNILLPLVLSR--RPVKEMMSKVDSVSRELG----IHQLLEKYPYEISGGQKQRVAVARAIITSPEILLAD 170
Cdd:PRK14267 95 NPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAAlwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552782194 171 EPTGALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAAR-AKRVLFIKDGIL 222
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARvSDYVAFLYLGKL 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-241 |
1.99e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQ------PTEGRVYLNGMDTSTIknkDASSFRREkLGFVFQDFNL 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQI---DAIKLRKE-VGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 99 LDTLSVKDNILLPL----VLSRRPVKEMMskvDSVSRELG----IHQLLEKYPYEISGGQKQRVAVARAIITSPEILLAD 170
Cdd:PRK14246 102 FPHLSIYDNIAYPLkshgIKEKREIKKIV---EECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 171 EPTGALDSKSSAALLDVFEDINSMgQTILMVTHSTAAAAR-AKRVLFIKDGILY-----NQIF---RGEKTERQMFQEIS 241
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARvADYVAFLYNGELVewgssNEIFtspKNELTEKYVIGRIS 257
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-203 |
2.04e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.36 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQP---TEGRVYLNGMdtstiknKDASSFRREKLGFVFQDFNLLDT 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM-------PIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LSVKDNILLP--LVLSRR-PVKEMMSKVDSVSRELGI----HQLL--EKYPYEISGGQKQRVAVARAIITSPEILLADEP 172
Cdd:TIGR00955 114 LTVREHLMFQahLRMPRRvTKKEKRERVDEVLQALGLrkcaNTRIgvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|.
gi 552782194 173 TGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-220 |
3.12e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 20 TQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtSTIKNKDASSFRReKLGFVFQD-FNL 98
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRR-KIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 99 LDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDS 178
Cdd:PRK13642 94 FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 552782194 179 KSSAALLDVFEDI-NSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PRK13642 174 TGRQEIMRVIHEIkEKYQLTVLSITHDLDEAASSDRILVMKAG 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-202 |
9.67e-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: 96.73 E-value: 9.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRREKLGFVFQD---FNLLD 100
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP---VTRRSPRDAIRAGIAYVPEDrkrEGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 TLSVKDNILLPLVLSrrpvkemmskvdsvsrelgihqllekypyeisGGQKQRVAVARAIITSPEILLADEPTGALDSKS 180
Cdd:cd03215 92 DLSVAENIALSSLLS--------------------------------GGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180
....*....|....*....|..
gi 552782194 181 SAALLDVFEDINSMGQTILMVT 202
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLLIS 161
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-177 |
3.00e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.55 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTR---FQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiknk 79
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 80 DASSFRREKLGFVFQD-FNLLDTLSVKDNIL-LPLVLSrrpvkemmSKVDSVSRELGIHQLLEK----------YPYEIS 147
Cdd:PRK15112 80 GDYSYRSQRIRMIFQDpSTSLNPRQRISQILdFPLRLN--------TDLEPEQREKQIIETLRQvgllpdhasyYPHMLA 151
|
170 180 190
....*....|....*....|....*....|
gi 552782194 148 GGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-203 |
1.72e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTrfqgtQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtSTIKNKD 80
Cdd:PRK13652 1 MHLIETRDLCYSYSG-----SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG---EPITKEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASSFRReKLGFVFQ--DFNLLDTLSVKDNILLP--LVLSRRPVKEmmsKVDSVSRELGIHQLLEKYPYEISGGQKQRVAV 156
Cdd:PRK13652 73 IREVRK-FVGLVFQnpDDQIFSPTVEQDIAFGPinLGLDEETVAH---RVSSALHMLGLEELRDRVPHHLSGGEKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 552782194 157 ARAIITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTH 203
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTH 196
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
23-245 |
1.85e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.23 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLL-NILAMLDQPTE----GRVYLNGMDTSTiKNKDASSFRREkLGFVFQDFN 97
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLrSINRMNDLNPEvtitGSIVYNGHNIYS-PRTDTVDLRKE-IGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 98 LLdTLSVKDNILLPLVLSRRPVKEMMSKVdsVSRELG-------IHQLLEKYPYEISGGQKQRVAVARAIITSPEILLAD 170
Cdd:PRK14239 97 PF-PMSIYENVVYGLRLKGIKDKQVLDEA--VEKSLKgasiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 171 EPTGALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAAR-AKRVLFIKDG--ILYNQIfrgekteRQMF-----QEISD 242
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSMQQASRiSDRTGFFLDGdlIEYNDT-------KQMFmnpkhKETED 245
|
...
gi 552782194 243 TLT 245
Cdd:PRK14239 246 YIS 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-220 |
4.03e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.38 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKtRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASsfrrEK 88
Cdd:COG4604 4 IKNVSK-RYGGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 89 LGFVFQDFNLLDTLSVKDnillpLVL------SR-RPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAII 161
Cdd:COG4604 77 LAILRQENHINSRLTVRE-----LVAfgrfpySKgRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 162 TSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHS-TAAAARAKRVLFIKDG 220
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDiNFASCYADHIVAMKDG 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-180 |
4.40e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.18 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNgmDTSTIKNKDAsS 83
Cdd:PTZ00265 383 IQFKNVRFHYDTR---KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINL-K 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLGFVFQDfNLLDTLSVKDNILLPLV----------------------LSRR---------PVKEMMSKVDS---- 128
Cdd:PTZ00265 457 WWRSKIGVVSQD-PLLFSNSIKNNIKYSLYslkdlealsnyynedgndsqenKNKRnscrakcagDLNDMSNTTDSneli 535
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 129 ----------------VSRELGIHQLLEKYP--YE---------ISGGQKQRVAVARAIITSPEILLADEPTGALDSKS 180
Cdd:PTZ00265 536 emrknyqtikdsevvdVSKKVLIHDFVSALPdkYEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-203 |
1.13e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.41 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKTRFQGTqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDT---STIKNK 79
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGV-VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEwvdMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 80 DASSFRREKLGFVFQDFNLLDTLSVKDNIL------LPLVLSRRpvKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQR 153
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNLTeaigleLPDELARM--KAVITLKMVGFDEEKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 154 VAVARAIITSPEILLADEPTGALDSKSSAALLD-VFEDINSMGQTILMVTH 203
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSH 486
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-185 |
1.30e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTL-LNILAMLdqPTEGRVYLNGMDTSTIKNKDASSFRReKLGFVFQDFN--LLD 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 TLSVKDNILLPLVLSRRPV--KEMMSKVDSVSRELGIH-QLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:PRK15134 378 RLNVLQIIEEGLRVHQPTLsaAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
....*...
gi 552782194 178 SKSSAALL 185
Cdd:PRK15134 458 KTVQAQIL 465
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-211 |
2.22e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.65 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTrfQGTQVEALKDIHFTVEKGEYVAIMGESGSGKS-TLLNILAMLDQPteGRVY-----LNGMDTS 74
Cdd:PRK11022 1 MALLNVDKLSVHFGD--ESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 75 TIKNKDASSFRREKLGFVFQD------------FNLLDTLSVKDNillplvLSRRPVK----EMMSKV---DSVSRelgi 135
Cdd:PRK11022 77 RISEKERRNLVGAEVAMIFQDpmtslnpcytvgFQIMEAIKVHQG------GNKKTRRqraiDLLNQVgipDPASR---- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 136 hqlLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQ-TILMVTHSTAAAARA 211
Cdd:PRK11022 147 ---LDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEA 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-173 |
7.23e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 90.28 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 21 QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiknkdASSFRREK--LGFVFQDFNL 98
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK-----LPPHERARagIAYVPQGREI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 99 LDTLSVKDNILLplVLSRRPVKEmmSKVDSVSREL--GIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:TIGR03410 87 FPRLTVEENLLT--GLAALPRRS--RKIPDEIYELfpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-210 |
1.89e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.00 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 21 QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRREkLGFVFQD-FNLL 99
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 DT-LSVKDNILLPL-VLSRRPVKEMMSKVDSVSRELGI---HQLleKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:PRK10261 415 DPrQTVGDSIMEPLrVHGLLPGKAAAARVAWLLERVGLlpeHAW--RYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 552782194 175 ALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR 210
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVER 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-203 |
2.20e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNgmdtstiknkdassfRREKLGFVFQDFNLLDTLSV 104
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNILlplvLSRRPVKEMMSKVDSVSRELGI------------HQLLEKYPYEI-------------------------S 147
Cdd:COG0488 79 LDTVL----DGDAELRALEAELEELEAKLAEpdedlerlaelqEEFEALGGWEAearaeeilsglgfpeedldrpvselS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 148 GGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALldvfED-INSMGQTILMVTH 203
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWL----EEfLKNYPGTVLVVSH 207
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-225 |
2.50e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 89.76 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 20 TQVEALKDIHFTVEKGEYVAIMGESGSGKStlLNILAMLD------QPTEGRVYLNGMDTStiknkdASSFRREKLGFVF 93
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVA------PCALRGRKIATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 94 QD----FNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRElGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLA 169
Cdd:PRK10418 86 QNprsaFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLE-NAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 170 DEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQ 225
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-220 |
3.58e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.02 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFR-----REKLGFVFqdfnll 99
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSLAFPF------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 dtlSVKDNILL---PLVLSRRP----VKEMMSKVDsvsrelgIHQLLEK-YPyEISGGQKQRVAVARAII-------TSP 164
Cdd:COG4559 91 ---TVEEVVALgraPHGSSAAQdrqiVREALALVG-------LAHLAGRsYQ-TLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 165 EILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQG 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-203 |
5.98e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.13 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 12 IYKTrFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMD---TSTIKNKDASsfrrek 88
Cdd:PRK11288 10 IGKT-FPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfASTTAALAAG------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 89 LGFVFQDFNLLDTLSVKDNILLPLVLSRRPV---KEMMSKVDSVSRELGIH---QLLEKYpyeISGGQKQRVAVARAIIT 162
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHKGGIvnrRLLNYEAREQLEHLGVDidpDTPLKY---LSIGQRQMVEIAKALAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-203 |
6.49e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.67 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 27 DIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFRReKLGFVFQDFNLLDTLSVKD 106
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 107 NILLPL--------VLSRRPVkemMSKVDSVsrelGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDS 178
Cdd:PRK11831 104 NVAYPLrehtqlpaPLLHSTV---MMKLEAV----GLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180
....*....|....*....|....*.
gi 552782194 179 KSSAALLDVFEDINS-MGQTILMVTH 203
Cdd:PRK11831 177 ITMGVLVKLISELNSaLGVTCVVVSH 202
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-220 |
8.99e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.85 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 17 FQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFrREKLGFVFQDF 96
Cdd:PRK11176 351 YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASL-RNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 NLL-DTlsVKDNILLPL--VLSRRPVK---EMMSKVDSVSR-ELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLA 169
Cdd:PRK11176 427 HLFnDT--IANNIAYARteQYSREQIEeaaRMAYAMDFINKmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 170 DEPTGALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEKADEILVVEDG 554
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-223 |
9.27e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.38 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 5 DVQHVKKIYKTR-----FQGT----------QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLN 69
Cdd:COG4586 3 EVENLSKTYRVYekepgLKGAlkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 70 GMDTStiknKDASSFRReKLGFVF-QDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISG 148
Cdd:COG4586 83 GYVPF----KRRKEFAR-RIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 149 GQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTA-AAARAKRVLFIKDG-ILY 223
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHDMDdIEALCDRVIVIDHGrIIY 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-223 |
1.03e-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: 91.23 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKTrFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTikNKDASsfrREK 88
Cdd:TIGR01257 931 VKNLVKI-FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--NLDAV---RQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 89 LGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILL 168
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 169 ADEPTGALDSKSSAALLDVFEDINSmGQTILMVTHST-AAAARAKRVLFIKDGILY 223
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMdEADLLGDRIAIISQGRLY 1139
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-240 |
1.40e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 18 QGTQVEALKDIHFTVEKGEYVAIMGESGSGKS-TLLNILAMLDQpTEGRVYLNGM----------DTSTIKNKDASSFRR 86
Cdd:PRK10261 25 EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 EKLGFVFQD----FNLLDTL--SVKDNILLPLVLSR----RPVKEMMSKVdsvsRELGIHQLLEKYPYEISGGQKQRVAV 156
Cdd:PRK10261 104 ADMAMIFQEpmtsLNPVFTVgeQIAESIRLHQGASReeamVEAKRMLDQV----RIPEAQTILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 157 ARAIITSPEILLADEPTGALDSKSSAALLD---VFEDINSMGqtILMVTHSTAAAAR-AKRVLFikdgilynqIFRGEKT 232
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQlikVLQKEMSMG--VIFITHDMGVVAEiADRVLV---------MYQGEAV 248
|
....*...
gi 552782194 233 ERQMFQEI 240
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-220 |
1.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 14 KTRFQgtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLN--GMDTSTIKNKDASSFRREkLGF 91
Cdd:PRK13645 19 KTPFE---FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPANLKKIKEVKRLRKE-IGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 92 VFQ--DFNLLDTLSVKDNILLPLVLSRRPvKEMMSKVDSVsreLGIHQLLEKY----PYEISGGQKQRVAVARAIITSPE 165
Cdd:PRK13645 95 VFQfpEYQLFQETIEKDIAFGPVNLGENK-QEAYKKVPEL---LKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRiADEVIVMHEG 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-220 |
1.89e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKIYktrfqGTQVeALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiknkdA 81
Cdd:PRK13537 6 APIDFRNVEKRY-----GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 SSFRREKLGFVFQDFNLLDTLSVKDNILL---PLVLSRRPVKEMMSKVDSVSRelgIHQLLEKYPYEISGGQKQRVAVAR 158
Cdd:PRK13537 75 ARHARQRVGVVPQFDNLDPDFTVRENLLVfgrYFGLSAAAARALVPPLLEFAK---LENKADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 159 AIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEG 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-222 |
2.32e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 86.01 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQDFNLLDTlS 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNI-------------LLPLVLSRRPVKEMMSKVDSVSRELGIHqllekypyeISGGQKQRVAVARAIITSPEILLAD 170
Cdd:cd03244 94 IRSNLdpfgeysdeelwqALERVGLKEFVESLPGGLDTVVEEGGEN---------LSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552782194 171 EPTGALDSKSSAALLDVfedINSM--GQTILMVTHSTAAAARAKRVLFIKDGIL 222
Cdd:cd03244 165 EATASVDPETDALIQKT---IREAfkDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-177 |
2.83e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.75 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstiknKDASSFRREKL----GF 91
Cdd:PRK13548 11 RLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG--------RPLADWSPAELarrrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 92 VFQDFNLLDTLSVKDNI---LLPLVLSRRPVKEMmskVDSVSRELGIHQLLEK-YPyEISGGQKQRVAVARAI--ITSPE 165
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVamgRAPHGLSRAEDDAL---VAAALAQVDLAHLAGRdYP-QLSGGEQQRVQLARVLaqLWEPD 156
|
170
....*....|....*.
gi 552782194 166 ----ILLADEPTGALD 177
Cdd:PRK13548 157 gpprWLLLDEPTSALD 172
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-220 |
4.57e-20 |
|
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: 89.03 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYktrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASS 83
Cdd:TIGR01193 474 IVINDVSYSY-----GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS---LKDIDRHT 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREkLGFVFQDFNLLDTlSVKDNILLPLV--LSRRPVKEMMS----KVDSVSRELGIHQLLEKYPYEISGGQKQRVAVA 157
Cdd:TIGR01193 546 LRQF-INYLPQEPYIFSG-SILENLLLGAKenVSQDEIWAACEiaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 158 RAIITSPEILLADEPTGALDSKSSAALLDVFEDINSmgQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKIIVLDHG 684
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-220 |
5.72e-20 |
|
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: 84.77 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 13 YKTRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfrREKLGFV 92
Cdd:cd03369 12 LSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL----RSSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 93 FQDFNLLDTlSVKDNIllpLVLSRRPVKEMMSKVdSVSrELGIHqllekypyeISGGQKQRVAVARAIITSPEILLADEP 172
Cdd:cd03369 88 PQDPTLFSG-TIRSNL---DPFDEYSDEEIYGAL-RVS-EGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 552782194 173 TGALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03369 153 TASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-240 |
6.47e-20 |
|
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: 85.14 E-value: 6.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStikNKDAss 83
Cdd:TIGR03740 1 LETKNLSKRFGKQ------TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDL-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frrEKLGFVFQDFNLLDTLSVKDNilLPLVLSRRPVKEmmSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITS 163
Cdd:TIGR03740 70 ---HKIGSLIESPPLYENLTAREN--LKVHTTLLGLPD--SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNH 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGIL-YNQIFRGEKTERQMFQEI 240
Cdd:TIGR03740 143 PKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQlADHIGIISEGVLgYQGKINKSENLEKLFVEV 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-181 |
6.59e-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: 88.32 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 22 VEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQ--PTEGRVY----------------------------LNGM 71
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvgepcpvcggtLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 72 DTSTIKNKDASSFR-REKLGFVFQ-DFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGG 149
Cdd:TIGR03269 93 EVDFWNLSDKLRRRiRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGG 172
|
170 180 190
....*....|....*....|....*....|..
gi 552782194 150 QKQRVAVARAIITSPEILLADEPTGALDSKSS 181
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTA 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-225 |
6.63e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFrREKLGFVFQD 95
Cdd:PRK11160 347 TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP---IADYSEAAL-RQAISVVSQR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLL-DTLsvKDNILLPL-VLSRRPVKEMMSKVdsvsrelGIHQLLEKYP----------YEISGGQKQRVAVARAIITS 163
Cdd:PRK11160 423 VHLFsATL--RDNLLLAApNASDEALIEVLQQV-------GLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDInSMGQTILMVTHSTAAAARAKRVLFIKDGILYNQ 225
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-225 |
1.15e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.53 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 39 AIMGESGSGKSTLLNILAMLDQPTEGRVYLNGM---DTSTIKNKDASSFRReKLGFVFQDFNLLdTLSVKDNILLPLVLS 115
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllgGRSIFNYRDVLEFRR-RVGMLFQRPNPF-PMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 116 RR-PVKEMMSKVDSVSRELG----IHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAallDVFED 190
Cdd:PRK14271 129 KLvPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTE---KIEEF 205
|
170 180 190
....*....|....*....|....*....|....*...
gi 552782194 191 INSMGQ--TILMVTHSTAAAAR-AKRVLFIKDGILYNQ 225
Cdd:PRK14271 206 IRSLADrlTVIIVTHNLAQAARiSDRAALFFDGRLVEE 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-220 |
1.44e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 15 TRFQGTQVE-------ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASsfRRe 87
Cdd:PRK10253 6 ARLRGEQLTlgygkytVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 88 kLGFVFQDFNLLDTLSVKDNILL------PLVLSRRpvKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAII 161
Cdd:PRK10253 83 -IGLLAQNATTPGDITVQELVARgryphqPLFTRWR--KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 162 TSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRyASHLIALREG 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-203 |
2.29e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.86 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 35 GEYVAIMGESGSGKSTLLNILAmldqpteGRVYLNGMD-TSTIKNKDASSFRREKLGFVFQDFNLLDTLSVKDNIL---- 109
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALA-------GRIQGNNFTgTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVfcsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 110 --LPLVLSRrpvKEMMSKVDSVSRELGIHQ-----LLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSA 182
Cdd:PLN03211 167 lrLPKSLTK---QEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180
....*....|....*....|.
gi 552782194 183 ALLDVFEDINSMGQTILMVTH 203
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-210 |
2.38e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.45 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQ--PT---EGRVYLNGMDTSTiKNKDASSFRReKLGFVFQDFNL 98
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA-PDVDPVEVRR-RIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 99 LDTlSVKDNILL-PLVLSrrpVKEMMSKVdsVSRELGIHQL-------LEKYPYEISGGQKQRVAVARAIITSPEILLAD 170
Cdd:PRK14243 103 FPK-SIYDNIAYgARING---YKGDMDEL--VERSLRQAALwdevkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552782194 171 EPTGALDSKSSaalLDVFEDINSMGQ--TILMVTHSTAAAAR 210
Cdd:PRK14243 177 EPCSALDPIST---LRIEELMHELKEqyTIIIVTHNMQQAAR 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-215 |
2.70e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.01 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAML-DQPTEGRVYLNGMDTSTIKN---- 78
Cdd:PTZ00265 1166 IEIMDVNFRYISR---PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNeqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 79 ----------KDASSFRREKLGFVFQD---FN-----LLDTLSVKDNILLPL-----VLSRRPVKEMMS----------- 124
Cdd:PTZ00265 1243 qgdeeqnvgmKNVNEFSLTKEGGSGEDstvFKnsgkiLLDGVDICDYNLKDLrnlfsIVSQEPMLFNMSiyenikfgked 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 125 ----KVDSVSRELGIHQLLE----KY-----PY--EISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFE 189
Cdd:PTZ00265 1323 atreDVKRACKFAAIDEFIEslpnKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260
....*....|....*....|....*..
gi 552782194 190 DI-NSMGQTILMVTHSTAAAARAKRVL 215
Cdd:PTZ00265 1403 DIkDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-251 |
3.34e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 86.42 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKiyktRFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLdQPT---EGRVYLNGmdtSTIKNK 79
Cdd:TIGR02633 1 LLEMKGIVK----TFGG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSG---SPLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 80 DASSFRREKLGFVFQDFNLLDTLSVKDNILLPLVLS----RRPVKEMMSKVDSVSRELGIHQLLEKYPY-EISGGQKQRV 154
Cdd:TIGR02633 71 NIRDTERAGIVIIHQELTLVPELSVAENIFLGNEITlpggRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 155 AVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHS-TAAAARAKRVLFIKDGilynqifRGEKTE 233
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDG-------QHVATK 223
|
250
....*....|....*...
gi 552782194 234 RQMFQEISDTLTVMAGKE 251
Cdd:TIGR02633 224 DMSTMSEDDIITMMVGRE 241
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-203 |
3.95e-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: 82.54 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 30 FTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtsTIKNKDASSFRREKLGFVFQDfNLLDTLSVKDNI- 108
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIARGLLYLGHAP-GIKTTLSVLENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 109 LLPLVLSRRPVKEMMSKVDSVSRE-LGIHQLlekypyeiSGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDV 187
Cdd:cd03231 96 FWHADHSDEQVEEALARVGLNGFEdRPVAQL--------SAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*.
gi 552782194 188 FEDINSMGQTILMVTH 203
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-203 |
7.65e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 81.64 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdassfRREKLGFVFQDFNLLDTL 102
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNI--LLPLVLS-RRPVKEMMSKVDSVSRE-LGIHQLlekypyeiSGGQKQRVAVARAIITSPEILLADEPTGALDS 178
Cdd:TIGR01189 89 SALENLhfWAAIHGGaQRTIEDALAAVGLTGFEdLPAAQL--------SAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*
gi 552782194 179 KSSAALLDVFEDINSMGQTILMVTH 203
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-204 |
1.63e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASSFrrekLGFvfQDFnLLDTLSV 104
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY----LGH--RNA-MKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNillpLVLSRRPVKEMMSKVDSVSRELGIHQLLE-KYPYeISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAA 183
Cdd:PRK13539 91 AEN----LEFWAAFLGGEELDIAAALEAVGLAPLAHlPFGY-LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|.
gi 552782194 184 LLDVFEDINSMGQTILMVTHS 204
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATHI 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-209 |
2.37e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.23 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 27 DIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTstikNKDASSFRReklgfvfqdfNLL------- 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQ----------DLLylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 --DTLSVKDN--ILLPL--VLSRRPVKEMMSKVDSVSRE-LGIHQLlekypyeiSGGQKQRVAVARAIITSPEILLADEP 172
Cdd:PRK13538 85 ikTELTALENlrFYQRLhgPGDDEALWEALAQVGLAGFEdVPVRQL--------SAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 552782194 173 TGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAA 209
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVA 193
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-204 |
2.58e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKD 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGR------RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 81 ASsfrREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMS-KVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARA 159
Cdd:PRK10895 75 RA---RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552782194 160 IITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHS 204
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-202 |
3.24e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfRREKLGFVFQD---FNLL 99
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA---IRAGIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 DTLSVKDNILLPLV--LSRRPV---KEMMSKVDSVSRELGI-----HQLLEkypyEISGGQKQRVAVARAIITSPEILLA 169
Cdd:COG1129 343 LDLSIRENITLASLdrLSRGGLldrRRERALAEEYIKRLRIktpspEQPVG----NLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552782194 170 DEPT-----GAldsKSsaallDVFEDINSM---GQTILMVT 202
Cdd:COG1129 419 DEPTrgidvGA---KA-----EIYRLIRELaaeGKAVIVIS 451
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-173 |
5.14e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 80.55 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRREKLGFVFQDFNLLDTLS 103
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTD---LTGLDEHEIARLGIGRKFQKPTVFEELT 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 104 VKDNILLPL--------VLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:COG4674 102 VFENLELALkgdrgvfaSLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-220 |
5.18e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNgmdtstiknkdassfRREKLGFVFQDFNL-LDTLs 103
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP---------------AGARVLFLPQRPYLpLGTL- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 vKDNILLPLV---LSRRPVKEMMSKV------DSVSRELGIHQLLekypyeiSGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:COG4178 443 -REALLYPATaeaFSDAELREALEAVglghlaERLDEEADWDQVL-------SLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552782194 175 ALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:COG4178 515 ALDEENEAALYQLLREELP-GTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-219 |
6.17e-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: 78.35 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkdassfrreklgfvfqdfnlldtlsv 104
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDL------------------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 kdnillpLVLSRRPvkeMMSkvDSVSRElgihQLLekYPY--EISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSA 182
Cdd:cd03223 67 -------LFLPQRP---YLP--LGTLRE----QLI--YPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*..
gi 552782194 183 ALLDVFEDinsMGQTILMVTHSTAAAARAKRVLFIKD 219
Cdd:cd03223 129 RLYQLLKE---LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-203 |
6.51e-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: 77.49 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRfqgtqvEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVylngmdtstiknkdaSS 83
Cdd:cd03221 1 IELENLSKTYGGK------LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------TW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 FRREKLGFVfqdfnlldtlsvkdnillplvlsrrpvkemmskvdsvsrelgiHQLlekypyeiSGGQKQRVAVARAIITS 163
Cdd:cd03221 60 GSTVKIGYF-------------------------------------------EQL--------SGGEKMRLALAKLLLEN 88
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSmgqTILMVTH 203
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-251 |
6.67e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKiyktRFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLdQPT---EGRVYLNGmdtstiK 77
Cdd:PRK13549 3 EYLLEMKNITK----TFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEG------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 78 NKDASSFR-REKLGFV--FQDFNLLDTLSVKDNILLPLVLSRRPV---KEMMSKVDSVSRELGIHQLLEKYPYEISGGQK 151
Cdd:PRK13549 70 ELQASNIRdTERAGIAiiHQELALVKELSVLENIFLGNEITPGGImdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 152 QRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHS-TAAAARAKRVLFIKDGilyNQIfrGE 230
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDG---RHI--GT 224
|
250 260
....*....|....*....|.
gi 552782194 231 KTERQMFQEisDTLTVMAGKE 251
Cdd:PRK13549 225 RPAAGMTED--DIITMMVGRE 243
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-220 |
1.19e-17 |
|
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: 78.91 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 19 GTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLniLAMLD--QPTEGRVYLNGMDTSTIKNKDASSFRREKLGFVFQDF 96
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGemQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 NLLDTlSVKDNILLPLVLSRRPVKEMmskVDSVSRELGIHQLLEKYPYEI-------SGGQKQRVAVARAIITSPEILLA 169
Cdd:cd03290 89 WLLNA-TVEENITFGSPFNKQRYKAV---TDACSLQPDIDLLPFGDQTEIgerginlSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552782194 170 DEPTGALDSKSSAALLD--VFEDINSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-203 |
1.34e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGrvylngmdtsTIKNKDASsfrreKLGFVFQDFNLLDTLsv 104
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKL-----RIGYVPQKLYLDTTL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 kdnillPLVLSR----RP-VK--EMMSKVDSVSRELGIHQLLEKypyeISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:PRK09544 83 ------PLTVNRflrlRPgTKkeDILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180
....*....|....*....|....*..
gi 552782194 178 SKSSAALLDVFEDI-NSMGQTILMVTH 203
Cdd:PRK09544 153 VNGQVALYDLIDQLrRELDCAVLMVSH 179
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-210 |
1.44e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 17 FQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASsfrrEKLGFVFQDF 96
Cdd:PRK09536 13 FGDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 NLLDTLSVKDNIllplVLSRRPVKEMMSKVDSVSR--------ELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILL 168
Cdd:PRK09536 87 SLSFEFDVRQVV----EMGRTPHRSRFDTWTETDRaaverameRTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552782194 169 ADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR 210
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAAR 204
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-203 |
2.51e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.95 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTRfQGTqVEALKDIHFTVEKGEYVAIMGESGSGKS----TLLNILAMLDQPTEGRVYLNGMDTSTI 76
Cdd:COG4170 1 MPLLDIRNLTIEIDTP-QGR-VKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 77 KNKDASSFRREKLGFVFQD-FNLLD-TLSVKDNIL--LP-----------LVLSRRPVKEMMSKVdsvsrelGI--HQ-L 138
Cdd:COG4170 79 SPRERRKIIGREIAMIFQEpSSCLDpSAKIGDQLIeaIPswtfkgkwwqrFKWRKKRAIELLHRV-------GIkdHKdI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 139 LEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSM-GQTILMVTH 203
Cdd:COG4170 152 MNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISH 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-203 |
2.57e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKiyktRFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNgmdtSTIknkdas 82
Cdd:COG0488 315 VLELEGLSK----SYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETV------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 sfrreKLGFVFQDFNLLD-TLSVKDNIllplvlsrRPVKEMMSKVDsvsrelgIHQLLE----------KYPYEISGGQK 151
Cdd:COG0488 379 -----KIGYFDQHQEELDpDKTVLDEL--------RDGAPGGTEQE-------VRGYLGrflfsgddafKPVGVLSGGEK 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 152 QRVAVARAIITSPEILLADEPTGALDSKSSAAL---LDVFEdinsmGqTILMVTH 203
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLEALeeaLDDFP-----G-TVLLVSH 487
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-184 |
2.68e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNkdasSFRREKLGFVFQDFNLLDTlSV 104
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH----SVLRQGVAMVQQDPVVLAD-TF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNILLPLVLSRRPVKEMMSKVD--SVSREL--GIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKS 180
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQlaELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
....
gi 552782194 181 SAAL 184
Cdd:PRK10790 512 EQAI 515
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-210 |
2.71e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.52 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDASsfrrEKLGFVFQDFNLLDTLSV 104
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNILL---P-LVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKS 180
Cdd:PRK11231 94 RELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190
....*....|....*....|....*....|
gi 552782194 181 SAALLDVFEDINSMGQTILMVTHSTAAAAR 210
Cdd:PRK11231 174 QVELMRLMRELNTQGKTVVTVLHDLNQASR 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-203 |
2.95e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYktrfqgTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAs 82
Cdd:PRK15439 11 LLCARSISKQY------SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 sfrrEKLG--FVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVdsvsRELGIHQLLEKYPYEISGGQKQRVAVARAI 160
Cdd:PRK15439 84 ----HQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLL----AALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 552782194 161 ITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-225 |
3.58e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLdQPTEGRVYLNGMDTSTIKNKDASSFR-----REKLGF---VFQdf 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFampVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 nlldtlsvkdniLLPLVLSRRPVKEMMSK-VDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAII-TSPEI------LL 168
Cdd:COG4138 89 ------------YLALHQPAGASSEAVEQlLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegqlLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 169 ADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHS-TAAAARAKRVLFIKDGILYNQ 225
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKLVAS 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-210 |
4.03e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.49 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 27 DIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkDASSFRREKLGFVFQDFNLLDTLSVKD 106
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-----ARARLARARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 107 NILL---PLVLSRRPVKEMMSKVDSVSRelgihqlLEKYP----YEISGGQKQRVAVARAIITSPEILLADEPTGALDSK 179
Cdd:PRK13536 134 NLLVfgrYFGMSTREIEAVIPSLLEFAR-------LESKAdarvSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190
....*....|....*....|....*....|.
gi 552782194 180 SSAALLDVFEDINSMGQTILMVTHSTAAAAR 210
Cdd:PRK13536 207 ARHLIWERLRSLLARGKTILLTTHFMEEAER 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-177 |
4.35e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 22 VEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRREKLGFVFQD---FNL 98
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED---ITGLSPRERRRLGVAYIPEDrlgRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 99 LDTLSVKDNILL------PL----VLSRRPV----KEMMSKVD--SVSRELGIHQLlekypyeiSGGQKQRVAVARAIIT 162
Cdd:COG3845 348 VPDMSVAENLILgryrrpPFsrggFLDRKAIrafaEELIEEFDvrTPGPDTPARSL--------SGGNQQKVILARELSR 419
|
170
....*....|....*
gi 552782194 163 SPEILLADEPTGALD 177
Cdd:COG3845 420 DPKLLIAAQPTRGLD 434
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-220 |
2.04e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.26 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILA--MLDQPTEGRVYLNGMDtstIKNKDASSFRREKLGFVFQdfnlld 100
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGED---ITDLPPEERARLGIFLAFQ------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 tlsvkdnillplvlsrRPVKEMMSKVDSVSRELGihqllekypYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKS 180
Cdd:cd03217 85 ----------------YPPEIPGVKNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552782194 181 SAALLDVFEDINSMGQTILMVTH--STAAAARAKRVLFIKDG 220
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDG 181
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-220 |
2.33e-16 |
|
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: 74.59 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAM--LDQPTEGRVYLNGmdtstIKNKDasSFRREkLGFVFQDFNLLDTL 102
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING-----RPLDK--NFQRS-TGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNILLPLVLsrrpvkemmskvdsvsRELGIhqllekypyeisgGQKQRVAVARAIITSPEILLADEPTGALDSKSSA 182
Cdd:cd03232 95 TVREALRFSALL----------------RGLSV-------------EQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552782194 183 ALLDVFEDINSMGQTILMVTH--STAAAARAKRVLFIKDG 220
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-210 |
2.68e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.23 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQ-----PTEGRVYLNGMDTSTiKNKDASSFRREkLGFVFQDFNLL 99
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYE-RRVNLNRLRRQ-VSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 dTLSVKDNILLPL-VLSRRPVKEMMSKVDSVSRELG----IHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:PRK14258 101 -PMSVYDNVAYGVkIVGWRPKLEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 552782194 175 ALDSKSSAALLDVFEDINSMGQ-TILMVTHSTAAAAR 210
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSR 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-203 |
3.32e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 7 QHVKKIYktrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLN-GMdtstiknkdassfr 85
Cdd:TIGR03719 8 NRVSKVV-----PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGI-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 86 reKLGFVFQDFNLLDTLSVKDNILLPLvlsrRPVKEMMSKVDSVSRELG-----IHQLLEKY------------------ 142
Cdd:TIGR03719 69 --KVGYLPQEPQLDPTKTVRENVEEGV----AEIKDALDRFNEISAKYAepdadFDKLAAEQaelqeiidaadawdldsq 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 143 -----------PYE-----ISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSmgqTILMVTH 203
Cdd:TIGR03719 143 leiamdalrcpPWDadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTH 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-204 |
5.02e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkdaSSFRREKLGFVFQD------FN 97
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-------QALQKNLVAYVPQSeevdwsFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 98 LLdtlsVKDNILLP----LVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:PRK15056 95 VL----VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|.
gi 552782194 174 GALDSKSSAALLDVFEDINSMGQTILMVTHS 204
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-205 |
5.43e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLD--QPTEGRVYLNGMDtstIKNKDASSFRREKLGFVFQD------- 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGED---ILELSPDERARAGIFLAFQYpveipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 --FNLLDT-LSVKDNILLPLVLSRRPVKEMMskvdsvsRELGIHQ-LLEKYPYE-ISGGQKQRVAVARAIITSPEILLAD 170
Cdd:COG0396 93 svSNFLRTaLNARRGEELSAREFLKLLKEKM-------KELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 552782194 171 EPTGALDsksSAALLDVFEDINSM---GQTILMVTHST 205
Cdd:COG0396 166 ETDSGLD---IDALRIVAEGVNKLrspDRGILIITHYQ 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-220 |
6.33e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.67 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQD 95
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 -FNLLDTlsVKDNILLPlvlsrRPvKEMMSKVDSVSRELGIH----QLLEKYPYEI-------SGGQKQRVAVARAIITS 163
Cdd:PRK10789 398 pFLFSDT--VANNIALG-----RP-DATQQEIEHVARLASVHddilRLPQGYDTEVgergvmlSGGQKQRISIARALLLN 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 164 PEILLADEPTGALDSKSSAALLdvfEDINSMGQ--TILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQIL---HNLRQWGEgrTVIISAHRLSALTEASEILVMQHG 525
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-203 |
7.33e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 2 ALLDVQHVKKiyktRFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA 81
Cdd:PRK10762 3 ALLQLKGIDK----AFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 82 ssfRREKLGFVFQDFNLLDTLSVKDNILlplvLSRRPV--------KEMMSKVDSVSRELGI----HQLLEkypyEISGG 149
Cdd:PRK10762 77 ---QEAGIGIIHQELNLIPQLTIAENIF----LGREFVnrfgridwKKMYAEADKLLARLNLrfssDKLVG----ELSIG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552782194 150 QKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-220 |
8.14e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.69 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAmlDQPTEGrvYLNGMDTSTIKNKDASSFRReKLGFVFQDFNLLDTLSV 104
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG--VITGGDRLVNGRPLDSSFQR-SIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNILLPLVLsRRP----VKEMMSKVDSVSRELGihqlLEKYPYEISG--------GQKQRVAVARAIITSPEILL-ADE 171
Cdd:TIGR00956 854 RESLRFSAYL-RQPksvsKSEKMEYVEEVIKLLE----MESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 172 PTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAK--RVLFIKDG 220
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-220 |
2.26e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 10 KKIYKTrFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLdQPT---EGRVYLNGmDTSTIKNKDASsfrr 86
Cdd:NF040905 5 RGITKT-FPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDG-EVCRFKDIRDS---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 EKLGFVF--QDFNLLDTLSVKDNILLPLVLSRRPV----------KEMMSKVdsvsrelGIHQLLEKYPYEISGGQKQRV 154
Cdd:NF040905 76 EALGIVIihQELALIPYLSIAENIFLGNERAKRGVidwnetnrraRELLAKV-------GLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 155 AVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDG 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-220 |
3.86e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 21 QVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDtstIKNKDASSFRREKLGFVFQDFNLLD 100
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 TLSVKDNILLP-LVLSRRPVKEMMSKVDSVSRELgiHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSK 179
Cdd:PRK11614 94 RMTVEENLAMGgFFAERDQFQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552782194 180 SSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENG 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-210 |
1.61e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.97 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKdasSFRREkLGFVFQDFNLLDTLSV 104
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARK-VAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDnillpLV-LSRRPVKEMMSKVDSVSRE--------LGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGA 175
Cdd:PRK10575 103 RE-----LVaIGRYPWHGALGRFGAADREkveeaislVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 552782194 176 LDsksSAALLDVFEDINSMGQ----TILMVTHSTAAAAR 210
Cdd:PRK10575 178 LD---IAHQVDVLALVHRLSQerglTVIAVLHDINMAAR 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-203 |
6.75e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.75 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTrfqgtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtSTIKNKDass 83
Cdd:COG4152 2 LELKGLTKRFGD------KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frREKLGFVFQDFNLLDTLSVKDNIL-------LPLVLSRRPVKEMMSKVDsvsrelgihqlLEKYPY----EISGGQKQ 152
Cdd:COG4152 70 --RRRIGYLPEERGLYPKMKVGEQLVylarlkgLSKAEAKRRADEWLERLG-----------LGDRANkkveELSKGNQQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 153 RVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSH 187
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
25-229 |
8.08e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.06 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPT---EGRVYLNGMDtstiKNKDASSFRREKLgFVFQDFNLLDT 101
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----YKEFAEKYPGEII-YVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LSVKDNIllplvlsrrpvkemmskvDSVSRELGiHQLLEKypyeISGGQKQRVAVARAIITSPEILLADEPTGALDSKSS 181
Cdd:cd03233 98 LTVRETL------------------DFALRCKG-NEFVRG----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 182 aalldvFEDINSMgQTILMVTHSTAAAARAK----------RVLFIKDGilyNQIFRG 229
Cdd:cd03233 155 ------LEILKCI-RTMADVLKTTTFVSLYQasdeiydlfdKVLVLYEG---RQIYYG 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-222 |
8.39e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.86 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGtqVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIknkdaSSFRREKLGFV--F 93
Cdd:PRK11300 14 RFGG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-----PGHQIARMGVVrtF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 94 QDFNLLDTLSVKDNILLPL-------VLS--------RRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVAR 158
Cdd:PRK11300 87 QHVRLFREMTVIENLLVAQhqqlktgLFSgllktpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 159 AIITSPEILLADEPTGALDSKSSAALLDVFEDI-NSMGQTILMVTHSTaaaaraKRVLFIKDGIL 222
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDM------KLVMGISDRIY 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-223 |
9.45e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 9.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTsTIKNKDASsfrREKLGFVFQDFNLLDTL- 102
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-TAEQPEDY---RKLFSAVFTDFHLFDQLl 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 ----SVKDNILLPLVLSRRpvkEMMSKVDSVSRELGIHQLlekypyeiSGGQKQRVAVARAIITSPEILLADEptgalds 178
Cdd:PRK10522 414 gpegKPANPALVEKWLERL---KMAHKLELEDGRISNLKL--------SKGQKKRLALLLALAEERDILLLDE------- 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 179 ksSAALLD-VFEDI---------NSMGQTILMVTHSTAAAARAKRVLFIKDGILY 223
Cdd:PRK10522 476 --WAADQDpHFRREfyqvllpllQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-211 |
9.83e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTstikNKDASSFRREkLGFVFQDFNLLDTLSV 104
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQ-LCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNILLPLVLSRRPVKemmskVDSVSRELGIHQLLEkYPYEI-SGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAA 183
Cdd:PRK13540 92 RENCLYDIHFSPGAVG-----ITELCRLFSLEHLID-YPCGLlSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*...
gi 552782194 184 LLDVFEDINSMGQTILMVTHSTAAAARA 211
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNKA 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-203 |
1.08e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVeaLKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNG--MDTStiknKDASSFRREKLGFVF 93
Cdd:PRK13638 10 RYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYS----KRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 94 QD------FNLLDT---LSVKdNILLPLVLSRRPVKEMMSKVDSvsrelgihQLLEKYPYE-ISGGQKQRVAVARAIITS 163
Cdd:PRK13638 84 QDpeqqifYTDIDSdiaFSLR-NLGVPEAEITRRVDEALTLVDA--------QHFRHQPIQcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-204 |
2.45e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.15 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 9 VKKIYKTRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTstiknkdassfrrek 88
Cdd:PRK13545 24 LKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAA--------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 89 lgFVFQDFNLLDTLSVKDNILLP---LVLSRRPVKEMMSKVDSVSrELG--IHQLLEKYpyeiSGGQKQRVAVARAIITS 163
Cdd:PRK13545 89 --LIAISSGLNGQLTGIENIELKglmMGLTKEKIKEIIPEIIEFA-DIGkfIYQPVKTY----SSGMKSRLGFAISVHIN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHS 204
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHS 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-173 |
3.79e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYL-------NGMDTstiknkdassfrREKLGFVFQDF 96
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdaGDIAT------------RRRVGYMSQAF 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 97 NLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:NF033858 349 SLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-177 |
7.13e-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: 68.01 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLdQPTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQDFNLLdTLSV 104
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTW----RKAFGVIPQKVFIF-SGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNiLLPlvLSRRPVKEMMskvdSVSRELGIHQLLEKYP-----------YEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:TIGR01271 1309 RKN-LDP--YEQWSDEEIW----KVAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....
gi 552782194 174 GALD 177
Cdd:TIGR01271 1382 AHLD 1385
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-202 |
7.80e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 26 KDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA--------SSFRREKlGFvFQDFn 97
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgmayiTESRRDN-GF-FPNF- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 98 lldtlSVKDNILLPLVLSRRPVKEMMSKVDSvSRELGIHQ-----------LLEKYPYEISGGQKQRVAVARAIITSPEI 166
Cdd:PRK09700 357 -----SIAQNMAISRSLKDGGYKGAMGLFHE-VDEQRTAEnqrellalkchSVNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190
....*....|....*....|....*....|....*.
gi 552782194 167 LLADEPTGALDSKSSAALLDVFEDINSMGQTILMVT 202
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-204 |
7.92e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 66.38 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmDTSTIKnkdassfrreklgfvfQDFNLLDTLS 103
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIA----------------ISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNI---LLPLVLSRRPVKEMMSKVDSVSrELG--IHQLLEKYpyeiSGGQKQRVAVARAIITSPEILLADEPTGALDS 178
Cdd:PRK13546 102 GIENIefkMLCMGFKRKEIKAMTPKIIEFS-ELGefIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180
....*....|....*....|....*.
gi 552782194 179 KSSAALLDVFEDINSMGQTILMVTHS 204
Cdd:PRK13546 177 TFAQKCLDKIYEFKEQNKTIFFVSHN 202
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-225 |
9.46e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 30 FTVEKGEYVAIMGESGSGKSTLLNILAMLdQPTEGRVYLNGMDTSTIKNKDASSFRreklGFVFQdfnlldtlSVKDNIL 109
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQ--------QQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 110 LP----LVLSR---RPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAII-TSPEI------LLADEPTGA 175
Cdd:PRK03695 84 MPvfqyLTLHQpdkTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqVWPDInpagqlLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552782194 176 LDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGILYNQ 225
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLAS 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-235 |
1.34e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstiknkdassfrreKLGFVFQdFNLLDTLSV 104
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQ-TSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNILLPLVLSRrpvkemmSKVDSVSRELGIHQLLEKYPYE-----------ISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:TIGR01271 504 KDNIIFGLSYDE-------YRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 174 GALDSKSSAallDVFEDINS---MGQTILMVTHSTAAAARAKRVLFIKDGILYnqiFRGEKTERQ 235
Cdd:TIGR01271 577 THLDVVTEK---EIFESCLCklmSNKTRILVTSKLEHLKKADKILLLHEGVCY---FYGTFSELQ 635
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-203 |
2.28e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 22 VEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfRREKLGFVFQDFNLLDT 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA---LENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 102 LSVKDNILlplvLSRRPVK-------EMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:PRK10982 88 RSVMDNMW----LGRYPTKgmfvdqdKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180
....*....|....*....|....*....
gi 552782194 175 ALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-220 |
2.72e-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: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLN-ILAMLDQpTEGRVYLNGmdtstiknkdassfrreKLGFVFQDfNLLDTLS 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG-----------------SVAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNILLPLVLSRR------------PVKEMMSKVDSVsrELGihqllEKyPYEISGGQKQRVAVARAIITSPEILLADE 171
Cdd:TIGR00957 715 LRENILFGKALNEKyyqqvleacallPDLEILPSGDRT--EIG-----EK-GVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552782194 172 PTGALDSKSSAALLDvfEDINSMG----QTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:TIGR00957 787 PLSAVDAHVGKHIFE--HVIGPEGvlknKTRILVTHGISYLPQVDVIIVMSGG 837
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-203 |
2.79e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 7 QHVKKIYktrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLngMDTSTIknkdassfrr 86
Cdd:PRK11819 10 NRVSKVV-----PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGIKV---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 eklGFVFQDFNLLDTLSVKDNILLPLvlsrRPVKEMMSKVDSVSRELG-----IHQLLEKY------------------- 142
Cdd:PRK11819 73 ---GYLPQEPQLDPEKTVRENVEEGV----AEVKAALDRFNEIYAAYAepdadFDALAAEQgelqeiidaadawdldsql 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782194 143 ----------PYE-----ISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAAL---LDVFEdinsmGqTILMVTH 203
Cdd:PRK11819 146 eiamdalrcpPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLeqfLHDYP-----G-TVVAVTH 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-177 |
4.29e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNIL--AMLDQPTEGRVYLNGMDTStiknkdassfrreklgfvfQDFNLLDTL 102
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG-------------------REASLIDAI 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552782194 103 SVKDNILLplvlsrrpVKEMMSKVDsvsreLGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:COG2401 107 GRKGDFKD--------AVELLNAVG-----LSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
25-220 |
5.81e-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: 64.11 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLN-ILAMLDqpTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQDFNLLdTLS 103
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVPLQKW----RKAFGVIPQKVFIF-SGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 104 VKDNIllplvlsrRPV-KEMMSKVDSVSRELGIHQLLEKYP-----------YEISGGQKQRVAVARAIITSPEILLADE 171
Cdd:cd03289 93 FRKNL--------DPYgKWSDEEIWKVAEEVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552782194 172 PTGALDSKSSAALLDVFEDINSmGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:cd03289 165 PSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-203 |
6.86e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 1 MALLDVQHVKKIYKTrfQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQP----TEGRVYLNGMDTSTI 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKT--SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 77 KNKDASSFRREKLGFVFQDFNllDTLSVKDNILLPLVLS-----------------RRPVKEMMSKVdsvsrelGI--HQ 137
Cdd:PRK15093 79 SPRERRKLVGHNVSMIFQEPQ--SCLDPSERVGRQLMQNipgwtykgrwwqrfgwrKRRAIELLHRV-------GIkdHK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 138 -LLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDIN-SMGQTILMVTH 203
Cdd:PRK15093 150 dAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISH 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-235 |
1.10e-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: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtstiknkdassfrreKLGFVFQdFNLLDTLSV 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQ-FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNILLPLVLSRRPVKemmskvdSVSRELGIHQLLEKYPYE-----------ISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:cd03291 115 KENIIFGVSYDEYRYK-------SVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782194 174 GALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDGILYnqiFRGEKTERQ 235
Cdd:cd03291 188 GYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSY---FYGTFSELQ 246
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-222 |
1.11e-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: 64.58 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQDFNL------ 98
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQDPVLfsgslr 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 99 --LDTLS--VKDNILLPLVLS--RRPVKEMMSKVDSVSRELGihqllekypYEISGGQKQRVAVARAIITSPEILLADEP 172
Cdd:TIGR00957 1378 mnLDPFSqySDEEVWWALELAhlKTFVSALPDKLDHECAEGG---------ENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552782194 173 TGALDSKS----SAALLDVFEDInsmgqTILMVTHSTAAAARAKRVLFIKDGIL 222
Cdd:TIGR00957 1449 TAAVDLETdnliQSTIRTQFEDC-----TVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-204 |
1.45e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 3 LLDVQHVKKIYKtrfqGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTiknkdAS 82
Cdd:TIGR01257 1937 ILRLNELTKVYS----GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----NI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 83 SFRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIIT 162
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHS 204
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2129
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-222 |
2.91e-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: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTL-LNILAMLDQpTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQ 94
Cdd:cd03288 28 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDI-FDGKIVIDGIDISKLPLHTL----RSRLSIILQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 95 D---------FNLLDTLSVKDNIL---LPLVLSRRPVKEMMSKVDSVSRELGihqllEKYpyeiSGGQKQRVAVARAIIT 162
Cdd:cd03288 103 DpilfsgsirFNLDPECKCTDDRLweaLEIAQLKNMVKSLPGGLDAVVTEGG-----ENF----SVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552782194 163 SPEILLADEPTGALDSKSSAALLDV----FEDinsmgQTILMVTHSTAAAARAKRVLFIKDGIL 222
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVvmtaFAD-----RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-252 |
3.57e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 20 TQVEALKDIHFTVEKGEYVAIMGESGSGKSTLlnILAMLDQptegrvyLNGMDTSTIKNKDASSFRrEKLGFVFQdfnll 99
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSL--ISAMLGE-------LSHAETSSVVIRGSVAYV-PQVSWIFN----- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 dtLSVKDNILLPLVL-SRRPVKEMmsKVDSVSRELGI---HQLLE--KYPYEISGGQKQRVAVARAIITSPEILLADEPT 173
Cdd:PLN03232 693 --ATVRENILFGSDFeSERYWRAI--DVTALQHDLDLlpgRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 174 GALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDGILynqifrgekTERQMFQEISDTLTVM------ 247
Cdd:PLN03232 769 SALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI---------KEEGTFAELSKSGSLFkklmen 839
|
....*
gi 552782194 248 AGKED 252
Cdd:PLN03232 840 AGKMD 844
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-220 |
4.05e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILA-MLDQPTE-------GRVYLNGMDTSTIknkDASSFRREKL------- 89
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAI---DAPRLARLRAvlpqaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 90 -GFVFqdfnlldtlSVKDNILL---PLVlsRRPVKEMMSKVDSVSREL---GIHQLLEKYPYEISGGQKQRVAVARAI-- 160
Cdd:PRK13547 94 pAFAF---------SAREIVLLgryPHA--RRAGALTHRDGEIAWQALalaGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 161 -------ITSPEILLADEPTGALDSKSSAALLDVFEDIN---SMGqtILMVTHSTAAAAR-AKRVLFIKDG 220
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwNLG--VLAIVHDPNLAARhADRIAMLADG 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-225 |
5.99e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLlnILAMLDQ--PTEgrvylngmdtstiknkDASSFRREKLGFVFQ---DFNLl 99
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSL--ISAMLGElpPRS----------------DASVVIRGTVAYVPQvswIFNA- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 dtlSVKDNIL--LPLVLSRRpvkEMMSKVDSVSRELGI---HQLLE--KYPYEISGGQKQRVAVARAIITSPEILLADEP 172
Cdd:PLN03130 694 ---TVRDNILfgSPFDPERY---ERAIDVTALQHDLDLlpgGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552782194 173 TGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDGILYNQ 225
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-203 |
9.23e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 26 KDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVylngmdtstiknkdassFRREKLGFVFQDFNLLDTLSVK 105
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMAVFSQHHVDGLDLS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 106 DNILLPLVLSRRPVKEmmSKVDSVSRELGIHQLLEKYP-YEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAAL 184
Cdd:PLN03073 589 SNPLLYMMRCFPGVPE--QKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
170 180
....*....|....*....|..
gi 552782194 185 ---LDVFEDinsmgqTILMVTH 203
Cdd:PLN03073 667 iqgLVLFQG------GVLMVSH 682
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-203 |
1.18e-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: 60.95 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 31 TVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRvYLNGMDTSTIKNKdassFRREKLGFVFQDfnLLD---TLSVK-- 105
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGD-YDEEPSWDEVLKR----FRGTELQDYFKK--LANgeiKVAHKpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 106 --DNIllPLVLSRRpVKEMMSKVD------SVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:COG1245 168 yvDLI--PKVFKGT-VRELLEKVDergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*.
gi 552782194 178 SKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:COG1245 245 IYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-203 |
1.34e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAmlDQP----TEGRVYLNGmdtSTIKNKDASsfRREKLGfVFQDF-N 97
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKG---ESILDLEPE--ERAHLG-IFLAFqY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 98 LLDTLSVKDNILLPLVLSRRPVKEMMSKVDS------VSRELGIHQL----LEKYPYE-ISGGQKQRVAVARAIITSPEI 166
Cdd:CHL00131 93 PIEIPGVSNADFLRLAYNSKRKFQGLPELDPlefleiINEKLKLVGMdpsfLSRNVNEgFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552782194 167 LLADEPTGALDSKssaALLDVFEDINSM---GQTILMVTH 203
Cdd:CHL00131 173 AILDETDSGLDID---ALKIIAEGINKLmtsENSIILITH 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-177 |
1.68e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 28 IHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKnkdassfRREKLGFVFQDFNLLDTLSVKDN 107
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 108 ILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKypyEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-178 |
2.22e-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: 58.96 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 20 TQVEALKDIHFTVEKG-----EYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTS----TIKNKDASSFRreklg 90
Cdd:cd03237 5 TMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVR----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 91 fvfqdfnllDTLSVKDNILLplvlsrrpvKEMMSKVDsVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLAD 170
Cdd:cd03237 80 ---------DLLSSITKDFY---------THPYFKTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
....*...
gi 552782194 171 EPTGALDS 178
Cdd:cd03237 141 EPSAYLDV 148
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-177 |
4.05e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDA-------SSFRREKLGFVFQdfn 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivyISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 98 lldtLSVKDNILLPLV--LSRRPVK-----EMMSKVDSV--------SRELGIHQLlekypyeiSGGQKQRVAVARAIIT 162
Cdd:PRK10762 345 ----MSVKENMSLTALryFSRAGGSlkhadEQQAVSDFIrlfniktpSMEQAIGLL--------SGGNQQKVAIARGLMT 412
|
170
....*....|....*
gi 552782194 163 SPEILLADEPTGALD 177
Cdd:PRK10762 413 RPKVLILDEPTRGVD 427
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-206 |
4.16e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 31 TVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNkdassFRREKLGFVFQDFnLLDTLSVkdnILL 110
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDE-----FRGSELQNYFTKL-LEGDVKV---IVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 111 PLVLSRRP------VKEMMSKVDS------VSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDS 178
Cdd:cd03236 93 PQYVDLIPkavkgkVGELLKKKDErgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 552782194 179 KSSAALLDVFEDINSMGQTILMVTHSTA 206
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-178 |
6.98e-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: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 31 TVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVylngmdTSTIKnkdaSSFrreKLGFVFQDFNLldtlSVKDNIll 110
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLK----ISY---KPQYISPDYDG----TVEEFL-- 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552782194 111 plvlsRRPVKEMMSkvDS-----VSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDS 178
Cdd:COG1245 423 -----RSANTDDFG--SSyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
23-203 |
7.16e-10 |
|
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: 57.66 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAmlDQP----TEGRVYLNGMDTSTIKNKDassfrREKLG-FV-FQdf 96
Cdd:TIGR01978 14 EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIA--GHPsyevTSGTILFKGQDLLELEPDE-----RARAGlFLaFQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 NLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEKYPYE-----------ISGGQKQRVAVARAIITSPE 165
Cdd:TIGR01978 85 YPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDeeflnrsvnegFSGGEKKRNEILQMALLEPK 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-217 |
1.24e-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: 55.79 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 17 FQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLN-ILAmldqpTEGRVYLNgmdtstiknKDASSFRREKLGFVFQD 95
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLY-----ASGKARLI---------SFLPKFSRNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDtlsvkdnillplvlsrrpvkemmskvdsvsreLGIHQL-LEKYPYEISGGQKQRVAVARAIITSPE--ILLADEP 172
Cdd:cd03238 69 QFLID--------------------------------VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552782194 173 TGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFI 217
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-220 |
1.27e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 10 KKIYKTRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYlngmdtstiknkdassfRREKL 89
Cdd:PTZ00243 661 KMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------------AERSI 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 90 GFVFQDFNLLDTlSVKDNILLplVLSRRPVKemMSKVDSVSR-ELGIHQLLEKYPYEI-------SGGQKQRVAVARAII 161
Cdd:PTZ00243 724 AYVPQQAWIMNA-TVRGNILF--FDEEDAAR--LADAVRVSQlEADLAQLGGGLETEIgekgvnlSGGQKARVSLARAVY 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782194 162 TSPEILLADEPTGALDSKSSAAlldVFEDI---NSMGQTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PTZ00243 799 ANRDVYLLDDPLSALDAHVGER---VVEECflgALAGKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-220 |
1.31e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQD--------- 95
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQSpvlfsgtvr 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNlLDTLSVKDNILLPLVLSRRPVKEMMSKvdsvsRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGA 175
Cdd:PLN03232 1328 FN-IDPFSEHNDADLWEALERAHIKDVIDR-----NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552782194 176 LDSKSSAALL-DVFEDINSMgqTILMVTHSTAAAARAKRVLFIKDG 220
Cdd:PLN03232 1402 VDVRTDSLIQrTIREEFKSC--TMLVIAHRLNTIIDCDKILVLSSG 1445
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-229 |
1.53e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 11 KIYKTRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAM-LDQ---PTEGRVYLNGMDTSTIKNkdassFRR 86
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGfhiGVEGVITYDGITPEEIKK-----HYR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 EKLGFVFQDFNLLDTLSVKDNillpLVLSRRpVKEMMSKVDSVSRELGIHQLLEKYPYE------------------ISG 148
Cdd:TIGR00956 138 GDVVYNAETDVHFPHLTVGET----LDFAAR-CKTPQNRPDGVSREEYAKHIADVYMATyglshtrntkvgndfvrgVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 149 GQKQRVAVARAIITSPEILLADEPTGALDSkSSAalldvFEDINSMgQTILMVTHSTA-----AAARAKRVLFIKDGILY 223
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDS-ATA-----LEFIRAL-KTSANILDTTPlvaiyQCSQDAYELFDKVIVLY 285
|
....*...
gi 552782194 224 N--QIFRG 229
Cdd:TIGR00956 286 EgyQIYFG 293
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-238 |
1.57e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 20 TQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLN-ILAMLDQPTEGRVYLNGMDTSTIKNKDASsfrREKLGFVFQD--- 95
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAI---RAGIAMVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTLSVKDNILLPLV--LSRRPVKEMMSKVDSVSRELGIHQLLEKYPY----EISGGQKQRVAVARAIITSPEILLA 169
Cdd:TIGR02633 348 HGIVPILGVGKNITLSVLksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 170 DEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAA-ARAKRVLFIKDGILYNQIFRGEKTERQMFQ 238
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVlGLSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-177 |
2.47e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILA---MLDqptEGRVylngmdtstIKNKDASSFR------REKLGFVFqD 95
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRI---------IYEQDLIVARlqqdppRNVEGTVY-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 F------NLLDTLsvKDNILLPLVLSRRPVKEMMSKVDSVSRELG----------IHQLLEKYPY-------EISGGQKQ 152
Cdd:PRK11147 86 FvaegieEQAEYL--KRYHDISHLVETDPSEKNLNELAKLQEQLDhhnlwqlenrINEVLAQLGLdpdaalsSLSGGWLR 163
|
170 180
....*....|....*....|....*
gi 552782194 153 RVAVARAIITSPEILLADEPTGALD 177
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-182 |
2.73e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssfrREKLGFVFQD--------- 95
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQApvlfsgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNlLDTLSVKDNILLPLVLSRRPVKemmskvDSVSRE-LGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:PLN03130 1331 FN-LDPFNEHNDADLWESLERAHLK------DVIRRNsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
....*...
gi 552782194 175 ALDSKSSA 182
Cdd:PLN03130 1404 AVDVRTDA 1411
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-177 |
3.29e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 31 TVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVylngmdTSTIKnkdaSSFrreKLGFVFQDFNLldtlSVKDnill 110
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELK----ISY---KPQYIKPDYDG----TVED---- 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 111 plVLSRRPVKEMMSKVDS-VSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:PRK13409 420 --LLRSITDDLGSSYYKSeIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-229 |
4.08e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGrvylngmdtsTIKNKDASSfrrekLGFVFQD--------F 96
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSENAN-----IGYYAQDhaydfendL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 NLLDTLS----VKDNILlplvlsrrpvkemmskvdSVSRELGihQLL------EKYPYEISGGQKQRVAVARAIITSPEI 166
Cdd:PRK15064 400 TLFDWMSqwrqEGDDEQ------------------AVRGTLG--RLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 167 LLADEPTGALDSKSSAAL---LDVFEDinsmgqTILMVTHSTA-AAARAKRVLFIKDGILYNqiFRG 229
Cdd:PRK15064 460 LVMDEPTNHMDMESIESLnmaLEKYEG------TLIFVSHDREfVSSLATRIIEITPDGVVD--FSG 518
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-222 |
5.85e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDassfrREKLGFVF-----QDFN 97
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 98 L-LD------TLSVKDNiLLPLVLsrRPVKEMmSKVDSVSRELGIH-QLLEKYPYEISGGQKQRVAVARAIITSPEILLA 169
Cdd:PRK15439 352 LyLDaplawnVCALTHN-RRGFWI--KPAREN-AVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552782194 170 DEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAAR-AKRVLFIKDGIL 222
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-204 |
6.10e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 40 IMGESGSGKSTLLNILAMLDQPTEGRVYlngmdtstIKNKDASSFRREKLGFVFQDFNLLDTLSVKDNILLplvlsRRPV 119
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIY--------YKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKF-----WSEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 120 KEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTIL 199
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVL 177
|
....*
gi 552782194 200 MVTHS 204
Cdd:PRK13541 178 LSSHL 182
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-102 |
1.13e-08 |
|
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: 55.19 E-value: 1.13e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 28 IHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtSTIKNKDASSFRREklgF--VFQDFNLLDTL 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG---QPVTADNREAYRQL---FsaVFSDFHLFDRL 421
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-190 |
1.79e-08 |
|
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: 54.56 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRFqgtqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNgmDTSTIKNKDASs 83
Cdd:TIGR03719 323 IEAENLTKAFGDKL------LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYVDQS- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frREKLG---FVFQDF-NLLDTLSVKDnillplvlsrrpvKEMMSKVdSVSR--ELGIHQllEKYPYEISGGQKQRVAVA 157
Cdd:TIGR03719 394 --RDALDpnkTVWEEIsGGLDIIKLGK-------------REIPSRA-YVGRfnFKGSDQ--QKKVGQLSGGERNRVHLA 455
|
170 180 190
....*....|....*....|....*....|...
gi 552782194 158 RAIITSPEILLADEPTGALDSKSSAALLDVFED 190
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLN 488
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-177 |
2.29e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 31 TVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRvYLNGMDTSTIKNKdassFRREKLGFVFQDfnLLD---TLSVK-- 105
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWDEVLKR----FRGTELQNYFKK--LYNgeiKVVHKpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 106 --DniLLPLVLSRRpVKEMMSKVD------SVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:PRK13409 168 yvD--LIPKVFKGK-VRELLKKVDergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-177 |
4.46e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLlnilAM------LDQPTEGRVYLNG--MDTSTIKnkDASsfrREKLGFVFQD- 95
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTEL----AMsvfgrsYGRNISGTVFKDGkeVDVSTVS--DAI---DAGLAYVTEDr 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 ----FNLLDTlsVKDNILLPLV--LSRRPV--------------KEMMSKVDSVSRELGihqllekypyEISGGQKQRVA 155
Cdd:NF040905 347 kgygLNLIDD--IKRNITLANLgkVSRRGVideneeikvaeeyrKKMNIKTPSVFQKVG----------NLSGGNQQKVV 414
|
170 180
....*....|....*....|..
gi 552782194 156 VARAIITSPEILLADEPTGALD 177
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-201 |
8.87e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 11 KIYKTRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYlngmdtstiknkdaSSFRR---- 86
Cdd:PRK10938 5 QISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ--------------SQFSHitrl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 87 --EKLGFV----FQDFNLlDTLSV-KDNillplvlSRRPVKEMM-------SKVDSVSRELGIHQLLEKYPYEISGGQKQ 152
Cdd:PRK10938 71 sfEQLQKLvsdeWQRNNT-DMLSPgEDD-------TGRTTAEIIqdevkdpARCEQLAQQFGITALLDRRFKYLSTGETR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552782194 153 RVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMV 201
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
16-214 |
1.10e-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: 51.10 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 16 RFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLL--NILAmldqptEG-RVYLNGMdtstiknkdaSSFRREKLGFV 92
Cdd:cd03270 2 IVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdTIYA------EGqRRYVESL----------SAYARQFLGQM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 93 FQDF-----NLLDTLSVKDNIL-----------------LPLVLSRRPVKEMMSKVDSVsrelGIHQL-LEKYPYEISGG 149
Cdd:cd03270 66 DKPDvdsieGLSPAIAIDQKTTsrnprstvgtvteiydyLRLLFARVGIRERLGFLVDV----GLGYLtLSRSAPTLSGG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782194 150 QKQRVAVARAI---ITSPEILLaDEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRV 214
Cdd:cd03270 142 EAQRIRLATQIgsgLTGVLYVL-DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHV 208
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-203 |
1.32e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 20 TQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAmlDQPT----EGRVYLNGMDtstiknKDASSFRREKlGFVFQD 95
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--GRKTggyiEGDIRISGFP------KKQETFARIS-GYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 96 FNLLDTLSVKDNIL------LPLVLSRrpvKEMMSKVDSVSRELGIHQLLEK---YP--YEISGGQKQRVAVARAIITSP 164
Cdd:PLN03140 962 DIHSPQVTVRESLIysaflrLPKEVSK---EEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANP 1038
|
170 180 190
....*....|....*....|....*....|....*....
gi 552782194 165 EILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTH 203
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-201 |
1.70e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 27 DIHFTVEKGEYVAIMGESGSGKSTLLN-ILAMLDQPTEGRVYLNGMDTSTIKNKDASsfrREKLGFVFQD---FNLLDTL 102
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQAI---AQGIAMVPEDrkrDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNILLPlVLSR-----------------RPVKEMmsKVDSVSRELGIHQLlekypyeiSGGQKQRVAVARAIITSPE 165
Cdd:PRK13549 357 GVGKNITLA-ALDRftggsriddaaelktilESIQRL--KVKTASPELAIARL--------SGGNQQKAVLAKCLLLNPK 425
|
170 180 190
....*....|....*....|....*....|....*.
gi 552782194 166 ILLADEPTGALDSKSSAALLDVFEDINSMGQTILMV 201
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-238 |
5.42e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 28 IHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTSTIKNKDAssFR---------REKLGFVfqdfnl 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDA--IRagimlcpedRKAEGII------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 99 lDTLSVKDNI---------LLPLVLSRRPVKEMMS------KVDSVSRELGIHQLlekypyeiSGGQKQRVAVARAIITS 163
Cdd:PRK11288 344 -PVHSVADNInisarrhhlRAGCLINNRWEAENADrfirslNIKTPSREQLIMNL--------SGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552782194 164 PEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAA-ARAKRVLFIKDGILYNQIFRGEKTERQMFQ 238
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVlGVADRIVVMREGRIAGELAREQATERQALS 490
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-220 |
5.44e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 34 KGEYVAIMGESGSGKSTLLNILA-MLDQPTEGRVYLNGmdtstiknkdassfrreklgfvfqdfnlldtlsvkdnillpl 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALArELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 113 vlsrrpvkemmSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLD------ 186
Cdd:smart00382 39 -----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552782194 187 VFEDINSMGQTILMVTH------STAAAARAKRVLFIKDG 220
Cdd:smart00382 108 LLLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLI 147
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-203 |
3.29e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNIlaMLDQ--PTEGRVYL---------------------------NGMDTST 75
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGQlqADSGRIHCgtklevayfdqhraeldpektvmdnlaEGKQEVM 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 76 IKNKDassfrREKLGFVfQDFnlldtlsvkdniLLPLVLSRRPVKEMmskvdsvsrelgihqllekypyeiSGGQKQRVA 155
Cdd:PRK11147 413 VNGRP-----RHVLGYL-QDF------------LFHPKRAMTPVKAL------------------------SGGERNRLL 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552782194 156 VARAIITSPEILLADEPTGALDSKSsaalLDVFEDINSMGQ-TILMVTH 203
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVET----LELLEELLDSYQgTVLLVSH 495
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-177 |
9.09e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 24 ALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGmdtSTIKNKDASSFRREKLGFVFQD---FNLLD 100
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNANEAINHGFALVTEErrsTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 101 TLSVKDNILLP----------LVLSRRPVKEMMSKVDSVSRELGIHQLLEKypyEISGGQKQRVAVARAIITSPEILLAD 170
Cdd:PRK10982 340 YLDIGFNSLISnirnyknkvgLLDNSRMKSDTQWVIDSMRVKTPGHRTQIG---SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
....*..
gi 552782194 171 EPTGALD 177
Cdd:PRK10982 417 EPTRGID 423
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
100-219 |
1.05e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 100 DTLSVKDNILL---PLVLSRrpvKEMMSKVDSVSRELGIHQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTGAL 176
Cdd:NF000106 99 ESFSGRENLYMigr*LDLSR---KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 552782194 177 DSKSSAallDVFEDINSM---GQTILMVTHSTAAAARAKRVLFIKD 219
Cdd:NF000106 176 DPRTRN---EVWDEVRSMvrdGATVLLTTQYMEEAEQLAHELTVID 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-223 |
3.22e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMlDQPTE--------GRVYLNGMDTSTIKnkdassfrrEKLGFVFQDF 96
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGETIWDIK---------KHIGYVSSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 97 NLlD---TLSVKDNIL--------LPLVLSRRPVKEMMSKVDSvsreLGIHQLLEKYPYE-ISGGQKQRVAVARAIITSP 164
Cdd:PRK10938 346 HL-DyrvSTSVRNVILsgffdsigIYQAVSDRQQKLAQQWLDI----LGIDKRTADAPFHsLSWGQQRLALIVRALVKHP 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782194 165 EILLADEPTGALDSKSSAALLDVFEDINSMGQT-ILMVTHSTAAAAR--AKRVLFIKDGILY 223
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAciTHRLEFVPDGDIY 482
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-203 |
3.29e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 42 GESGSGKSTLLNILAMLDQPTEGRVYLNgmdtstiknkdassfRREKLG------FVFQDFNLLDTL-----------SV 104
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLD---------------PNERLGklrqdqFAFEEFTVLDTVimghtelwevkQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 105 KDNIL-LPlvlsrrpvkEM-----------------MSKVDSVSR------ELGI----HQLLEKypyEISGGQKQRVAV 156
Cdd:PRK15064 99 RDRIYaLP---------EMseedgmkvadlevkfaeMDGYTAEARagelllGVGIpeeqHYGLMS---EVAPGWKLRVLL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552782194 157 ARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSmgqTILMVTH 203
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS---TMIIISH 210
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-205 |
4.15e-05 |
|
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: 44.35 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 27 DIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYlngmdtstiknKDassfRREKLGFVFQD-FNLLDTLsvK 105
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT-----------KP----AKGKLFYVPQRpYMTLGTL--R 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 106 DNILLPLV--------LSRRPVKEMMSKVD---SVSRELGIhQLLEKYPYEISGGQKQRVAVARAIITSPEILLADEPTG 174
Cdd:TIGR00954 533 DQIIYPDSsedmkrrgLSDKDLEQILDNVQlthILEREGGW-SAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|.
gi 552782194 175 ALDSKSSAALldvFEDINSMGQTILMVTHST 205
Cdd:TIGR00954 612 AVSVDVEGYM---YRLCREFGITLFSVSHRK 639
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-208 |
1.89e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 32 VEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMdtstiknkdassfrreklgfvfqdfnlldTLSVKDNillp 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI-----------------------------TPVYKPQ---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 112 lvlsrrpvkemmsKVDsvsrelgihqllekypyeISGGQKQRVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDI 191
Cdd:cd03222 69 -------------YID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*...
gi 552782194 192 NSMG-QTILMVTHSTAAA 208
Cdd:cd03222 118 SEEGkKTALVVEHDLAVL 135
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
147-177 |
2.86e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 2.86e-04
10 20 30
....*....|....*....|....*....|.
gi 552782194 147 SGGQKQRVAVARAIITSPEILLADEPTGALD 177
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
90-245 |
3.16e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 90 GFVFQDFNL--LDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQL-LEKYPYEISGGQKQRVAVARAI------ 160
Cdd:PRK00635 418 GKTFAEFQQmsLQELFIFLSQLPSKSLSIEEVLQGLKSRLSILIDLGLPYLtPERALATLSGGEQERTALAKHLgaelig 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 161 ITSpeILlaDEPTGALDSKSSAALLDVFEDINSMGQTILMVTHSTAAAARAKRVLFIKDGIlynQIFRGE---KTERQMF 237
Cdd:PRK00635 498 ITY--IL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGA---GIFGGEvlfNGSPREF 570
|
....*...
gi 552782194 238 QEISDTLT 245
Cdd:PRK00635 571 LAKSDSLT 578
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-72 |
7.92e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 7.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 552782194 23 EALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLD--QPTEGRVYLNGMD 72
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKD 66
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-188 |
9.26e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 25 LKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNGMDTStiknkdASSFR--REKLGFVFQDFNLLDTl 102
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG------AYGLRelRRQFSMIPQDPVLFDG- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 103 SVKDNI-------------LLPLVLSRRPVKEMMSKVDSVSRELGIHqllekypyeISGGQKQRVAVARAIIT--SPEIL 167
Cdd:PTZ00243 1399 TVRQNVdpfleassaevwaALELVGLRERVASESEGIDSRVLEGGSN---------YSVGQRQLMCMARALLKkgSGFIL 1469
|
170 180
....*....|....*....|....*
gi 552782194 168 LaDEPTG----ALDSKSSAALLDVF 188
Cdd:PTZ00243 1470 M-DEATAnidpALDRQIQATVMSAF 1493
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-236 |
1.74e-03 |
|
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: 38.36 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 39 AIMGESGSGKSTLLNILAM-----LDQPTEGRVYLNGMDTSTiknkdassfrrEKLGFVfqdfnlldTLSVKDNILLPLV 113
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYaltgeLPPNSKGGAHDPKLIREG-----------EVRAQV--------KLAFENANGKKYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 114 LSRRpvkemMSKVDSVsreLGIHQ-----LLEKYPYEISGGQKQ------RVAVARAIITSPEILLADEPTGALDSKS-S 181
Cdd:cd03240 87 ITRS-----LAILENV---IFCHQgesnwPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782194 182 AALLDVFEDINSMG--QTILmVTHSTAAAARAkrvlfikdgilyNQIFRGEKTERQM 236
Cdd:cd03240 159 ESLAEIIEERKSQKnfQLIV-ITHDEELVDAA------------DHIYRVEKDGRQK 202
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-53 |
1.87e-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: 39.23 E-value: 1.87e-03
10 20 30
....*....|....*....|....*....|....*
gi 552782194 19 GTQVEALKDIHFTVEKGEYVAIMGESGSGKSTLLN 53
Cdd:TIGR00630 618 GARENNLKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-190 |
2.63e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 4 LDVQHVKKIYKTRFqgtqveALKDIHFTVEKGEYVAIMGESGSGKSTLLNILAMLDQPTEGRVYLNgmDTSTIKNKDASs 83
Cdd:PRK11819 325 IEAENLSKSFGDRL------LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVKLAYVDQS- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 84 frREKLG---FVFQDF-NLLDTLSVKDnillplvlsrrpvKEMMSKVdSVSR--ELGIHQllEKYPYEISGGQKQRVAVA 157
Cdd:PRK11819 396 --RDALDpnkTVWEEIsGGLDIIKVGN-------------REIPSRA-YVGRfnFKGGDQ--QKKVGVLSGGERNRLHLA 457
|
170 180 190
....*....|....*....|....*....|...
gi 552782194 158 RAIITSPEILLADEPTGALDSKSSAALLDVFED 190
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
63-205 |
3.55e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.14 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 63 EGRVYLNGMDTSTIKNKDASSFRREKLGFVFQDFNLLDTLSVKDNILLPLVLSRRPVKEMMSKVDSVSRELGIHQLLEK- 141
Cdd:pfam13304 149 SPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGg 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782194 142 ----YPYEISGGQKQ---RVAVARAIITSPEILLADEPTGALDSKSSAALLDVFEDINSMGQTILMVTHST 205
Cdd:pfam13304 229 ggelPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-220 |
3.95e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.95 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782194 146 ISGGQKQRVAVA-----RAIITSPEILLaDEPTGALDSKSSAALLDVFEDINSMGQTILMVTH---STAAAARAKRVLFI 217
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHlpeLAELADKLIHIKKV 156
|
...
gi 552782194 218 KDG 220
Cdd:cd03227 157 ITG 159
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
20-56 |
8.31e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 36.77 E-value: 8.31e-03
10 20 30
....*....|....*....|....*....|....*..
gi 552782194 20 TQVEALkDIHFTVEKGEYVAIMGESGSGKSTLLNILA 56
Cdd:cd01136 53 TGVRAI-DGLLTCGEGQRIGIFAGSGVGKSTLLGMIA 88
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
14-51 |
8.51e-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: 8.51e-03
10 20 30
....*....|....*....|....*....|....*...
gi 552782194 14 KTRFQGTQVEALKDIHFTVEKGEYVAIMGESGSGKSTL 51
Cdd:TIGR00630 1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| |
