|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-264 |
6.47e-168 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 464.67 E-value: 6.47e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 1 MNPTVSINEVTKEYRIYRNNKERIKDAIWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGH 80
Cdd:PRK13546 1 MNVSVNIKNVTKEYRIYRTNKERMKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 81 IDKTGDVSVIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATI 160
Cdd:PRK13546 81 VDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 161 NPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKYEAFLKD 240
Cdd:PRK13546 161 NPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLND 240
|
250 260
....*....|....*....|....
gi 2095287788 241 FKKKSTAEQKAFRQALDENRFVIK 264
Cdd:PRK13546 241 FKKKSKAEQKEFRNKLDESRFVIK 264
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-239 |
9.63e-119 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 339.36 E-value: 9.63e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 1 MNPTVSINEVTKEYRIYRNNKERIKDAIWPKHKNK--TFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTH 78
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHEPSRSLKELLLRRRRTRreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 79 GHIDKTGDVS-VIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSIS 157
Cdd:COG1134 81 GRVEVNGRVSaLLELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 158 ATINPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKYEAF 237
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
..
gi 2095287788 238 LK 239
Cdd:COG1134 241 LA 242
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-254 |
1.65e-99 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 301.04 E-value: 1.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 1 MNPTVSINEVTKEYRIYRNNKERIKDAIWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGH 80
Cdd:PRK13545 1 MNYKVKFEHVTKKYKMYNKPFDKLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 81 IDKTGDVSVIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATI 160
Cdd:PRK13545 81 VDIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 161 NPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKYEAFLKD 240
Cdd:PRK13545 161 NPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKK 240
|
250
....*....|....
gi 2095287788 241 FKKKSTAEQKAFRQ 254
Cdd:PRK13545 241 YNQMSVEERKDFRE 254
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-225 |
9.69e-93 |
|
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: 272.48 E-value: 9.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYRIYRNNKERIKDAIWPKHKN--KTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHID 82
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGRKGevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 83 KTGDVS-VIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATIN 161
Cdd:cd03220 81 VRGRVSsLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 162 PEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFG 225
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-239 |
3.78e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.05 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYriyrnnkerikdaiwpkhknKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--- 81
Cdd:COG1131 1 IEVRGLTKRY--------------------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvl 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 82 --DKTGD-------VSVIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKL 152
Cdd:COG1131 61 geDVARDpaevrrrIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 153 GFSISATINPEILVIDEALS----VGDQTFtqksLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVE 228
Cdd:COG1131 141 GLALALLHDPELLILDEPTSgldpEARREL----WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
250
....*....|...
gi 2095287788 229 DVLPKY--EAFLK 239
Cdd:COG1131 217 ELKARLleDVFLE 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
31-244 |
5.38e-37 |
|
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: 130.75 E-value: 5.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFyALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVIAINA------------GLNG 98
Cdd:COG4555 9 KKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREarrqigvlpderGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 99 NLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE---ALSVGD 175
Cdd:COG4555 88 RLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEptnGLDVMA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 176 QTFTQKSLKkiyEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKY------EAFLKDFKKK 244
Cdd:COG4555 168 RRLLREILR---ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIgeenleDAFVALIGSE 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
35-221 |
7.40e-30 |
|
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: 110.18 E-value: 7.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 35 KTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI------------DKTGDVSVIAINAGLNGNLTG 102
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikkepeEVKRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIefkmlcmgfkkneikaltpeivefselgefiyqpvkKYSSGMRSKLGFSISATINPEILVIDEALSvGDQTFTQKS 182
Cdd:cd03230 91 RENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS-GLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095287788 183 LKK-IYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03230 134 FWElLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
23-227 |
1.60e-29 |
|
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: 110.67 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 23 RIKDaIWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHG-----HIDKTGDVSVIAINAG-- 95
Cdd:cd03263 2 QIRN-LTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtayinGYSIRTDRKAARQSLGyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 96 -----LNGNLTGMENIEFkmLCM--GFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVID 168
Cdd:cd03263 81 pqfdaLFDELTVREHLRF--YARlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 169 EALSVGDqtftQKSLKKIYEFKEDEK---TIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSV 227
Cdd:cd03263 159 EPTSGLD----PASRRAIWDLILEVRkgrSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-221 |
4.97e-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: 106.53 E-value: 4.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYriyrnnkerikdaiwpKHKNktfyALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--- 81
Cdd:cd03268 1 LKTNDLTKTY----------------GKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfd 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 82 -----DKTGDVSVIA--INA-GLNGNLTGMENIEFKMLCMGFKKNEIKaltpEIVEFSELGEFIYQPVKKYSSGMRSKLG 153
Cdd:cd03268 61 gksyqKNIEALRRIGalIEApGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 154 FSISATINPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
36-229 |
3.98e-27 |
|
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: 104.37 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 36 TFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGH--------IDKTGDV----SVIAINAGLNGNLTGM 103
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREVrrriGIVFQDLSVDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEAlSVGDQTFTQKSL 183
Cdd:cd03265 92 ENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP-TIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095287788 184 -KKIYEFKEDEK-TIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVED 229
Cdd:cd03265 171 wEYIEKLKEEFGmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-225 |
1.84e-26 |
|
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: 102.45 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYRIyrnnkerikdaiwpkhKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKT 84
Cdd:cd03266 2 ITADALTKRFRD----------------VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 85 G-DVS-----------VIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKL 152
Cdd:cd03266 66 GfDVVkepaearrrlgFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095287788 153 GFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFG 225
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
39-220 |
2.52e-25 |
|
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: 99.28 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD-VSVIAINA--------GLNGNLTGMENIEFK 109
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpLDIAARNRigylpeerGLYPKMKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 110 MLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEF 189
Cdd:cd03269 95 AQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL 174
|
170 180 190
....*....|....*....|....*....|.
gi 2095287788 190 KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:cd03269 175 ARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-221 |
1.26e-24 |
|
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: 98.17 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYRIYRNN---KERIKDAIWPKHKNKTfyALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:cd03267 1 IEVSNLSKSYRVYSKEpglIGSLKSLFKRKYREVE--ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 82 ---------DKTGDVSVIAINAG----LNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGM 148
Cdd:cd03267 79 rvaglvpwkRRKKFLRRIGVVFGqktqLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 149 RSKLGFSISATINPEILVIDEAlSVGDQTFTQkslKKIYEF-----KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEP-TIGLDVVAQ---ENIRNFlkeynRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-231 |
1.16e-23 |
|
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: 95.73 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYRiyrnnkerikdaiwpkHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHG--HID 82
Cdd:cd03258 2 IELKNVSKVFG----------------DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsvLVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 83 KTgDVSVIAiNAGL------------NGNL----TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFiyqpVKKY-- 144
Cdd:cd03258 66 GT-DLTLLS-GKELrkarrrigmifqHFNLlssrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDK----ADAYpa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 145 --SSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEF-KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03258 140 qlSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
250
....*....|
gi 2095287788 222 KDFGSVEDVL 231
Cdd:cd03258 220 VEEGTVEEVF 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
39-239 |
1.61e-23 |
|
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: 95.09 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIAINAGLNGNLTGM--------------- 103
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEV-LVDGKDITKKNLRELRRKVGLvfqnpddqlfaptve 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLgfSIsATI---NPEILVIDEALSVGDQTFTQ 180
Cdd:COG1122 95 EDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV--AI-AGVlamEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 181 KSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKYEAFLK 239
Cdd:COG1122 172 ELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
32-220 |
5.97e-23 |
|
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: 91.54 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 32 HKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDktgdvsviainaglngnltgmeniefkml 111
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 112 cmgFKKNEIKALTPEIVEfSELGeFIYQpvkkYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEFKE 191
Cdd:cd00267 58 ---IDGKDIAKLPLEELR-RRIG-YVPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE 128
|
170 180
....*....|....*....|....*....
gi 2095287788 192 DEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:cd00267 129 EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-231 |
1.65e-21 |
|
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: 90.40 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKeyrIYRNNKERIKDAIWPKH-------KNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPT 77
Cdd:cd03294 1 IKIKGLYK---IFGKNPQKAFKLLAKGKskeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 78 HGHIDKTGDvSVIAINA------------------GLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQ 139
Cdd:cd03294 78 SGKVLIDGQ-DIAAMSRkelrelrrkkismvfqsfALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 140 PVKKYSSGMRSKLGFSISATINPEILVIDEALSVGD---QTFTQKSLKKIYefKEDEKTIFFVSHNLRQVKEFCTKIAWI 216
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpliRREMQDELLRLQ--AELQKTIVFITHDLDEALRLGDRIAIM 234
|
250
....*....|....*
gi 2095287788 217 EAGQLKDFGSVEDVL 231
Cdd:cd03294 235 KDGRLVQVGTPEEIL 249
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
31-220 |
3.45e-21 |
|
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: 88.29 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI---DKTGDVSVIAINAGLNG--------- 98
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdGKDLTKLSLKELRRKVGlvfqnpddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 99 --NLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQ 176
Cdd:cd03225 88 ffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095287788 177 TFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:cd03225 168 AGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
28-221 |
7.16e-21 |
|
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: 87.55 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 28 IWPKHKNKTFyALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGH-------IDKTGD----------VSVI 90
Cdd:cd03255 9 TYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgtdISKLSEkelaafrrrhIGFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 91 AINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE- 169
Cdd:cd03255 88 FQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEp 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 170 --ALsvgDQTFTQKSLKKIYEF-KEDEKTIFFVSHNlRQVKEFCTKIAWIEAGQL 221
Cdd:cd03255 168 tgNL---DSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
9.41e-21 |
|
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: 91.12 E-value: 9.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 1 MNPTVSINEVTKEYRiyrnnkerikdaiwpkhkNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGsLTPTHGH 80
Cdd:COG1123 1 MTPLLEVRDLSVRYP------------------GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGR 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 81 IdkTGDVSV-----IAINAGLNGNLTGM---------------ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQP 140
Cdd:COG1123 62 I--SGEVLLdgrdlLELSEALRGRRIGMvfqdpmtqlnpvtvgDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 141 VKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEF-KEDEKTIFFVSHNLRQVKEFCTKIAWIEAG 219
Cdd:COG1123 140 PHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
250
....*....|..
gi 2095287788 220 QLKDFGSVEDVL 231
Cdd:COG1123 220 RIVEDGPPEEIL 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
40-172 |
1.33e-20 |
|
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: 85.39 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTGD--------VSVIAINAGLNGNLTGMENI 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqDLTDDerkslrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 107 EFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKY----SSGMRSKLGFSISATINPEILVIDEALS 172
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERpgtlSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-203 |
1.48e-20 |
|
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: 86.76 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYRiyrnnkerikdaiwpkHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--- 81
Cdd:cd03293 1 LEVRNVSKTYG----------------GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 82 -----DKTGDVSVIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFiyqpVKKY----SSGMRSKL 152
Cdd:cd03293 65 gepvtGPGPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGF----ENAYphqlSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 153 GFSISATINPEILVIDEALSVGDQtFT----QKSLKKIYEfkEDEKTIFFVSHNL 203
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDA-LTreqlQEELLDIWR--ETGKTVLLVTHDI 192
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-230 |
3.17e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.47 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAINA--------GLNG 98
Cdd:COG4152 5 KGLTKRFgdkTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGePLDPEDRRRigylpeerGLYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 99 NLTGMENIEF----KmlcmGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFsISATI-NPEILVIDEALS- 172
Cdd:COG4152 85 KMKVGEQLVYlarlK----GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL-IAALLhDPELLILDEPFSg 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 173 ---VGdqtftQKSLKK-IYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:COG4152 160 ldpVN-----VELLKDvIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
23-221 |
4.10e-20 |
|
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: 86.02 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 23 RIKD-AIWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTG----------- 85
Cdd:cd03257 3 EVKNlSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkDLLKlsrrlrkirrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 86 DVSVIAINAG--LNGNLTGMENIE--FKMLCMGFKKNEIKALTPEIVEFSELGEFIYqpvKKY----SSGMRSKLGFSIS 157
Cdd:cd03257 83 EIQMVFQDPMssLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVL---NRYphelSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 158 ATINPEILVIDEALSVGDQTfTQKS----LKKIYEfkEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03257 160 LALNPKLLIADEPTSALDVS-VQAQildlLKKLQE--ELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
35-225 |
1.74e-19 |
|
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: 83.72 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 35 KTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTG------DVSVIAINAGLNGNL 100
Cdd:cd03259 8 KTYgsvRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrDVTGvpperrNIGMVFQDYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQ---T 177
Cdd:cd03259 88 TVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAklrE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095287788 178 FTQKSLKKIyeFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFG 225
Cdd:cd03259 168 ELREELKEL--QRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-236 |
1.82e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.91 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYRIYRNN---KERIKDAIWPKHKNKTfyALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG4586 2 IEVENLSKTYRVYEKEpglKGALKGLFRREYREVE--AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 82 dktgdvSViainAGLNGNLtgmENIEFKM---LCMG--------------FK---------KNEIKALTPEIVEFSELGE 135
Cdd:COG4586 80 ------RV----LGYVPFK---RRKEFARrigVVFGqrsqlwwdlpaidsFRllkaiyripDAEYKKRLDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 136 FIYQPVKKYSSG--MRSKLgfsISATI-NPEILVIDEA---LSVgdqtFTQkslKKIYEF-----KEDEKTIFFVSHNLR 204
Cdd:COG4586 147 LLDTPVRQLSLGqrMRCEL---AAALLhRPKILFLDEPtigLDV----VSK---EAIREFlkeynRERGTTILLTSHDMD 216
|
250 260 270
....*....|....*....|....*....|..
gi 2095287788 205 QVKEFCTKIAWIEAGQLKDFGSVEDVLPKYEA 236
Cdd:COG4586 217 DIEALCDRVIVIDHGRIIYDGSLEELKERFGP 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
39-214 |
1.08e-18 |
|
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: 81.81 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTGDVSVIA-------INAGLNGN---LTGM 103
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrvfgkPLEKERKRIGyvpqrrsIDRDFPISvrdVVLM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ENIEFKMLCMGFKKNEIKALTpEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSL 183
Cdd:cd03235 94 GLYGHKGLFRRLSKADKAKVD-EALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIY 172
|
170 180 190
....*....|....*....|....*....|.
gi 2095287788 184 KKIYEFKEDEKTIFFVSHNLRQVKEFCTKIA 214
Cdd:cd03235 173 ELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
50-221 |
5.84e-18 |
|
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: 79.65 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 50 GDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-----------------DVSVIAINAGLNGNLTGMENIEFKMlc 112
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYALFPHLNVRENLAFGL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 113 MGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEFKED 192
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|
gi 2095287788 193 EK-TIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03297 181 LNiPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
39-213 |
8.03e-18 |
|
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: 78.24 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdktgdvsviainaGLNGnltgmENIEFkmlcmgfkKN 118
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI-------------LVDG-----KEVSF--------AS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 119 EIKALtpeivefsELG-EFIYQpvkkYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIF 197
Cdd:cd03216 69 PRDAR--------RAGiAMVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVI 136
|
170
....*....|....*.
gi 2095287788 198 FVSHNLRQVKEFCTKI 213
Cdd:cd03216 137 FISHRLDEVFEIADRV 152
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
31-220 |
1.65e-17 |
|
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: 77.61 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI---------------DKTGDVSVIAI 92
Cdd:cd03229 4 KNVSKRYgqkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgedltdledelpPLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 93 NAGLNGNLTGMENIEFkmlcmgfkkneikALtpeivefselgefiyqpvkkySSGMRSKLGFSISATINPEILVIDEALS 172
Cdd:cd03229 84 DFALFPHLTVLENIAL-------------GL---------------------SGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 173 VGDQTFT---QKSLKKIyeFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:cd03229 130 ALDPITRrevRALLKSL--QAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
7.77e-17 |
|
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: 79.56 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 3 PTVSINEVTKEYriyrnnkerikdaiwPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI- 81
Cdd:COG1123 259 PLLEVRNLSKRY---------------PVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIl 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 82 ---------------DKTGDVSVIAIN--AGLNGNLTGMENIEFKMLCMG-FKKNEIKALTPEIVEFSELGEFIYQpvkK 143
Cdd:COG1123 324 fdgkdltklsrrslrELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLAD---R 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 144 Y----SSGMRSKLGF-SISATiNPEILVIDEALSVGDQTfTQ-------KSLKkiyefKEDEKTIFFVSHNLRQVKEFCT 211
Cdd:COG1123 401 YphelSGGQRQRVAIaRALAL-EPKLLILDEPTSALDVS-VQaqilnllRDLQ-----RELGLTYLFISHDLAVVRYIAD 473
|
250 260
....*....|....*....|
gi 2095287788 212 KIAWIEAGQLKDFGSVEDVL 231
Cdd:COG1123 474 RVAVMYDGRIVEDGPTEEVF 493
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
40-258 |
1.73e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVS-------------------VIAINAGLNGNL 100
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRigylpqeppldddltvldtVLDGDAELRALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TGMENIEFKMLCMGFKKNEIKALTPEIVEF-------------SELG---EFIYQPVKKYSSGMRSKLG-----FSisat 159
Cdd:COG0488 94 AELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilSGLGfpeEDLDRPVSELSGGWRRRVAlaralLS---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 160 iNPEILVIDE------ALSVgdqtftqkslkkiyEFKED-----EKTIFFVSHN---LRQVkefCTKIAWIEAGQLKDF- 224
Cdd:COG0488 170 -EPDLLLLDEptnhldLESI--------------EWLEEflknyPGTVLVVSHDryfLDRV---ATRILELDRGKLTLYp 231
|
250 260 270
....*....|....*....|....*....|....
gi 2095287788 225 GSvedvlpkYEAFLkdfkkkstaEQKAFRQALDE 258
Cdd:COG0488 232 GN-------YSAYL---------EQRAERLEQEA 249
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
2.10e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.85 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 1 MNPTVSINEVTKEYRiyrnnkerikdaiwpkHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGH 80
Cdd:COG1136 1 MSPLLELRNLTKSYG----------------TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 81 IdKTGDVSVIAINAG------------------LNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVK 142
Cdd:COG1136 65 V-LIDGQDISSLSERelarlrrrhigfvfqffnLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 143 KYSSGMRSKLgfSIS-ATIN-PEILVIDE---ALsvgDqtftQKSLKKIYEF-----KEDEKTIFFVSHNLRqVKEFCTK 212
Cdd:COG1136 144 QLSGGQQQRV--AIArALVNrPKLILADEptgNL---D----SKTGEEVLELlrelnRELGTTIVMVTHDPE-LAARADR 213
|
....*....
gi 2095287788 213 IAWIEAGQL 221
Cdd:COG1136 214 VIRLRDGRI 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
40-169 |
3.15e-16 |
|
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: 74.82 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG------------DVSVIAINAGLNGNLTGMENIE 107
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPELTVRENLR 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 108 FKMLCMGFKKNEIKALtpEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:COG4133 98 FWAALYGLRADREAID--EALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
39-231 |
4.99e-16 |
|
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: 74.78 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTG-DVSVIAI--------NAGLNGNLTGME 104
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeDITGlPPHEIARlgigrtfqIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 105 NIE----------FKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE---AL 171
Cdd:cd03219 95 NVMvaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEpaaGL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 172 SVGDqtfTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:cd03219 175 NPEE---TEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
35-213 |
1.12e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 35 KTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHG---------HIDKTGDvsviAINAG------- 95
Cdd:COG3845 13 KRFggvVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGeilidgkpvRIRSPRD----AIALGigmvhqh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 96 --LNGNLTGMENIefkMLCM---GFKKNEIKALTPEIVEFSElgefiyqpvkkyssgmrsKLGFSI--SATI-------- 160
Cdd:COG3845 89 fmLVPNLTVAENI---VLGLeptKGGRLDRKAARARIRELSE------------------RYGLDVdpDAKVedlsvgeq 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 161 -----------NPEILVIDEALSV-----GDQTFtqKSLKKiyeFKEDEKTIFFVSHNLRQVKEFCTKI 213
Cdd:COG3845 148 qrveilkalyrGARILILDEPTAVltpqeADELF--EILRR---LAAEGKSIIFITHKLREVMAIADRV 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
40-225 |
2.33e-15 |
|
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: 72.08 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDktgdvsviainagLNG-NLTGMENIEF-KMLcmgfkk 117
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-------------LDGkDLASLSPKELaRKI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 118 neikALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE---ALSVGDQtftQKSLKKIYEF-KEDE 193
Cdd:cd03214 76 ----AYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEptsHLDIAHQ---IELLELLRRLaRERG 148
|
170 180 190
....*....|....*....|....*....|..
gi 2095287788 194 KTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFG 225
Cdd:cd03214 149 KTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
39-231 |
2.81e-15 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 73.20 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTGDVSVIA-------INAGLngNLTGMEni 106
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkPPRRARRRIGyvpqraeVDWDF--PITVRD-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 107 efkMLCMG----------FKKNEiKALTPEIVEFSELGEFIYQPVKKYSSGMR----------SklgfsisatiNPEILV 166
Cdd:COG1121 97 ---VVLMGrygrrglfrrPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQqrvllaralaQ----------DPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 167 IDEALSvG-DQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIeAGQLKDFGSVEDVL 231
Cdd:COG1121 163 LDEPFA-GvDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-210 |
3.52e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 35 KTFY---ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVI-----AINAG-------LN-- 97
Cdd:COG1129 12 KSFGgvkALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrsprdAQAAGiaiihqeLNlv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 98 GNLTGMENIefkmlCMG--------FKKNEIKALTPEIveFSELGEFI--YQPVKKYSSGMR-----SKlgfSISAtiNP 162
Cdd:COG1129 92 PNLSVAENI-----FLGreprrgglIDWRAMRRRAREL--LARLGLDIdpDTPVGDLSVAQQqlveiAR---ALSR--DA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 163 EILVIDE---ALSVGDqtfTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFC 210
Cdd:COG1129 160 RVLILDEptaSLTERE---VERLFRIIRRLKAQGVAIIYISHRLDEVFEIA 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-231 |
4.18e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.57 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 5 VSINEVTKEYRiyrnnkerikdaiwpkHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKT 84
Cdd:COG1135 2 IELENLSKTFP----------------TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV-LV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 85 GDVSVIAIN-AGL------------NGNL----TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIyqpvKKY--- 144
Cdd:COG1135 65 DGVDLTALSeRELraarrkigmifqHFNLlssrTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKA----DAYpsq 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 145 -SSGMRSKLGfsIS---ATiNPEILVIDEALSVGD-QTfTQ---KSLKKIyefkeDEK---TIFFVSHNLRQVKEFCTKI 213
Cdd:COG1135 141 lSGGQKQRVG--IAralAN-NPKVLLCDEATSALDpET-TRsilDLLKDI-----NRElglTIVLITHEMDVVRRICDRV 211
|
250
....*....|....*...
gi 2095287788 214 AWIEAGQLKDFGSVEDVL 231
Cdd:COG1135 212 AVLENGRIVEQGPVLDVF 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
9-231 |
4.91e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.91 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 9 EVTKEYRIYRNNKER----IKDAIWPK---HKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGH- 80
Cdd:PRK10070 6 EIKNLYKIFGEHPQRafkyIEQGLSKEqilEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 81 ------IDKTGD----------VSVIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKY 144
Cdd:PRK10070 86 lidgvdIAKISDaelrevrrkkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 145 SSGMRSKLGFSISATINPEILVIDEALSVGD---QTFTQKSLKKIYefKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:PRK10070 166 SGGMRQRVGLARALAINPDILLMDEAFSALDpliRTEMQDELVKLQ--AKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
250
....*....|
gi 2095287788 222 KDFGSVEDVL 231
Cdd:PRK10070 244 VQVGTPDEIL 253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
39-225 |
5.15e-15 |
|
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: 71.84 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGdVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIAINAGLNG-------------NLTGMEN 105
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI-RIDGQDVLKQPQKLRRrigylpqefgvypNFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 106 IEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE---ALSVGDQTFTQKS 182
Cdd:cd03264 93 LDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEptaGLDPEERIRFRNL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095287788 183 LKKIYEfkedEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFG 225
Cdd:cd03264 173 LSELGE----DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
37-241 |
1.13e-14 |
|
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: 71.11 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIAI------------NAGLNGNLTGME 104
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI-LLDGKDITNLpphkrpvntvfqNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 105 NIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGD---QTFTQK 181
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDlklRKDMQL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 182 SLKKIYefKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVlpkYE----AFLKDF 241
Cdd:cd03300 172 ELKRLQ--KELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI---YEepanRFVADF 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
42-219 |
1.45e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 42 DVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD------------VSVIAINAGLNGNLTGMENIEFK 109
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDNLDLEFTVRENLLVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 110 MLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSiSATIN-PEILVIDEALSVGDQTFTQKSLKKIYE 188
Cdd:PRK13536 139 GRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLA-RALINdPQLLILDEPTTGLDPHARHLIWERLRS 217
|
170 180 190
....*....|....*....|....*....|.
gi 2095287788 189 FKEDEKTIFFVSHNLRQVKEFCTKIAWIEAG 219
Cdd:PRK13536 218 LLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
31-245 |
3.06e-14 |
|
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: 70.02 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVS-------------VIAiNAGL 96
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGeDIReqdpvelrrkigyVIQ-QIGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 97 NGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYqpVKKY----SSGMRSKLGFSISATINPEILVIDEALS 172
Cdd:cd03295 87 FPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEF--ADRYphelSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 173 VGDqTFTQKSLKKiyEF----KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL--PKYEaFLKDFKKKS 245
Cdd:cd03295 165 ALD-PITRDQLQE--EFkrlqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILrsPAND-FVAEFVGAD 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
40-241 |
3.85e-14 |
|
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: 69.84 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-------DKTGDVSVIAI---------NAGLNGNLTGM 103
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgediSGLSEAELYRLrrrmgmlfqSGALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ENIEFKMLCMG-FKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALS----VGDQTF 178
Cdd:cd03261 96 ENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAgldpIASGVI 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 179 TQ--KSLKKIYEFkedekTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKYEAFLKDF 241
Cdd:cd03261 176 DDliRSLKKELGL-----TSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
39-220 |
5.33e-14 |
|
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: 69.52 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHG--HIDKTG--------------DVSVIAINAGLNGNLTG 102
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGsvLIDGTDinklkgkalrqlrrQIGMIFQQFNLIERLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENI---------EFKMLCMGFKKNEI-KALtpEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALS 172
Cdd:cd03256 96 LENVlsgrlgrrsTWRSLFGLFPKEEKqRAL--AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 173 VGDQTFTQK---SLKKIYefKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:cd03256 174 SLDPASSRQvmdLLKRIN--REEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
38-237 |
7.11e-14 |
|
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: 71.02 E-value: 7.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--DKTgDVSVIAINA-----GL--------NGNLtg 102
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIliDGI-DLRQIDPASlrrqiGVvlqdvflfSGTI-- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIefkmlCMGFKKNEIKALTpEIVEFSELGEFIYQPVKKY-----------SSGMRSKLGfsisatI------NPEIL 165
Cdd:COG2274 566 RENI-----TLGDPDATDEEII-EAARLAGLHDFIEALPMGYdtvvgeggsnlSGGQRQRLA------IarallrNPRIL 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 166 VIDEALSVGDQTFTQKSLKKIYEFKEDeKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVLPKYEAF 237
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKG-RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
31-225 |
9.37e-14 |
|
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: 68.44 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTG------DVSVIAINAGL 96
Cdd:cd03301 4 ENVTKRFgnvTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrDVTDlppkdrDIAMVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 97 NGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGD- 175
Cdd:cd03301 84 YPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 176 ----QTFTQksLKKIYefKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFG 225
Cdd:cd03301 164 klrvQMRAE--LKRLQ--QRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
39-231 |
1.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPthghidKTGDVSVIAINAGLNGNLTGM--------------- 103
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRP------QKGKVLVSGIDTGDFSKLQGIrklvgivfqnpetqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ------ENIEF--KMLCMgfKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGD 175
Cdd:PRK13644 91 vgrtveEDLAFgpENLCL--PPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 176 QTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVL 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
35-235 |
1.50e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.48 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 35 KTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIA-----INA-----GLNGNL 100
Cdd:PRK11607 27 KSFdgqHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpINMmfqsyALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQ 180
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 181 KSLKKIYEFKED-EKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVlpkYE 235
Cdd:PRK11607 187 RMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI---YE 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
40-229 |
2.69e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIAI----NAGLNGNLTGMENI-EFK----- 109
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVKIGYfdqhQEELDPDKTVLDELrDGApggte 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 110 -----ML-CMGFKkneikaltpeivefselGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE-----------ALS 172
Cdd:COG0488 410 qevrgYLgRFLFS-----------------GDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEptnhldietleALE 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 173 VGDQTFtqkslkkiyefkedEKTIFFVSHNlRQ-VKEFCTKIAWIEAGQLKDF-GSVED 229
Cdd:COG0488 473 EALDDF--------------PGTVLLVSHD-RYfLDRVATRILEFEDGGVREYpGGYDD 516
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
42-220 |
3.09e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.29 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 42 DVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD------------VSVIAINAGLNGNLTGMENIEFK 109
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDPDFTVRENLLVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 110 MLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEF 189
Cdd:PRK13537 105 GRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL 184
|
170 180 190
....*....|....*....|....*....|.
gi 2095287788 190 KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:PRK13537 185 LARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
40-221 |
4.22e-13 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 66.38 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTG--------DVSVIAINAGLNGNlTGMENI 106
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkPLSAmpppewrrQVAYVPQEPALWGG-TVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 107 EFkmlcmGFKKNEIKALTPEIVE-FSELG---EFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKS 182
Cdd:COG4619 95 PF-----PFQLRERKFDRERALElLERLGlppDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095287788 183 LKKIYEF-KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:COG4619 170 EELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
40-220 |
5.90e-13 |
|
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: 64.39 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVsviainaglngnltgmeniefkmlcmgfkkne 119
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 120 ikaltpEIVEFSELgefiyqpvkkySSGMRSKLGFSISATINPEILVIDEA---LSVgdqtftqKSLKKIYEF-KEDEKT 195
Cdd:cd03221 64 ------KIGYFEQL-----------SGGEKMRLALAKLLLENPNLLLLDEPtnhLDL-------ESIEALEEAlKEYPGT 119
|
170 180
....*....|....*....|....*
gi 2095287788 196 IFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:cd03221 120 VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
39-231 |
1.27e-12 |
|
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: 65.15 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTGdVSVIAINA----------GLNGNLTGM 103
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrDITG-LPPHERARagigyvpegrRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ENIEfkMLCMGFKKNEIKALTPEIVE-FSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE-----ALSVGDQT 177
Cdd:cd03224 94 ENLL--LGAYARRRAKRKARLERVYElFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEpseglAPKIVEEI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 178 FtqKSLKKIyefKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:cd03224 172 F--EAIREL---RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
38-242 |
2.07e-12 |
|
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: 65.14 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPThghidkTGDVSVIAINAGLNGNLT------GM-------- 103
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPT------SGKVTVDGLDTLDEENLWeirkkvGMvfqnpdnq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 -------ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGF-SISAtINPEILVIDEALSVGD 175
Cdd:TIGR04520 90 fvgatveDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIaGVLA-MRPDIIILDEATSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 176 QTFTQKSLKKIYEFKEDE-KTIFFVSHNLRQVkEFCTKIAWIEAGQLKDFGSVEDVLPKYEaFLKDFK 242
Cdd:TIGR04520 169 PKGRKEVLETIRKLNKEEgITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQVE-LLKEIG 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
36-231 |
3.04e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.55 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 36 TFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVIAI------------NAGLNGNLTGM 103
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLpprerrvgfvfqHYALFPHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIyqpvKKY----SSGMRSKLgfsisA-----TINPEILVIDE---AL 171
Cdd:COG1118 94 ENIAFGLRVRPPSKAEIRARVEELLELVQLEGLA----DRYpsqlSGGQRQRV-----AlaralAVEPEVLLLDEpfgAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 172 --SVGDQtfTQKSLKKIyeFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:COG1118 165 daKVRKE--LRRWLRRL--HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
40-239 |
3.22e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----------DKTGDVSVIAINA-------------- 94
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrDKDGQLKVADKNQlrllrtrltmvfqh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 95 -GLNGNLTGMENI-EFKMLCMGFKKNE-----IKALTPEIVEFSELGEFiyqPVkKYSSGMRSKLGFSISATINPEILVI 167
Cdd:PRK10619 101 fNLWSHMTVLENVmEAPIQVLGLSKQEareraVKYLAKVGIDERAQGKY---PV-HLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095287788 168 DEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL-----PKYEAFLK 239
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFgnpqsPRLQQFLK 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-230 |
3.77e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 35 KTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVI-----AINAG---------LN 97
Cdd:PRK11288 12 KTFpgvKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFasttaALAAGvaiiyqelhLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 98 GNLTGMENIefkML-----CMGF-KKNEIKALTPEIVEfsELGEFI--YQPVKKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:PRK11288 92 PEMTVAENL---YLgqlphKGGIvNRRLLNYEAREQLE--HLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 170 ALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL-KDFGSVEDV 230
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYvATFDDMAQV 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-231 |
4.04e-12 |
|
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: 64.05 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 28 IWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-------------DKTGDVSVIAIN- 93
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrrkAFRRRVQMVFQDp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 94 -AGLNGNLTGMENIEFKMLCMGFKKNE---IKALtpEIVEFSElgEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:COG1124 89 yASLHPRHTVDRILAEPLRIHGLPDREeriAELL--EQVGLPP--SFLDRYPHQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 170 ALS---VGDQTFTQKSLKKIyefKEDEK-TIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:COG1124 165 PTSaldVSVQAEILNLLKDL---REERGlTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
38-233 |
4.09e-12 |
|
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: 64.04 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAI-------------NAGLNGNLtgM 103
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhDLALADPawlrrqvgvvlqeNVLFNRSI--R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ENIEFKMLCMGFKKneikaltpeIVEFSELG---EFIYQPVKKY-----------SSGMRSKLGFSISATINPEILVIDE 169
Cdd:cd03252 94 DNIALADPGMSMER---------VIEAAKLAgahDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095287788 170 ALSVGD---QTFTQKSLKKIYefkeDEKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVLPK 233
Cdd:cd03252 165 ATSALDyesEHAIMRNMHDIC----AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
39-231 |
5.78e-12 |
|
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: 63.79 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAINA-----GL--------NGNLtgME 104
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhDVRDYTLASlrrqiGLvsqdvflfNDTV--AE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 105 NIEFKmlcmgfKKNEIKALTPEIVEFSELGEFI------YQPV-----KKYSSGMRSKLgfSISATI--NPEILVIDEAL 171
Cdd:cd03251 95 NIAYG------RPGATREEVEEAARAANAHEFImelpegYDTVigergVKLSGGQRQRI--AIARALlkDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095287788 172 SVGD---QTFTQKSLKKIYEfkedEKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:cd03251 167 SALDtesERLVQAALERLMK----NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-220 |
5.89e-12 |
|
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: 62.40 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHidktgdvsvIAINaglngnltgmeNIEFKM 110
Cdd:cd03228 9 SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE---------ILID-----------GVDLRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 111 LCMGFKKNEIKALTPEIVEFSE-LGEFIyqpvkkYSSGMRSKLgfSISATI--NPEILVIDEALSVGDQTFTQKSLKKIY 187
Cdd:cd03228 69 LDLESLRKNIAYVPQDPFLFSGtIRENI------LSGGQRQRI--AIARALlrDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|...
gi 2095287788 188 EFKEDeKTIFFVSHNLRQVKeFCTKIAWIEAGQ 220
Cdd:cd03228 141 ALAKG-KTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
37-230 |
6.48e-12 |
|
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: 63.35 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGG-----SLTPTHGHID------KTGDVSVIAINAGLngnltGM-- 103
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLldgkdiYDLDVDVLELRRRV-----GMvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 -----------ENIEFKMLCMGFKKNEIKAltpEIVEFS----ELGEFIYQPVKKY--SSGMRSKLgfSISATI--NPEI 164
Cdd:cd03260 88 qkpnpfpgsiyDNVAYGLRLHGIKLKEELD---ERVEEAlrkaALWDEVKDRLHALglSGGQQQRL--CLARALanEPEV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 165 LVIDEALSVGDQTFTQKSLKKIYEFKeDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:cd03260 163 LLLDEPTSALDPISTAKIEELIAELK-KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
50-245 |
7.36e-12 |
|
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: 65.42 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 50 GDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-----DVSVIAINAG-------LNGNLTGMENIEFKMLCMGFKK 117
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltNISDVHQNMGycpqfdaIDDLLTGREHLYLYARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 118 NEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIF 197
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVV 2124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095287788 198 FVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKY-EAFLKDFKKKS 245
Cdd:TIGR01257 2125 LTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFgDGYIVTMKIKS 2173
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-235 |
7.38e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDV-----SVIAINAGLNGNLTGM----------- 103
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkDIFQIDAIKLRKEVGMvfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ---ENIEFKMLCMGFK-KNEIKALTPEIVE----FSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGD 175
Cdd:PRK14246 106 siyDNIAYPLKSHGIKeKREIKKIVEECLRkvglWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 176 QTFTQKSLKKIYEFKeDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL--PKYE 235
Cdd:PRK14246 186 IVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFtsPKNE 246
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
39-210 |
8.89e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGdvsvIAINAGLNGNLTGM----ENIE--FKMLC 112
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG----QPTRQALQKNLVAYvpqsEEVDwsFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 113 -----------MGF---KKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTF 178
Cdd:PRK15056 98 edvvmmgryghMGWlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190
....*....|....*....|....*....|..
gi 2095287788 179 TQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFC 210
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
33-235 |
9.15e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.05 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 33 KNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAiNAGLNG------------N 99
Cdd:PRK11153 14 GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqDLTALS-EKELRKarrqigmifqhfN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 100 L----TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFiyqpVKKY----SSGMRSKLGFSISATINPEILVIDEAL 171
Cdd:PRK11153 93 LlssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDK----ADRYpaqlSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 172 SVGDQTFTQ---KSLKKIYefKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL--PKYE 235
Cdd:PRK11153 169 SALDPATTRsilELLKDIN--RELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFshPKHP 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
37-230 |
1.84e-11 |
|
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: 62.36 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAI---NAG-------LNGNLTGMEN 105
Cdd:cd03296 15 FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGeDATDVPVqerNVGfvfqhyaLFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 106 IEF----KMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDqTFTQK 181
Cdd:cd03296 95 VAFglrvKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD-AKVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 182 SLKKIYEFKEDEK--TIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:cd03296 174 ELRRWLRRLHDELhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
40-231 |
2.41e-11 |
|
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: 61.98 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI---DKtgDVS---------VIAI---NAGLNGNLTGME 104
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldGR--DLAslsrrelarRIAYvpqEPPAPFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 105 NIEfkmlcMGFK--KNEIKALTPE---IV----EFSELGEFIYQPVKKYSSGMRSKlgfsisATI------NPEILVIDE 169
Cdd:COG1120 95 LVA-----LGRYphLGLFGRPSAEdreAVeealERTGLEHLADRPVDELSGGERQR------VLIaralaqEPPLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 170 ---ALSVGDQTFTQKSLKKIyeFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:COG1120 164 ptsHLDLAHQLEVLELLRRL--ARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-81 |
4.17e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.64 E-value: 4.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 31 KHKNKTFY--------ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG1101 5 KNLSKTFNpgtvnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI 63
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
39-221 |
4.89e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 60.84 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIAINAG------------------LNgNL 100
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQV-LVNGQDLSRLKRReipylrrrigvvfqdfrlLP-DR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGfsIS-ATIN-PEILVIDE---ALsvgD 175
Cdd:COG2884 95 TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVA--IArALVNrPELLLADEptgNL---D 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095287788 176 QTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:COG2884 170 PETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-226 |
5.16e-11 |
|
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: 60.50 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 29 WPKH-----KN-KTFYA------LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAINAg 95
Cdd:cd03369 1 WPEHgeievENlSVRYApdlppvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGiDISTIPLED- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 96 LNGNLTGMEniEFKMLCMGFKKNEikaLTPEiVEFSElgEFIYQPVK------KYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:cd03369 80 LRSSLTIIP--QDPTLFSGTIRSN---LDPF-DEYSD--EEIYGALRvsegglNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 170 ALSVGD---QTFTQKSLKKiyEFKedEKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGS 226
Cdd:cd03369 152 ATASIDyatDALIQKTIRE--EFT--NSTILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
34-233 |
5.53e-11 |
|
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: 60.70 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 34 NKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAINAGLNG-----------NLT 101
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGiDIRDISRKSLRSMigvvlqdtflfSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 102 GMENIEfkmlcmgFKKNEIKAlTPEIVEFSELG--EFIYQPVKKY-----------SSGMRSKLGFSISATINPEILVID 168
Cdd:cd03254 93 IMENIR-------LGRPNATD-EEVIEAAKEAGahDFIMKLPNGYdtvlgenggnlSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 169 EALS---VGDQTFTQKSLKKIYEfkedEKTIFFVSHNLRQVKeFCTKIAWIEAGQLKDFGSVEDVLPK 233
Cdd:cd03254 165 EATSnidTETEKLIQEALEKLMK----GRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDELLAK 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
39-239 |
6.88e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIAIN-----------AGLNGNL------- 100
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-TVGDIVVSSTSkqkeikpvrkkVGVVFQFpesqlfe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 -TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELG-EFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTF 178
Cdd:PRK13643 100 eTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 179 TQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKYEaFLK 239
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVD-FLK 239
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
39-205 |
7.79e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.87 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG--------DVSVIAINAGLNGNLTGMENIEFKM 110
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvegpgaERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 111 LCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDqTFT----QKSLKKI 186
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD-AFTreqmQTLLLKL 174
|
170
....*....|....*....
gi 2095287788 187 YefKEDEKTIFFVSHNLRQ 205
Cdd:PRK11248 175 W--QETGKQVLLITHDIEE 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
40-231 |
8.16e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.40 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD-------------VSVIAINAGLNGNLTGMENI 106
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 107 EfkmlcMGfkkneikaLTPEIVEFSELGE-----------------FIYQPVKKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:PRK09536 99 E-----MG--------RTPHRSRFDTWTEtdraaveramertgvaqFADRPVTSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 170 ALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
53-236 |
9.66e-11 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 60.07 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 53 IGLVGINGSGKSTLSNMIGGSLTPTHGH-IDKTGDVSVIAINAGLNGNLTGMENIEFKMLCMGFKKNEIKALTpeiVEFS 131
Cdd:PRK15177 16 IGILAAPGSGKTTLTRLLCGLDAPDEGDfIGLRGDALPLGANSFILPGLTGEENARMMASLYGLDGDEFSHFC---YQLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 132 ELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTfTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCT 211
Cdd:PRK15177 93 QLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNA-TQLRMQAALACQLQQKGLIVLTHNPRLIKEHCH 171
|
170 180
....*....|....*....|....*...
gi 2095287788 212 KIAWIEAGQL---KDFGSVEDVLPKYEA 236
Cdd:PRK15177 172 AFGVLLHGKItmcEDLAQATALFEQYQS 199
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
40-231 |
1.65e-10 |
|
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: 59.61 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIAI-----------------NAGLNGNLTG 102
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI-LVDGQDITGLsekelyelrrrigmlfqGGALFDSLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIEFKML-CMGFKKNEIKALTPEIVEFSELGEFIyqpvKKY----SSGMRSKLGF--SISatINPEILVIDEALS--- 172
Cdd:COG1127 100 FENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAA----DKMpselSGGMRKRVALarALA--LDPEILLYDEPTAgld 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 173 -VGDQTFTQ--KSLKKIYEFkedekTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:COG1127 174 pITSAVIDEliRELRDELGL-----TSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
39-221 |
1.81e-10 |
|
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: 59.67 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTG-DVSVIAiNAGLN---------GNLTGM 103
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrDITGlPPHRIA-RLGIArtfqnprlfPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ENIefkMLCMGFKKNE--IKALTP----------------EIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEIL 165
Cdd:COG0411 98 ENV---LVAAHARLGRglLAALLRlprarreereareraeELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 166 VIDE--A-LSVGDqtfTQKSLKKIYEFKEDEK-TIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:COG0411 175 LLDEpaAgLNPEE---TEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
39-231 |
1.87e-10 |
|
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: 60.59 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHID-KTGDVSVIAINAGLNG------------------- 98
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMTKPGPDGrgrakryigilhqeydlyp 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 99 ------NLTGMENIEFKmlcmgFKKNEIKAL-TPEIVEFSElgEFIYQPVKKY----SSGMRSKLGFSISATINPEILVI 167
Cdd:TIGR03269 379 hrtvldNLTEAIGLELP-----DELARMKAViTLKMVGFDE--EKAEEILDKYpdelSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 168 DEALSVGDQTFTQKSLKKIYEFKED-EKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
31-222 |
2.53e-10 |
|
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: 58.09 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdkTGDVSVIAInagLNGNLtgmeniefkm 110
Cdd:cd03247 9 SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI--TLDGVPVSD---LEKAL---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 111 lcmgfkKNEIKALTPEIVEFSELgefIYQPV-KKYSSGMRSKLGFSISATINPEILVIDEAlSVG-DQTFTQKSLKKIYE 188
Cdd:cd03247 74 ------SSLISVLNQRPYLFDTT---LRNNLgRRFSGGERQRLALARILLQDAPIVLLDEP-TVGlDPITERQLLSLIFE 143
|
170 180 190
....*....|....*....|....*....|....
gi 2095287788 189 FKEDeKTIFFVSHNLRQVKEFcTKIAWIEAGQLK 222
Cdd:cd03247 144 VLKD-KTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-230 |
6.01e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.49 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDV----SVIAINAGLngnltGM--- 103
Cdd:PRK13635 14 RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseeTVWDVRRQV-----GMvfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ------------ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEAL 171
Cdd:PRK13635 89 npdnqfvgatvqDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 172 SVGDQTFTQKSLKKIYEFKEDEK-TIFFVSHNLRQVKeFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-206 |
7.30e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.20 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 32 HKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVIAiNAGLNGNLTGM-------- 103
Cdd:PRK13650 15 KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE-NVWDIRHKIGMvfqnpdnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 -------ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQ 176
Cdd:PRK13650 94 fvgatveDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190
....*....|....*....|....*....|.
gi 2095287788 177 TFTQKSLKKIYEFKED-EKTIFFVSHNLRQV 206
Cdd:PRK13650 174 EGRLELIKTIKGIRDDyQMTVISITHDLDEV 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-207 |
7.69e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 24 IKD-AIWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdktgdvsviainAGLNGNLTG 102
Cdd:PRK15079 20 IKDgKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV------------AWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIEFKMlcmgfKKNEIK--------ALTPEIVefseLGEFIYQPVKKY------------------------------ 144
Cdd:PRK15079 88 MKDDEWRA-----VRSDIQmifqdplaSLNPRMT----IGEIIAEPLRTYhpklsrqevkdrvkammlkvgllpnlinry 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 145 ----SSGMRSKLGFSISATINPEILVIDE---ALSVGDQTFTQKSLKKIYefKEDEKTIFFVSHNLRQVK 207
Cdd:PRK15079 159 phefSGGQCQRIGIARALILEPKLIICDEpvsALDVSIQAQVVNLLQQLQ--REMGLSLIFIAHDLAVVK 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
39-235 |
7.95e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.89 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPtHGHIDKTGDVSVIAINAGLNGNL------------------ 100
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP-DDNPNSKITVDGITLTAKTVWDIrekvgivfqnpdnqfvga 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQ 180
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 181 KSLKKIYEFKEDEK-TIFFVSHNLRQVkEFCTKIAWIEAGQLKDFGSVEDVLPKYE 235
Cdd:PRK13640 181 QILKLIRKLKKKNNlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
38-231 |
9.26e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 58.64 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSV-----------IAI---NAGL-NGNLtg 102
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-LIDGVDIrdltleslrrqIGVvpqDTFLfSGTI-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIEFkmlcmgFKKN----EIKaltpEIVEFSELGEFIYQPVKKY-----------SSGMRSKLgfSISATI--NPEIL 165
Cdd:COG1132 431 RENIRY------GRPDatdeEVE----EAAKAAQAHEFIEALPDGYdtvvgergvnlSGGQRQRI--AIARALlkDPPIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 166 VIDEALSVGDqTFT----QKSLKKIYEfkedEKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:COG1132 499 ILDEATSALD-TETealiQEALERLMK----GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-136 |
1.20e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 57.80 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 1 MNPTVSINEVTKEYriyrnnkerikdaiwpkhknKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGH 80
Cdd:COG3842 2 AMPALELENVSKRY--------------------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 81 I-----DKTG------DVSVIAINAGLNGNLTGMENIEF--KMlcMGFKKNEIKALTPEIVEFSELGEF 136
Cdd:COG3842 62 IlldgrDVTGlppekrNVGMVFQDYALFPHLTVAENVAFglRM--RGVPKAEIRARVAELLELVGLEGL 128
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
39-81 |
1.70e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.86 E-value: 1.70e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
40-221 |
1.84e-09 |
|
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: 55.30 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGdvsvIAINAGLNGNLTGmeniefkmlCMGFKKNE 119
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWDPNELGD---------HVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 120 IKALTPEIVEfselgefiyqpvKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFV 199
Cdd:cd03246 85 DELFSGSIAE------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVI 152
|
170 180
....*....|....*....|..
gi 2095287788 200 SHNLRQVKEfCTKIAWIEAGQL 221
Cdd:cd03246 153 AHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
39-230 |
2.07e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 56.62 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI---------DKTG------DVSVIAINAglNGNL--- 100
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikyDKKSllevrkTVGIVFQNP--DDQLfap 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQ 180
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095287788 181 KSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
38-206 |
4.14e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.77 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGdvsvIAINAG----LNGNL------------- 100
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG----ITISKEnlkeIRKKIgiifqnpdnqfig 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 -TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDqtft 179
Cdd:PRK13632 99 aTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD---- 174
|
170 180 190
....*....|....*....|....*....|..
gi 2095287788 180 QKSLKKIYEF-----KEDEKTIFFVSHNLRQV 206
Cdd:PRK13632 175 PKGKREIKKImvdlrKTRKKTLISITHDMDEA 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
39-230 |
4.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.82 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--------DKTGDVSVIAINAGLNGNL--------TG 102
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditDKKVKLSDIRKKVGLVFQYpeyqlfeeTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKY--SSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQ 180
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFelSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 181 KSLKKIYEFKEDEK-TIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK13637 182 EILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
31-231 |
7.50e-09 |
|
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: 54.47 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHID-KTGDVSVIAIN-------------AGL 96
Cdd:cd03218 7 SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILlDGQDITKLPMHkrarlgigylpqeASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 97 NGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE------A 170
Cdd:cd03218 87 FRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEpfagvdP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 171 LSVGDqtftqksLKK-IYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:cd03218 167 IAVQD-------IQKiIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
33-231 |
7.53e-09 |
|
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: 55.44 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 33 KNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTP---THGHI-----------DKT------GDVSVI-- 90
Cdd:COG0444 14 RRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEIlfdgedllklsEKElrkirgREIQMIfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 91 -AINAgLNGNLT-G---MENIefkMLCMGFKKNEIKALTPEIVEfsELGefIYQP---VKKY----SSGMRSKLGFSISA 158
Cdd:COG0444 94 dPMTS-LNPVMTvGdqiAEPL---RIHGGLSKAEARERAIELLE--RVG--LPDPerrLDRYphelSGGMRQRVMIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 159 TINPEILVIDE---AL--SVGDQTFTQ-KSLKkiyefKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:COG0444 166 ALEPKLLIADEpttALdvTIQAQILNLlKDLQ-----RELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
40-210 |
7.71e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG------------DVSVIAINAGLNGNLTGMEN-- 105
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlctyqkQLCFVGHRSGINPYLTLRENcl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 106 --IEFKMLCMGFKkneikaltpEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSL 183
Cdd:PRK13540 97 ydIHFSPGAVGIT---------ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170 180 190
....*....|....*....|....*....|..
gi 2095287788 184 KKIYEFKEDEKTIFFVSH-----NLRQVKEFC 210
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHqdlplNKADYEEYH 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
40-82 |
7.91e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 7.91e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHID 82
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR 60
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
31-229 |
8.71e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 54.69 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTfyALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG----------------DVSVI---A 91
Cdd:PRK10419 21 KHQHQT--VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQMVfqdS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 92 INAgLNGNLTGMENIEFKML-CMGFKKNEIKALTPEIVEFSELGEFIYQPV-KKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:PRK10419 99 ISA-VNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 170 ALSVGDQTFTQKSLKKIYEFKEDEKTIF-FVSHNLRQVKEFCTKIAWIEAGQLkdfgsVED 229
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTAClFITHDLRLVERFCQRVMVMDNGQI-----VET 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
39-81 |
1.03e-08 |
|
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: 55.53 E-value: 1.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI 394
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
29-221 |
1.06e-08 |
|
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: 54.13 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 29 WPKHKNKtfyALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--DKTG----DVSVIAINAG------- 95
Cdd:cd03245 12 YPNQEIP---ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVllDGTDirqlDPADLRRNIGyvpqdvt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 96 -LNGNLTgmENIEFKMLCMgfKKNEIKaltpEIVEFSELGEFIYQPVKKY-----------SSGMRSKLGFSISATINPE 163
Cdd:cd03245 89 lFYGTLR--DNITLGAPLA--DDERIL----RAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 164 ILVIDEALSVGDQTFTQKSLKKIYEFKEDeKTIFFVSHNLRqVKEFCTKIAWIEAGQL 221
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-230 |
1.28e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG--------------DVSVIAIN 93
Cdd:PRK09700 9 AGIGKSFgpvHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 94 AGLNGNLTGMENIEFKMLCMgfKK---------NEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEI 164
Cdd:PRK09700 89 LSVIDELTVLENLYIGRHLT--KKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 165 LVIDEALSvgdqTFTQKSLKKIY----EFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK09700 167 IIMDEPTS----SLTNKEVDYLFlimnQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-233 |
1.33e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.97 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG----DVSV------IAI---NAGLNgNLTGMEN 105
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirTVTRaslrrnIAVvfqDAGLF-NRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 106 IEfkmlcMGfKKNEIKALTPEIVEFSELGEFIYQPVKKY-----------SSGMRSKLgfSISATI--NPEILVIDEALS 172
Cdd:PRK13657 429 IR-----VG-RPDATDEEMRAAAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRL--AIARALlkDPPILILDEATS 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 173 VGDQTfTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVLPK 233
Cdd:PRK13657 501 ALDVE-TEAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVAR 559
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
40-239 |
1.54e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.94 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--------DKTGDVSVIAINAG-------LNGNLTGME 104
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkvnDPKVDERLIRQEAGmvfqqfyLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 105 NIEFKML-CMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSL 183
Cdd:PRK09493 97 NVMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 184 KKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL-----PKYEAFLK 239
Cdd:PRK09493 177 KVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIknppsQRLQEFLQ 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
38-235 |
1.94e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.08 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG---DVSVIAInAGLNGNLtGM----------- 103
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpiDYSRKGL-MKLRESV-GMvfqdpdnqlfs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ----ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFT 179
Cdd:PRK13636 98 asvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095287788 180 QKSLKKIYEF-KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKYE 235
Cdd:PRK13636 178 SEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
39-226 |
1.96e-08 |
|
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: 53.27 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAINAgLNGNLTGM------------EN 105
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvDISKIGLHD-LRSRISIIpqdpvlfsgtirSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 106 IEFkmlcmgFKKNEIKALTpEIVEFSELGEFIYQPVKK-----------YSSGMRSKLGFSISATINPEILVIDEAL-SV 173
Cdd:cd03244 98 LDP------FGEYSDEELW-QALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARALLRKSKILVLDEATaSV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 174 GDQTFT--QKSLKKiyEFKedEKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGS 226
Cdd:cd03244 171 DPETDAliQKTIRE--AFK--DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
39-221 |
4.84e-08 |
|
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: 52.02 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVS---------------VIAINAGLNGNLTG 102
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSdlrgraipylrrkigVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKS 182
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095287788 183 LKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
39-230 |
6.41e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.09 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIG--GSLTPThghIDKTGDVSVIAINAGLNGNLT-------GM------ 103
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPE---VTITGSIVYNGHNIYSPRTDTvdlrkeiGMvfqqpn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 -------ENIEFKMLCMGFKKneiKALTPEIVEFSELGEFIYQPVKKY--------SSGMRSKLGFSISATINPEILVID 168
Cdd:PRK14239 97 pfpmsiyENVVYGLRLKGIKD---KQVLDEAVEKSLKGASIWDEVKDRlhdsalglSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 169 EALSVGDQTFTQKSLKKIYEFKEDeKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-221 |
6.49e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.40 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 24 IKDAIWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDvSVIAINAGLNGNLTGM 103
Cdd:PRK13642 7 VENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWNLRRKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ---------------ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVID 168
Cdd:PRK13642 86 vfqnpdnqfvgatveDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 169 EALSVGDQTFTQKSLKKIYEFKED-EKTIFFVSHNLRQVKEfCTKIAWIEAGQL 221
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
40-233 |
6.83e-08 |
|
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: 51.85 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAINAgLNG------------NLTGMENI 106
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqDIREVTLDS-LRRaigvvpqdtvlfNDTIGYNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 107 EFkmlcmgfkkNEIKALTPEIVEFSELGEfIYQPVKKYSSGMRSKLG-------------FSISATI--NPEILVIDEAL 171
Cdd:cd03253 96 RY---------GRPDATDEEVIEAAKAAQ-IHDKIMRFPDGYDTIVGerglklsggekqrVAIARAIlkNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 172 SVGDQTFTQKSLKKIYEFKEDeKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVLPK 233
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKG-RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
38-207 |
6.83e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD----VSVIAINAGLNGNL------------- 100
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmskLSSAAKAELRNQKLgfiyqfhhllpdf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQ 180
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180
....*....|....*....|....*...
gi 2095287788 181 KSLKKIYEFKEDEKTIFF-VSHNLRQVK 207
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLvVTHDLQLAK 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
40-221 |
6.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGdvSVIAINAGlNGNL------------------- 100
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG--YHITPETG-NKNLkklrkkvslvfqfpeaqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 --TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGE-FIYQPVKKYSSGMRSKLGFSISATINPEILVIDEAlSVGDQT 177
Cdd:PRK13641 100 enTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP-AAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095287788 178 FTQKSLKKIY-EFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:PRK13641 179 EGRKEMMQLFkDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
39-231 |
7.24e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHG------HIDKTGDVS-----VIAINAGLNGNLTGMENIE 107
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGelliddHPLHFGDYSyrsqrIRMIFQDPSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 108 fKMLCMGFKKNeiKALTPEIVEfselgEFIYQPVKK--------------YSSGMRSKLGFSISATINPEILVIDEALSV 173
Cdd:PRK15112 108 -QILDFPLRLN--TDLEPEQRE-----KQIIETLRQvgllpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 174 GDQTFTQKSLKKIYEFKEDEKTIF-FVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGISYiYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
33-235 |
7.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.01 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 33 KNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPThghidkTGDVSVIAINAGLNGNL------TGM--- 103
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPS------EGKVYVDGLDTSDEENLwdirnkAGMvfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ------------ENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEAL 171
Cdd:PRK13633 93 npdnqivativeEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 172 SVGDQTFTQKSLKKIYEF-KEDEKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVLPKYE 235
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-220 |
9.05e-08 |
|
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: 51.32 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 23 RIKDA--IWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVIAINAGL-NGN 99
Cdd:cd03250 2 SVEDAsfTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIqNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 100 LTgmENIEFkmlcmGFKKNE------IKA--LTPEIVEFS-----ELGEfiyqpvKkyssgmrsklGFSIS----ATI-- 160
Cdd:cd03250 82 IR--ENILF-----GKPFDEeryekvIKAcaLEPDLEILPdgdltEIGE------K----------GINLSggqkQRIsl 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 161 ------NPEILVIDEALS-----VGDQTFtQKSLKKiyeFKEDEKTIFFVSHNLRQVKEfCTKIAWIEAGQ 220
Cdd:cd03250 139 aravysDADIYLLDDPLSavdahVGRHIF-ENCILG---LLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
39-89 |
9.26e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 51.08 E-value: 9.26e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSV 89
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV 57
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
37-230 |
9.53e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 52.00 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSV---------IAI---NAGLNGNLTGME 104
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI-LIGGRDVtdlppkdrnIAMvfqSYALYPHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 105 NIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSK--LGFSIsaTINPEILVIDEALSVGD-----QT 177
Cdd:COG3839 95 NIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRvaLGRAL--VREPKVFLLDEPLSNLDaklrvEM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 178 FTQksLKKIyeFKEDEKTIFFVSHNlrQVkE---FCTKIAWIEAGQLKDFGSVEDV 230
Cdd:COG3839 173 RAE--IKRL--HRRLGTTTIYVTHD--QV-EamtLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
40-108 |
1.23e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.64 E-value: 1.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI----DKTGDVSVIAINA------GLNGNLTGMENIEF 108
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldgGDIDDPDVAEACHylghrnAMKPALTVAENLEF 96
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
39-81 |
1.46e-07 |
|
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: 52.08 E-value: 1.46e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
40-221 |
1.87e-07 |
|
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: 50.55 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD-------------VSVIAINAGLNGNlTGMENI 106
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFAR-SLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 107 EFKMLCMGFKKNEIKALTPEIVEF-SELGEFIYQPV----KKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQK 181
Cdd:cd03248 109 AYGLQSCSFECVKEAAQKAHAHSFiSELASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095287788 182 SLKKIYEFKEDeKTIFFVSHNLRQVkEFCTKIAWIEAGQL 221
Cdd:cd03248 189 VQQALYDWPER-RTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
40-229 |
2.15e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSV--------------IAINAGLNGNLTGMEN 105
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpakahqlgiylVPQEPLLFPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 106 IEFKMLCMGFKKNEIKALTPEI-------VEFSELGEFIYQPVKKYSSGMRsklgfsisatiNPEILVIDE---ALSVGD 175
Cdd:PRK15439 107 ILFGLPKRQASMQKMKQLLAALgcqldldSSAGSLEVADRQIVEILRGLMR-----------DSRILILDEptaSLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 176 qtfTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVED 229
Cdd:PRK15439 176 ---TERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
40-254 |
4.75e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAINA----------------GLNGNLTG 102
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqDVATLDADAlaqlrrehfgfifqryHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFI-YQPvKKYSSGMRSKLgfSIS-ATIN-PEILVIDEALSVGDQTFT 179
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVeYQP-SQLSGGQQQRV--SIArALMNgGQVILADEPTGALDSHSG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 180 QKSLKKIYEFKEDEKTIFFVSHNlRQVKEFCTKIAWIEAGQLkdfgsVEDVLPKYEAFLKDFKKKSTAEQKAFRQ 254
Cdd:PRK10535 181 EEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI-----VRNPPAQEKVNVAGGTEPVVNTASGWRQ 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
42-221 |
5.76e-07 |
|
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: 50.40 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 42 DVTFqaYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTGDVSVIAINAG-------LNGNLTGMENIEFK 109
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkDIETNLDAVRQSLGmcpqhniLFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 110 MLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSvGDQTFTQKSLKKIYEF 189
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS-GVDPYSRRSIWDLLLK 1106
|
170 180 190
....*....|....*....|....*....|..
gi 2095287788 190 KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-250 |
7.06e-07 |
|
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: 49.80 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGG--SLTPTHGHI-------DKTGDVSV------------------ 89
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcEKCGYVERpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 90 ------------------IAI----NAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSG 147
Cdd:TIGR03269 93 evdfwnlsdklrrrirkrIAImlqrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 148 MRSKLGFSISATINPEILVIDEALSVGD-QT--FTQKSLKKIyeFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDF 224
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDpQTakLVHNALEEA--VKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
250 260
....*....|....*....|....*.
gi 2095287788 225 GSVEDVLPKYEAFLKDFKKKSTAEQK 250
Cdd:TIGR03269 251 GTPDEVVAVFMEGVSEVEKECEVEVG 276
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
44-81 |
9.29e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 48.60 E-value: 9.29e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2095287788 44 TFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI 56
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
40-230 |
1.01e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.93 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAI----------NAGLNGNLTGMENIEF 108
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtDVSRLHArdrkvgfvfqHYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 109 --KMLCMGFKKN--EIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE---ALSVGDQTFTQK 181
Cdd:PRK10851 98 glTVLPRRERPNaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEpfgALDAQVRKELRR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095287788 182 SLKKIYEfkEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK10851 178 WLRQLHE--ELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
37-246 |
1.14e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHID------------KTGDVSVIAINAGLNG------ 98
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktKEKEKVLEKLVIQKTRfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 99 --------------------NLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGE-FIYQPVKKYSSGMRSKLGFSIS 157
Cdd:PRK13651 100 ikeirrrvgvvfqfaeyqlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 158 ATINPEILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLpKYEAF 237
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL-SDNKF 258
|
....*....
gi 2095287788 238 LKDFKKKST 246
Cdd:PRK13651 259 LIENNMEPP 267
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
31-220 |
1.86e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 48.67 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGsltpTHGHIDKTGD--------------------V 87
Cdd:TIGR02633 5 KGIVKTFggvKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG----VYPHGTWDGEiywsgsplkasnirdteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 88 SVIAINAGLNGNLTGMENIefkmlcmgFKKNEIkALTPEIVEFSEL----GEFIYQ----------PVKKYSSGMRSKLg 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENI--------FLGNEI-TLPGGRMAYNAMylraKNLLRElqldadnvtrPVGDYGGGQQQLV- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 154 fSISATINPE--ILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:TIGR02633 151 -EIAKALNKQarLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
31-221 |
1.87e-06 |
|
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: 47.52 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--------DKTGDVSVIAINAG---- 95
Cdd:cd03262 4 KNLHKSFgdfHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltDDKKNINELRQKVGmvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 96 ---LNGNLTGMENI-EFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEAL 171
Cdd:cd03262 84 qfnLFPHLTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095287788 172 SVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
40-169 |
2.10e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.80 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVIAINAGLNGNLTGMENIE-FKMLCMGFKKN 118
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNrFLRLRPGTKKE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 119 EI-KALtpeivEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:PRK09544 100 DIlPAL-----KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
42-221 |
2.47e-06 |
|
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: 47.10 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 42 DVTFQAyaGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-----------DVSVIAINAGLNGNLTGMENIefkm 110
Cdd:cd03298 18 DLTFAQ--GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFAHLTVEQNV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 111 lcmGFKKNEIKALTPE-------IVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSL 183
Cdd:cd03298 92 ---GLGLSPGLKLTAEdrqaievALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095287788 184 KKIYEFKEDEK-TIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:cd03298 169 DLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
40-241 |
2.70e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.44 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSV---IAINA--GL-------------NGNL- 100
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI-RVGDITIdtaRSLSQqkGLirqlrqhvgfvfqNFNLf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 ---TGMEN-IEFKMLCMGFKKNEIKALTPEIVEFSELG--EFIYQpvKKYSSGMRSKLGFSISATINPEILVIDEALSVG 174
Cdd:PRK11264 98 phrTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAgkETSYP--RRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 175 DQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL--PKYE---AFLKDF 241
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFadPQQPrtrQFLEKF 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
31-220 |
2.72e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTF---YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGsLTPtHG----------------HIDKTGDVSVIA 91
Cdd:PRK13549 9 KNITKTFggvKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYP-HGtyegeiifegeelqasNIRDTERAGIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 92 INAGLN--GNLTGMENIefkmlcmgFKKNEI--------KALTPEIVE-FSELGEFI--YQPVKKYSSGmRSKLgFSISA 158
Cdd:PRK13549 87 IHQELAlvKELSVLENI--------FLGNEItpggimdyDAMYLRAQKlLAQLKLDInpATPVGNLGLG-QQQL-VEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 159 TINPE--ILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:PRK13549 157 ALNKQarLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
50-255 |
2.75e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 50 GDVIGLVGINGSGKSTLSNMIGGSLTPTHGHidktgdvsvIAINAGLNGNLTGMENIEFkmlcmgFKKNE-----IKALT 124
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGE---------IGLAKGIKLGYFAQHQLEF------LRADEsplqhLARLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 125 PEIVE---------FSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEFkedEKT 195
Cdd:PRK10636 403 PQELEqklrdylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 196 IFFVSHNLRQVKEFCTKIAWIEAGQLKDF-GSVEDvlpkYEAFLKDFKKKSTAEQKAFRQA 255
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKVEPFdGDLED----YQQWLSDVQKQENQTDEAPKEN 536
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
39-230 |
3.00e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.41 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTL---------SN-MIGGSLT---------PTHgHIDK--TGDVSVIAIN--AG 95
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTafalmgllaANgRIGGSATfngreilnlPEK-ELNKlrAEQISMIFQDpmTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 96 LNGNL-TGMENIEFKMLCMGFKKNE-----IKALtpEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:PRK09473 110 LNPYMrVGEQLMEVLMLHKGMSKAEafeesVRML--DAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 170 ALSVGDQTFTQKSLKKIYEFKEDEKT-IFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-88 |
4.44e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 4.44e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 46 QAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVS 88
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIS 403
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
40-225 |
5.52e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.41 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMI-------GGSLT----PT--------HGHIDKTGDVSVIainagLNGNL 100
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQVLldgvPLvqydhhylHRQVALVGQEPVL-----FSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TgmENIEFKmlCMGFKKNEIKALTPE------IVEF-----SELGEFIYQpvkkYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:TIGR00958 572 R--ENIAYG--LTDTPDEEIMAAAKAanahdfIMEFpngydTEVGEKGSQ----LSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 170 ALSVGDqTFTQKSLKKIYEFKedEKTIFFVSHNLRQVkEFCTKIAWIEAGQLKDFG 225
Cdd:TIGR00958 644 ATSALD-AECEQLLQESRSRA--SRTVLLIAHRLSTV-ERADQILVLKKGSVVEMG 695
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
39-230 |
5.70e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.33 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD------VSVIAINAGL---NGN-----LTGME 104
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenIREVRKFVGLvfqNPDdqifsPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 105 NIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE------ALSVGDQTF 178
Cdd:PRK13652 99 DIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEptagldPQGVKELID 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 179 TQKSLKKIYEFkedekTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK13652 179 FLNDLPETYGM-----TVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
34-258 |
6.15e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.77 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 34 NKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI---------DKTGDVSVIAINAGLNGNL---- 100
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELITNPYSKKIKNFkelr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 -----------------TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGE-FIYQPVKKYSSGMRSKLGFSISATINP 162
Cdd:PRK13631 116 rrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 163 EILVIDEALSVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSvedvlpKYEAFL-KDF 241
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT------PYEIFTdQHI 269
|
250
....*....|....*..
gi 2095287788 242 KKKSTAEQKAFRQALDE 258
Cdd:PRK13631 270 INSTSIQVPRVIQVIND 286
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-214 |
6.36e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 50 GDVIGLVGINGSGKSTLSNMIGGSLTPTHGhidktgdvSVIAINAGlngnltgmeniefkmlcmgfkkneikaLTPEIVE 129
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGG--------GVIYIDGE---------------------------DILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 130 FSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEF------KEDEKTIFFVSHNL 203
Cdd:smart00382 47 DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRlllllkSEKNLTVILTTNDE 126
|
170
....*....|.
gi 2095287788 204 RQVKEFCTKIA 214
Cdd:smart00382 127 KDLGPALLRRR 137
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
40-225 |
6.55e-06 |
|
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: 45.62 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHghidKTGDVSVIAINAGLNgnltgmeniEFKmLCMGFKKNE 119
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG----VSGEVLINGRPLDKR---------SFR-KIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 120 ---IKALTP-EIVEFS-ELgefiyqpvKKYSSGMRSKLgfSISATI--NPEILVIDEALSvGDQTFTQ----KSLKKIye 188
Cdd:cd03213 91 dilHPTLTVrETLMFAaKL--------RGLSGGERKRV--SIALELvsNPSLLFLDEPTS-GLDSSSAlqvmSLLRRL-- 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2095287788 189 fKEDEKTIFFVSHNLR-QVKEFCTKIAWIEAGQLKDFG 225
Cdd:cd03213 158 -ADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
40-106 |
6.73e-06 |
|
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: 46.85 E-value: 6.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIA----INAGLNGNLTGMENI 106
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-EIGETVKLAyvdqSRDALDPNKTVWEEI 407
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
92-233 |
7.38e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 92 INAGLNGNLTGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEAL 171
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 172 SVGDQTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPK 233
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-203 |
7.44e-06 |
|
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: 46.70 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 46 QAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSV----IainaglngnltgmeNIEFKMLCMGFKKNEIK 121
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyI--------------SPDYDGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 122 A------LTPEIVEFSELGEFIYQPVKKYSSGMRSKLgfSISATINPE--ILVIDEA---LSVGDQTFTQKSLKKIYEfk 190
Cdd:COG1245 428 DdfgssyYKTEIIKPLGLEKLLDKNVKDLSGGELQRV--AIAACLSRDadLYLLDEPsahLDVEQRLAVAKAIRRFAE-- 503
|
170
....*....|...
gi 2095287788 191 EDEKTIFFVSHNL 203
Cdd:COG1245 504 NRGKTAMVVDHDI 516
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-262 |
8.26e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.93 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHID--------KTGDVSVIAINA-------------- 94
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithKTKDKYIRPVRKrigmvfqfpesqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 95 -------------GLNGNLTGMENIEFKMLC-MGFKKNeikaltpeIVEFSelgefiyqPVKKYSSGMRSKLGFSISAtI 160
Cdd:PRK13646 100 edtvereiifgpkNFKMNLDEVKNYAHRLLMdLGFSRD--------VMSQS--------PFQMSGGQMRKIAIVSILA-M 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 161 NPEILVIDEALSVGDQTFTQKSLKKIYEFKEDE-KTIFFVSHNLRQVKEFCTKIAWIEAGQLKD-------FGSVEDV-- 230
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSqtspkelFKDKKKLad 242
|
250 260 270
....*....|....*....|....*....|....*.
gi 2095287788 231 ----LPKYEAFLKDFKKKSTAEQKAFrqALDENRFV 262
Cdd:PRK13646 243 whigLPEIVQLQYDFEQKYQTKLKDI--ALTEEEFV 276
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
40-81 |
8.57e-06 |
|
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: 45.50 E-value: 8.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV 69
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
39-94 |
8.58e-06 |
|
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: 46.51 E-value: 8.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIAINA 94
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-AVNGVPLADADA 391
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
40-240 |
9.08e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.78 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAIN------AGLNGNLTGMENIEFKMLC 112
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkPISMLSSRqlarrlALLPQHHLTPEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 113 ----------MGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKS 182
Cdd:PRK11231 98 aygrspwlslWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 183 LKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPkyEAFLKD 240
Cdd:PRK11231 178 MRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT--PGLLRT 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
39-239 |
9.33e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI----------DKTGDVSVIAINAGLNGNL-------- 100
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstSKNKDIKQIRKKVGLVFQFpesqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGE--FIYQPVKKYSSGMRSKLGFSISAtINPEILVIDEAlSVGDQTF 178
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKNPFELSGGQMRRVAIAGILA-MEPKILVLDEP-TAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 179 TQKSLKKIY-EFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLPKYEaFLK 239
Cdd:PRK13649 180 GRKELMTLFkKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVD-FLE 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-201 |
1.23e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 2 NPTVSINEVTKEYRIYRNNKER---IKDAIWPKHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSL--TP 76
Cdd:COG2401 5 NPFFVLMRVTKVYSSVLDLSERvaiVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 77 THGhidkTGDVSVIAInaglNGNLTGMENIefkmlcmgFKKNEIKALTpEIVEFSELGE--FIYQPVKKYSSGMRSKLGF 154
Cdd:COG2401 85 VAG----CVDVPDNQF----GREASLIDAI--------GRKGDFKDAV-ELLNAVGLSDavLWLRRFKELSTGQKFRFRL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095287788 155 SISATINPEILVIDEALSVGDQTFTQKSLKKIYEF-KEDEKTIFFVSH 201
Cdd:COG2401 148 ALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-81 |
1.26e-05 |
|
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: 45.94 E-value: 1.26e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2095287788 42 DVTFQAyaGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG4615 352 DLTIRR--GELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
99-235 |
1.29e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.29 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 99 NLTGMENIEF--KMLCMGFKKNEIKALTPEIVEFSELGEFIYQ----PVKKYSSGMRSKLGFSISATINPEILVIDEALS 172
Cdd:PRK14247 96 NLSIFENVALglKLNRLVKSKKELQERVRWALEKAQLWDEVKDrldaPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 173 VGDQTFTQKSLKKIYEFKEDeKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL--PKYE 235
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFtnPRHE 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
38-230 |
1.52e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTlSNMIGGSLTPTHGHIDKTG------------------DVSVIAINAGLNGN 99
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKST-TGLALLRLINSQGEIWFDGqplhnlnrrqllpvrhriQVVFQDPNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 100 LTGMENIEfkmlcMGFKKNEiKALTPEIVE------FSELG---EFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEA 170
Cdd:PRK15134 379 LNVLQIIE-----EGLRVHQ-PTLSAAQREqqviavMEEVGldpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095287788 171 LSVGDQTFTQKSLKKIYEFKEDEKTIF-FVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYlFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
40-231 |
1.70e-05 |
|
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: 45.08 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHG-HID----KTGDVSV------I-----AINAGLNGNLTGM 103
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgeRRGGEDVwelrkrIglvspALQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 EniefkMLCMGF-----------KKNEIKALtpEIVEFSELGEFIYQPVKKYSSGMRSKLGfsIS-ATI-NPEILVIDEA 170
Cdd:COG1119 99 D-----VVLSGFfdsiglyreptDEQRERAR--ELLELLGLAHLADRPFGTLSQGEQRRVL--IArALVkDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 171 LS----VGDQTFTQkSLKKIyeFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:COG1119 170 TAgldlGARELLLA-LLDKL--AAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-220 |
1.70e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD--------------VSVIAINAGLNGNLTGME 104
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngpkssqeagIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 105 NI----EF--KMLCMGFKK--NEIKALTPEI-VEFSElgefiYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGD 175
Cdd:PRK10762 99 NIflgrEFvnRFGRIDWKKmyAEADKLLARLnLRFSS-----DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095287788 176 QTFTQKSLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQ 220
Cdd:PRK10762 174 DTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
39-169 |
1.86e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSV----------IA-INAGLNGNL----TG 102
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgDMADarhrravcprIAyMPQGLGKNLyptlSV 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 103 MENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSiSATI-NPEILVIDE 169
Cdd:NF033858 96 FENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLC-CALIhDPDLLILDE 162
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-234 |
1.92e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.09 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 143 KYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKsLKKIYEFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLK 222
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-IEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
90
....*....|....
gi 2095287788 223 DFGSVEDVL--PKY 234
Cdd:PRK14271 242 EEGPTEQLFssPKH 255
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-81 |
1.96e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.96e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
40-259 |
2.16e-05 |
|
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: 45.71 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVIAINAGLNgNLTGMENIEF-KMLCMGFKKN 118
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQ-NDSLRENILFgKALNEKYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 119 EIK--ALTP--EIV---EFSELGEfiyqPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIY--EF 189
Cdd:TIGR00957 733 VLEacALLPdlEILpsgDRTEIGE----KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEG 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 190 KEDEKTIFFVSHNLRQVKEFCTKIAwIEAGQLKDFGSVEDVLPKYEAFLKDFKKKSTAEQKafrQALDEN 259
Cdd:TIGR00957 809 VLKNKTRILVTHGISYLPQVDVIIV-MSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQ---GHLEDS 874
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
53-169 |
2.16e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 53 IGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVSVIAINA----GLNGNLTGMeniEFKMLCM-GFKKNEIKAltpEI 127
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQhhvdGLDLSSNPL---LYMMRCFpGVPEQKLRA---HL 611
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2095287788 128 VEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:PLN03073 612 GSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
37-205 |
2.48e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTL------------SNMIGGSLTpTHGHIDKTGDVSVIAINAGLngnltGM- 103
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnrlndlipGFRVEGKVT-FHGKNLYAPDVDPVEVRRRI-----GMv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 104 ------------ENIEFKMLCMGFKKNeikalTPEIVEFSELGEFIYQPVK--------KYSSGMRSKLGFSISATINPE 163
Cdd:PRK14243 97 fqkpnpfpksiyDNIAYGARINGYKGD-----MDELVERSLRQAALWDEVKdklkqsglSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095287788 164 ILVIDEALSVGDQTFTQKSLKKIYEFKEDeKTIFFVSHNLRQ 205
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQ 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-230 |
2.49e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 44.63 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVsviAINAGL-NGNL----------------- 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-TIGER---VITAGKkNKKLkplrkkvgivfqfpehq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 101 ----TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSG--MRSklgFSISATI--NPEILVIDEALS 172
Cdd:PRK13634 98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGgqMRR---VAIAGVLamEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 173 VGDQTFTQKSLKKIYEF-KEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
31-208 |
3.40e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.97 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-------------DKTGDVSVIAINA--G 95
Cdd:PRK13648 16 QYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKHIGIVFQNPdnQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 96 LNGNLT------GMENiefkmlcMGFKKNEIKALTPEIVEFSELGEFI-YQPvKKYSSGMRSKLGFSISATINPEILVID 168
Cdd:PRK13648 96 FVGSIVkydvafGLEN-------HAVPYDEMHRRVSEALKQVDMLERAdYEP-NALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2095287788 169 EALSVGDQTFTQKSLKKIYEFKED-EKTIFFVSHNLRQVKE 208
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME 208
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
40-81 |
3.77e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 43.68 E-value: 3.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGsLTPTHGHI 81
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEI 52
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
43-81 |
3.88e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.77 E-value: 3.88e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2095287788 43 VTFQAYAGDVIGLVGINGSGKSTLSNMIGGsLTPTHGHI 81
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSI 52
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-239 |
3.91e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.23 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 20 NKERIKDAIWPKHKNKT---FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGH-----------IDKTG 85
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 86 DVSVIAINAGLNGNL--------TGMENIEFKMLCMGFKKNEIKALTPEIVEFSELG-EFIYQPVKKYSSGMRSKLGFSI 156
Cdd:PRK13645 84 EVKRLRKEIGLVFQFpeyqlfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 157 SATINPEILVIDEALS----VGDQTFTQKSLKKiyeFKEDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVLP 232
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGgldpKGEEDFINLFERL---NKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
....*..
gi 2095287788 233 KYEAFLK 239
Cdd:PRK13645 241 NQELLTK 247
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-203 |
4.02e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.80 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 44 TFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD-----------VSVIAINAGLNGNLTGMENIEFKmLC 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHLTVAQNIGLG-LN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 113 MGFKKN-EIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEF-K 190
Cdd:PRK10771 98 PGLKLNaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVcQ 177
|
170
....*....|...
gi 2095287788 191 EDEKTIFFVSHNL 203
Cdd:PRK10771 178 ERQLTLLMVSHSL 190
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-81 |
4.07e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.01 E-value: 4.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 31 KHKNKTFYALKDVTFQAY-------------AGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI 68
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-86 |
4.11e-05 |
|
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: 43.94 E-value: 4.11e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2095287788 48 YAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD 86
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD 61
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-88 |
5.60e-05 |
|
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: 44.13 E-value: 5.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVS 88
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS 490
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
37-81 |
6.36e-05 |
|
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: 43.90 E-value: 6.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2095287788 37 FYALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGsLTPTHGHI 81
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEI 342
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
40-81 |
6.81e-05 |
|
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: 42.51 E-value: 6.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGG--SLTPTHGHI 81
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI 59
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
34-202 |
7.11e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 43.55 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 34 NKTFYALKDVT-------------FQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVSVIAINA----- 94
Cdd:PRK11432 3 QKNFVVLKNITkrfgsntvidnlnLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGeDVTHRSIQQrdicm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 95 -----GLNGNLTGMENIEF--KMLcmGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVI 167
Cdd:PRK11432 83 vfqsyALFPHMSLGENVGYglKML--GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2095287788 168 DEALSVGDQTFTQKSLKKIYEFKED-EKTIFFVSHN 202
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHD 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
41-172 |
7.30e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.48 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 41 KDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI----DKTGDVSVIAINAG-------LNGNLTGMENIEFK 109
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigeKRMNDVPPAERGVGmvfqsyaLYPHLSVAENMSFG 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095287788 110 MLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLgfSISATI--NPEILVIDEALS 172
Cdd:PRK11000 100 LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRV--AIGRTLvaEPSVFLLDEPLS 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
40-81 |
7.41e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 42.75 E-value: 7.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGG--SLTPTHGHI 81
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSI 59
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
50-231 |
1.01e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 42.67 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 50 GDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD-------------VSVIAINAGLNGNLTGMENIE-----FKML 111
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNATTPGDITVQELVArgrypHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 112 CMGFKKNEIKALTpEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYEF-K 190
Cdd:PRK10253 113 FTRWRKEDEEAVT-KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnR 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2095287788 191 EDEKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL 231
Cdd:PRK10253 192 EKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-70 |
1.05e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 1.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095287788 22 ERIKDAIwpKHKNKTFY-------ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMI 70
Cdd:PRK11176 336 ERAKGDI--EFRNVTFTypgkevpALRNINFKIPAGKTVALVGRSGSGKSTIANLL 389
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
31-87 |
1.12e-04 |
|
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: 42.26 E-value: 1.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 31 KHKNKTFYA--LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLtptHGHIDKTGDV 87
Cdd:cd03234 12 KAKNWNKYAriLNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGQI 67
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
99-235 |
1.59e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 99 NLTGMENIefkmlCMGFKKNEI---KALTPEIVEFSELGEFIYQPVK--------KYSSGMRSKLGFSISATINPEILVI 167
Cdd:PRK14267 99 HLTIYDNV-----AIGVKLNGLvksKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQRQRLVIARALAMKPKILLM 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 168 DEALSVGDQTFTQKSLKKIYEFKEDeKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDVL--PKYE 235
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFenPEHE 242
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
34-221 |
1.63e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 41.92 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 34 NKTFY---ALKDVTFQAYAGDVIGLVGINGSGKST----LSNMIGGSLTPtHGHIDKTG-----------DVSVIAINAG 95
Cdd:PRK09984 11 AKTFNqhqALHAVDLNIHHGEMVALLGPSGSGKSTllrhLSGLITGDKSA-GSHIELLGrtvqregrlarDIRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 96 -------LNGNLTGMENIEFKML-CMGFKKNEIKALTPE-----IVEFSELG--EFIYQPVKKYSSGMRSKLGFSISATI 160
Cdd:PRK09984 90 yifqqfnLVNRLSVLENVLIGALgSTPFWRTCFSWFTREqkqraLQALTRVGmvHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095287788 161 NPEILVIDEALSVGDQTFTQKSLKKIYEFKE-DEKTIFFVSHNLRQVKEFCTKIAWIEAGQL 221
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
39-81 |
1.68e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.32 E-value: 1.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
40-81 |
2.37e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.01 E-value: 2.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-66 |
2.70e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 2.70e-04
10 20
....*....|....*....|....*..
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTL 66
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTL 49
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
39-175 |
3.05e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 41.47 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI-----DKTG------DVSVIAINAGLNGNLTGMENIE 107
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqDITHvpaenrHVNTVFQSYALFPHMTVFENVA 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095287788 108 FKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSiSATIN-PEILVIDEALSVGD 175
Cdd:PRK09452 109 FGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA-RAVVNkPKVLLLDESLSALD 176
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
40-201 |
3.56e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSL--------------TPTHGHIDKTGDVSVIAInagLNGNLTGMEN 105
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgnnftgtilannrKPTKQILKRTGFVTQDDI---LYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 106 IEFKMLCMGFKK--NEIKALTPEIVeFSELG-----------EFIyqpvKKYSSGMRSKLGFSISATINPEILVIDEALS 172
Cdd:PLN03211 161 LVFCSLLRLPKSltKQEKILVAESV-ISELGltkcentiignSFI----RGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180
....*....|....*....|....*....
gi 2095287788 173 VGDQTFTQKSLKKIYEFKEDEKTIFFVSH 201
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
40-88 |
3.71e-04 |
|
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: 41.00 E-value: 3.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGDVS 88
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS 101
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
41-106 |
5.18e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 5.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 41 KDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIdKTGDVSVIA----INAGLNGNLTGMENI 106
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-KIGETVKLAyvdqSRDALDPNKTVWEEI 409
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
40-107 |
6.38e-04 |
|
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: 40.69 E-value: 6.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGsltpthghIDK--TGDVSVIA-INAG-------LNGNLTGMENIE 107
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDKdfNGEARPQPgIKVGylpqepqLDPTKTVRENVE 90
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
57-169 |
7.35e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 57 GINGSGKSTLSNMIGGSLTPTHGHI----DKTGDV-----SVIAINAGLNGNLTGMENIEFkmlcmgfkKNEI---KALT 124
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIyyknCNINNIakpycTYIGHNLGLKLEMTVFENLKF--------WSEIynsAETL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2095287788 125 PEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDE 169
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
54-81 |
7.90e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 7.90e-04
10 20
....*....|....*....|....*...
gi 2095287788 54 GLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
50-82 |
8.01e-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: 39.48 E-value: 8.01e-04
10 20 30
....*....|....*....|....*....|...
gi 2095287788 50 GDVIGLVGINGSGKSTLSNMIGGSLTPTHGHID 82
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE 57
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
39-81 |
8.01e-04 |
|
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: 40.42 E-value: 8.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
43-108 |
1.14e-03 |
|
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: 39.01 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095287788 43 VTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI--DKTGDVSV----------IAINAGLNGNLTGMENIEF 108
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllNGGPLDFQrdsiargllyLGHAPGIKTTLSVLENLRF 96
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
40-239 |
1.16e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSN-------------MIGGSLTPTHGHIDKTGDVSVIA-----INAGLNGNLT 101
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNalfrivelekgriMIDDCDVAKFGLTDLRRVLSIIPqspvlFSGTVRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 102 GMENIEFKMLCMGFKKNEIKaltpEIVEFSELG--EFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGD---Q 176
Cdd:PLN03232 1332 PFSEHNDADLWEALERAHIK----DVIDRNPFGldAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDvrtD 1407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 177 TFTQKSLKKiyEFKEdeKTIFFVSHNLRQVKEfCTKIAWIEAGQLKDFGSVEDVLPK-YEAFLK 239
Cdd:PLN03232 1408 SLIQRTIRE--EFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRdTSAFFR 1466
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
39-81 |
1.16e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 39.59 E-value: 1.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 62
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
35-72 |
1.19e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 1.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2095287788 35 KTFY---ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGG 72
Cdd:NF040905 9 KTFPgvkALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-230 |
1.53e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.45 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 31 KHKNKTFYALKDVTFQAYAGDVIGLVGINGSGKS----TLSNMI--GGSLTPTHGHIDKTGDVSVIAIN----------- 93
Cdd:PRK10261 23 MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSRQVIELSeqsaaqmrhvr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 94 ------------AGLNGNLTGMENI-EFKMLCMGFKKNEIKALTP---EIVEFSELGEFIYQPVKKYSSGMRSKLGFSIS 157
Cdd:PRK10261 103 gadmamifqepmTSLNPVFTVGEQIaESIRLHQGASREEAMVEAKrmlDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095287788 158 ATINPEILVIDEALSVGDQTFTQKSLKKIYEFKED-EKTIFFVSHNLRQVKEFCTKIAWIEAGQLKDFGSVEDV 230
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
39-203 |
1.86e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 38.70 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTG-DVS---------------VIAINAGLNGNLTG 102
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhDITrlknrevpflrrqigMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 103 MENIEFKMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKS 182
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180
....*....|....*....|.
gi 2095287788 183 LKKIYEFKEDEKTIFFVSHNL 203
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATHDI 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-81 |
2.13e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 2.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
39-81 |
2.94e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 38.46 E-value: 2.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEI 309
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
50-86 |
3.08e-03 |
|
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: 38.12 E-value: 3.08e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2095287788 50 GDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD 86
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPD 62
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
40-207 |
3.49e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 37.77 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD-------------VSVIAINAGLNGNlTGMENI 106
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGD-TVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 107 EFKMLCMGfKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKI 186
Cdd:PRK10247 102 IFPWQIRN-QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEII 180
|
170 180
....*....|....*....|..
gi 2095287788 187 YEFKEDEK-TIFFVSHNLRQVK 207
Cdd:PRK10247 181 HRYVREQNiAVLWVTHDKDEIN 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
50-86 |
4.15e-03 |
|
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: 38.23 E-value: 4.15e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2095287788 50 GDVIGLVGINGSGKSTLSNMIGGSLTPTHGHIDKTGD 86
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPS 135
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
40-67 |
5.92e-03 |
|
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: 37.88 E-value: 5.92e-03
10 20
....*....|....*....|....*...
gi 2095287788 40 LKDVTFQAYAGDVIGLVGINGSGKSTLS 67
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLA 401
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
38-81 |
6.49e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 37.64 E-value: 6.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2095287788 38 YALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK10522 337 FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
50-223 |
6.73e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 37.07 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 50 GDVIGLVGINGSGKSTL--------------SNMIGGSLTpthgHIDKTGDVSVIAINAG-------LNGNLTGMENIEF 108
Cdd:PRK10584 36 GETIALIGESGSGKSTLlailaglddgssgeVSLVGQPLH----QMDEEARAKLRAKHVGfvfqsfmLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095287788 109 KMLCMGFKKNEIKALTPEIVEFSELGEFIYQPVKKYSSGMRSKLGFSISATINPEILVIDEALSVGDQTFTQKSLKKIYE 188
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 2095287788 189 FKED-EKTIFFVSHNLrQVKEFCTKIAWIEAGQLKD 223
Cdd:PRK10584 192 LNREhGTTLILVTHDL-QLAARCDRRLRLVNGQLQE 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-70 |
6.81e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 37.77 E-value: 6.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2095287788 24 IKDAIWPKHKNKtfyALKDVTFQAYAGDVIGLVGINGSGKSTLSNMI 70
Cdd:PRK10789 318 IRQFTYPQTDHP---ALENVNFTLKPGQMLGICGPTGSGKSTLLSLI 361
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-81 |
8.17e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 37.50 E-value: 8.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095287788 39 ALKDVTFQAYAGDVIGLVGINGSGKSTLSNMIGGSLTPTHGHI 81
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
|
| |
