|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
52-350 |
3.68e-65 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 209.80 E-value: 3.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 52 VKEGSLAAQTAFTGTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAELARN 131
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 132 LMNRKQRLLNQGFIARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 212 VNPDQLEIQAKLPIEQQSALKVGSSIQYQIQGNS-KQLHAILTRISPVADQDSRQIEFFASPKEAIDSLSIGAFINGIIL 290
Cdd:COG0845 163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPgKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRIV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1428926761 291 HNDSNQGQTIPLDSIQNLQHDPFVWVIR-NQTIQKVKIRVVeQRYNENIALVQGLQSTDQV 350
Cdd:COG0845 243 LGERENALLVPASAVVRDGGGAYVFVVDaDGKVERRPVTLG-RRDGDQVEVLSGLKAGDRV 302
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
49-350 |
1.09e-48 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 167.11 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 49 LIPVKEGSLAAQTAFTGTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAEL 128
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 129 ARNLMNRKQRLLNQGFIARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQTL 208
Cdd:TIGR01730 83 AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 209 FEIVNPDQLEIQAKLPIEQQSALKVGSSIQYQIQGNSKQLH-AILTRISPVADQDSRQIEFFASPKEAIDSLSIGAFING 287
Cdd:TIGR01730 163 ATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFkGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFGRV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1428926761 288 IILHNDSNQGQTIPLDSIQNLQHDPFVWVIRNQTiqKVKIRVVE--QRYNENIALVQGLQSTDQV 350
Cdd:TIGR01730 243 TISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDG--KVSKRPVEvgLRNGGYVEIESGLKAGDQI 305
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
66-264 |
4.85e-17 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 79.09 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 66 TIRAV--------QQSSIQAQVSATATAVTAD-VGQKVQKGQVLVRLNNQDnaarLAQAQAN--LASAQAQAELARNLMN 134
Cdd:pfam16576 5 TIRAVgrvayderRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPE----LVAAQQEylLALRSGDALSKSELLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 135 R-KQRLLNQGFiarvefEQSQVDykgQLESVRAQQANVDIakkadrdgiiTSPISGVITKRQVEPGQTVSVGQTLFEIVN 213
Cdd:pfam16576 81 AaRQRLRLLGM------PEAQIA---ELERTGKVQPTVTV----------YAPISGVVTELNVREGMYVQPGDTLFTIAD 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1428926761 214 PDQLEIQAKLPIEQQSALKVGSSIQYQIQG-NSKQLHAILTRISPVADQDSR 264
Cdd:pfam16576 142 LSTVWVEADVPEQDLALVKVGQPAEVTLPAlPGKTFEGKVDYIYPTLDPKTR 193
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
65-350 |
3.08e-11 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 64.43 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 65 GTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAELARNLMNRKQRLLNQGF 144
Cdd:PRK11556 80 GTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 145 IARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQT--LFEIVNPDQLEIQAK 222
Cdd:PRK11556 160 VSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLVFT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 223 LPiEQQ-----SALKVGSSIQYQI--QGNSKQL-HAILTRISPVADQDSRQIEFFASPKEAIDSLSIGAFINGIILHNDS 294
Cdd:PRK11556 240 LP-ESDiatvvQAQKAGKPLVVEAwdRTNSKKLsEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTL 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1428926761 295 NQGQTIPLDSIQNLQHDPFVWVIRNQTIQKVKIRVVEQRYNENIALVQGLQSTDQV 350
Cdd:PRK11556 319 QNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRV 374
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
183-211 |
1.51e-04 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 39.70 E-value: 1.51e-04
10 20
....*....|....*....|....*....
gi 1428926761 183 ITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:cd06849 46 VEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
52-350 |
3.68e-65 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 209.80 E-value: 3.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 52 VKEGSLAAQTAFTGTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAELARN 131
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 132 LMNRKQRLLNQGFIARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 212 VNPDQLEIQAKLPIEQQSALKVGSSIQYQIQGNS-KQLHAILTRISPVADQDSRQIEFFASPKEAIDSLSIGAFINGIIL 290
Cdd:COG0845 163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPgKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRIV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1428926761 291 HNDSNQGQTIPLDSIQNLQHDPFVWVIR-NQTIQKVKIRVVeQRYNENIALVQGLQSTDQV 350
Cdd:COG0845 243 LGERENALLVPASAVVRDGGGAYVFVVDaDGKVERRPVTLG-RRDGDQVEVLSGLKAGDRV 302
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
49-350 |
1.09e-48 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 167.11 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 49 LIPVKEGSLAAQTAFTGTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAEL 128
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 129 ARNLMNRKQRLLNQGFIARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQTL 208
Cdd:TIGR01730 83 AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 209 FEIVNPDQLEIQAKLPIEQQSALKVGSSIQYQIQGNSKQLH-AILTRISPVADQDSRQIEFFASPKEAIDSLSIGAFING 287
Cdd:TIGR01730 163 ATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFkGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFGRV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1428926761 288 IILHNDSNQGQTIPLDSIQNLQHDPFVWVIRNQTiqKVKIRVVE--QRYNENIALVQGLQSTDQV 350
Cdd:TIGR01730 243 TISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDG--KVSKRPVEvgLRNGGYVEIESGLKAGDQI 305
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
64-263 |
3.71e-31 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 120.54 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 64 TGTIRAVQQSsIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLA----------------------- 120
Cdd:COG1566 38 DGRVEARVVT-VAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelgaeaeiaaae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 121 ----SAQAQAELARNLMNRKQRLLNQGFIARVEFEQSQVDY---KGQLESVRAQ------------------------QA 169
Cdd:COG1566 117 aqlaAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALdaaQAQLEAAQAQlaqaqaglreeeelaaaqaqvaqaEA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 170 NVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQTLFEIVNPDQLEIQAKLPIEQQSALKVGSSIQYQIQG-NSKQL 248
Cdd:COG1566 197 ALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAyPDRVF 276
|
250
....*....|....*
gi 1428926761 249 HAILTRISPVADQDS 263
Cdd:COG1566 277 EGKVTSISPGAGFTS 291
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
66-264 |
4.85e-17 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 79.09 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 66 TIRAV--------QQSSIQAQVSATATAVTAD-VGQKVQKGQVLVRLNNQDnaarLAQAQAN--LASAQAQAELARNLMN 134
Cdd:pfam16576 5 TIRAVgrvayderRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPE----LVAAQQEylLALRSGDALSKSELLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 135 R-KQRLLNQGFiarvefEQSQVDykgQLESVRAQQANVDIakkadrdgiiTSPISGVITKRQVEPGQTVSVGQTLFEIVN 213
Cdd:pfam16576 81 AaRQRLRLLGM------PEAQIA---ELERTGKVQPTVTV----------YAPISGVVTELNVREGMYVQPGDTLFTIAD 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1428926761 214 PDQLEIQAKLPIEQQSALKVGSSIQYQIQG-NSKQLHAILTRISPVADQDSR 264
Cdd:pfam16576 142 LSTVWVEADVPEQDLALVKVGQPAEVTLPAlPGKTFEGKVDYIYPTLDPKTR 193
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
54-242 |
5.70e-17 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 80.93 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 54 EGSLAAQTAFTGTIRAV-QQSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAELARNL 132
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSgNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 133 MNRKQRLLNQGFIARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQT--LFE 210
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQAnlLAT 160
|
170 180 190
....*....|....*....|....*....|..
gi 1428926761 211 IVNPDQLEIQAKLPIEQQSALKVGSSIQYQIQ 242
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVRSELSGAQLQ 192
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
183-281 |
3.35e-16 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 73.55 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 183 ITSPISGVITKRQVEPGQTVSVGQTLFEIVNPDQLEIQAKLPIEQQSALKVGSSIQYQIQGNSKQ-LHAILTRISPVADQ 261
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYtLEGKVVRISPTVDP 81
|
90 100
....*....|....*....|
gi 1428926761 262 DSRQIEFFASPKEAIDSLSI 281
Cdd:pfam13437 82 DTGVIPVRVSIENPKTPIPL 101
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
65-350 |
3.08e-11 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 64.43 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 65 GTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAELARNLMNRKQRLLNQGF 144
Cdd:PRK11556 80 GTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 145 IARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQT--LFEIVNPDQLEIQAK 222
Cdd:PRK11556 160 VSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLVFT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 223 LPiEQQ-----SALKVGSSIQYQI--QGNSKQL-HAILTRISPVADQDSRQIEFFASPKEAIDSLSIGAFINGIILHNDS 294
Cdd:PRK11556 240 LP-ESDiatvvQAQKAGKPLVVEAwdRTNSKKLsEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTL 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1428926761 295 NQGQTIPLDSIQNLQHDPFVWVIRNQTIQKVKIRVVEQRYNENIALVQGLQSTDQV 350
Cdd:PRK11556 319 QNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRV 374
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
67-209 |
4.28e-11 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 63.44 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 67 IRAVQQSsiqAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQ--------------------- 125
Cdd:PRK03598 41 IRTVNLG---FRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQldlmlagyrdeeiaqaraavk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 126 -----AELARNLMNRKQRLLNQGFIARVEFE-------QSQVDYKG------QLE-------------SVRAQQANVDIA 174
Cdd:PRK03598 118 qaqaaYDYAQNFYNRQQGLWKSRTISANDLEnarssrdQAQATLKSaqdklsQYRegnrpqdiaqakaSLAQAQAALAQA 197
|
170 180 190
....*....|....*....|....*....|....*
gi 1428926761 175 KKADRDGIITSPISGVITKRQVEPGQTVSVGQTLF 209
Cdd:PRK03598 198 ELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVF 232
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
49-206 |
4.35e-11 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 63.96 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 49 LIPVKEGSLAAQTAFTGTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAEL 128
Cdd:PRK15030 42 VVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANI 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1428926761 129 ARNLMNRKQRLLNQGFIARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQ 206
Cdd:PRK15030 122 AQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQ 199
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
50-206 |
2.43e-10 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 61.33 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 50 IPVKEGSLAAQTAFTGTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLN-----NQ--DNAARLAQAQANLASA 122
Cdd:PRK11578 39 LIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDpeqaeNQikEVEATLMELRAQRQQA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 123 QAQAELARNLMNRKQRLLNQGFIARVEFEQSQVDY---KGQLESVRAQ----QANVDIAKKADRDGIITSPISGVITKRQ 195
Cdd:PRK11578 119 EAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELavkQAQIGTIDAQikrnQASLDTAKTNLDYTRIVAPMAGEVTQIT 198
|
170
....*....|.
gi 1428926761 196 VEPGQTVSVGQ 206
Cdd:PRK11578 199 TLQGQTVIAAQ 209
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
25-207 |
2.85e-10 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 61.27 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 25 ACNQQEVPKTTASEPKkielipQDLIPVKEGSLAAQTAFTGTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRLN 104
Cdd:PRK09859 20 ACDDKSAENAAAMTPE------VGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 105 NQDNAARLAQAQANLASAQAQAELARNLMNRKQRLLNQGFIARVEFEQSQVDYKGQLESVRAQQANVDIAKKADRDGIIT 184
Cdd:PRK09859 94 PAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVT 173
|
170 180
....*....|....*....|...
gi 1428926761 185 SPISGVITKRQVEPGQTVSVGQT 207
Cdd:PRK09859 174 SPITGVSGKSSVTVGALVTANQA 196
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
74-256 |
2.89e-10 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 60.52 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 74 SIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQAELARNLMNRKQRLLNQGfIARVEFEQS 153
Cdd:PRK10559 49 AIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQA-MSREEIDQA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 154 QVDYKGQLESVRAQQANVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQTLFEIVNPDQLEIQAKLPIEQQSALKV 233
Cdd:PRK10559 128 NNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRP 207
|
170 180
....*....|....*....|...
gi 1428926761 234 GSSIQYQIQGNSKQLHAILTRIS 256
Cdd:PRK10559 208 GYRAEITPLGSNKVLKGTVDSVA 230
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
73-215 |
2.89e-10 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 60.81 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 73 SSIQAQVSATATAVTADVG-----------QKVQKGQVLVRLNNQDNAARLAQAQANLASAQAQ---------------- 125
Cdd:PRK10476 38 STDDAYIDADVVHVASEVGgrivelavtenQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQimttqrsvdaersnaa 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 126 ------------AELARNLMNRKQRLLNQGFI--------------ARVEFEQSQV----------DYKGQLESVRAQQA 169
Cdd:PRK10476 118 saneqveraranAKLATRTLERLEPLLAKGYVsaqqvdqartaqrdAEVSLNQALLqaqaaaaavgGVDALVAQRAAREA 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1428926761 170 NVDIAKKADRDGIITSPISGVITKRQVEPGQTVSVGQTLFEIVNPD 215
Cdd:PRK10476 198 ALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTD 243
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
24-206 |
3.25e-09 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 57.88 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 24 AACNQQEvPKTTASEPKKIelipqDLIPVKEGSLAAQTAFTGTIRAVQQSSIQAQVSATATAVTADVGQKVQKGQVLVRL 103
Cdd:PRK09578 21 AGCGKGD-SDAAAAAPREA-----TVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 104 NNQDNAARLAQAQANLASAQAQAELARNLMNRKQRLLNQGFIARVEFEQSQVD---YKGQLESVRAQ--QANVDIAKKAd 178
Cdd:PRK09578 95 DPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADerqAKAAVASAKAElaRAQLQLDYAT- 173
|
170 180
....*....|....*....|....*...
gi 1428926761 179 rdgiITSPISGVITKRQVEPGQTVSVGQ 206
Cdd:PRK09578 174 ----VTAPIDGRARRALVTEGALVGQDQ 197
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
72-234 |
2.34e-08 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 55.47 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 72 QSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLASA--------------QAQAEL-------AR 130
Cdd:PRK15136 61 QVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSvrqthqlminskqyQANIELqktalaqAQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1428926761 131 NLMNRKQRLLNQGFIARVEFEQSQvdykgqlESVRAQQANVDIAK---KADRDGI------------------------- 182
Cdd:PRK15136 141 SDLNRRVPLGNANLIGREELQHAR-------DAVASAQAQLDVAIqqyNANQAMIlntpledqpavqqaatevrnawlal 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1428926761 183 ----ITSPISGVITKRQVEPGQTVSVGQTLFEIVNPDQLEIQAKLPIEQQSALKVG 234
Cdd:PRK15136 214 qrtkIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIG 269
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
72-120 |
1.55e-05 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 41.66 E-value: 1.55e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1428926761 72 QSSIQAQVSATATAVTADVGQKVQKGQVLVRLNNQDNAARLAQAQANLA 120
Cdd:pfam13533 2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
159-211 |
3.78e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 45.90 E-value: 3.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1428926761 159 GQLESV----RAQQANVDIAKKADRD--GIITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:PRK12999 1049 GQPREVqvrdRSVKSTVAAREKADPGnpGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVI 1107
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
176-212 |
4.58e-05 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 41.21 E-value: 4.58e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1428926761 176 KADRDgiITSPISGVITKRQVEPGQTVSVGQTLFEIV 212
Cdd:COG0508 43 KATME--VPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
159-211 |
5.48e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 45.46 E-value: 5.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1428926761 159 GQLESV----RAQQANVDIAKKADRD--GIITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:COG1038 1049 GQPREVrvrdRSVKVTVASREKADPGnpGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTI 1107
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
183-211 |
1.28e-04 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 41.42 E-value: 1.28e-04
10 20
....*....|....*....|....*....
gi 1428926761 183 ITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:COG0511 107 IEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
183-211 |
1.51e-04 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 39.70 E-value: 1.51e-04
10 20
....*....|....*....|....*....
gi 1428926761 183 ITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:cd06849 46 VEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
183-211 |
1.68e-04 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 39.32 E-value: 1.68e-04
10 20
....*....|....*....|....*....
gi 1428926761 183 ITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:cd06850 39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
183-211 |
2.59e-04 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 38.94 E-value: 2.59e-04
10 20
....*....|....*....|....*....
gi 1428926761 183 ITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVL 30
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
183-211 |
1.00e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 40.98 E-value: 1.00e-03
10 20
....*....|....*....|....*....
gi 1428926761 183 ITSPISGVITKRQVEPGQTVSVGQTLFEI 211
Cdd:PRK09282 562 IQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
159-208 |
1.03e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 40.98 E-value: 1.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1428926761 159 GQLESVRAQQANVDIA---KKADRDGIITSPISGVITKRQVEPGQTVSVGQTL 208
Cdd:PRK09282 498 GMPEEVVVEPLKEIVVggrPRASAPGAVTSPMPGTVVKVKVKEGDKVKAGDTV 550
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
164-211 |
9.33e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 36.03 E-value: 9.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1428926761 164 VRAQQANVDIAKKADRDGIITSPISGVITKRQ-------VEPGQTVSVGQTLFEI 211
Cdd:COG0511 44 AAAAPAAAAAAAAASGGGAVKSPMVGTFYRAPspgakpfVKVGDKVKAGDTLCII 98
|
|
| |
