|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-273 |
3.62e-75 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 232.08 E-value: 3.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 3 KIFFLGECMVELKA------ISDSTLNQSFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLATQLVF 76
Cdd:cd01166 1 DVVTIGEVMVDLSPpgggrlEQADSFRKFFGGAEANVAVGLARL--GHRVALVTAVGDDPFGRFILAELRREGVDTSHVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 77 THANKVPGIYYIETDEQGERSFTYWRHDSAARKVV--DFFnpsvEEELASADMLFISGISLAvIEPASRDLFWQIVQRIK 154
Cdd:cd01166 79 VDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTpeDLD----EAALAGADHLHLSGITLA-LSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 155 KAGVKIVFDPNYRARLWqSEQETKGQYTIAFELADICLPGIEDLTTLYELHSAQAVMDYLAQFNIS--EVVVKNGPSSVF 232
Cdd:cd01166 154 ARGVTVSFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALGvkAVVVKLGAEGAL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1823256134 233 TKINGQLFEHQITPVtHVVDTTSAGDAFNGAYLGARMAGMD 273
Cdd:cd01166 233 VYTGGGRVFVPAYPV-EVVDTTGAGDAFAAGFLAGLLEGWD 272
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-273 |
1.96e-56 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 184.32 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 3 KIFFLGECMVELKAISDS-----------TLNQSFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLA 71
Cdd:COG0524 1 DVLVIGEALVDLVARVDRlpkggetvlagSFRRSPGGAAANVAVALARL--GARVALVGAVGDDPFGDFLLAELRAEGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 72 TQLVFTHANKVPGIYYIETDEQGERSFTYWRhdSAARkvvdFFNPSV--EEELASADMLFISGISLAviEPASRDLFWQI 149
Cdd:COG0524 79 TSGVRRDPGAPTGLAFILVDPDGERTIVFYR--GANA----ELTPEDldEALLAGADILHLGGITLA--SEPPREALLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 150 VQRIKKAGVKIVFDPNYRARLWQSEQETkgqYTIAFELADICLPGIEDLTTLYELHSAQAVMDYLAQFNISEVVVKNGPS 229
Cdd:COG0524 151 LEAARAAGVPVSLDPNYRPALWEPAREL---LRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1823256134 230 SVFTKINGQLFEHQITPVThVVDTTSAGDAFNGAYLGARMAGMD 273
Cdd:COG0524 228 GALLYTGGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLD 270
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-273 |
2.66e-34 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 126.69 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 3 KIFFLGECMVELKAISD---------STLNQSFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLATQ 73
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEglpgelvrvSTVEKGPGGKGANVAVALARL--GGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 74 LVFTHANKVPGIYYIETDEQGERSFTYWRHDSAARKVVDFFNPsvEEELASADMLFISGISLAVIEPASrdlfWQIVQRI 153
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEEN--EDLLENADLLYISGSLPLGLPEAT----LEELIEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 154 KKAGVKivFDPNYRARLWQseqeTKGQYTIAFELADICLPGIEDLTTLY--ELHSAQAVMDYLAQFN---ISEVVVKNGP 228
Cdd:pfam00294 153 AKNGGT--FDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALTgaKLDDIEEALAALHKLLakgIKTVIVTLGA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1823256134 229 SSVFTKINGQLFEHQITPVTHVVDTTSAGDAFNGAYLGARMAGMD 273
Cdd:pfam00294 227 DGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKS 271
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-265 |
1.17e-27 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 108.87 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 1 MKKIFFLGECMVELKAISDSTLNQSFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLATQLVFTHAN 80
Cdd:PRK09434 2 MNKVWVLGDAVVDLIPEGENRYLKCPGGAPANVAVGIARL--GGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 81 KVPGIYYIETDEQGERSFTYWRHDSAarkvvD-FFNPSVEEELASADMLFISGISLAViEPaSRDLFWQIVQRIKKAGVK 159
Cdd:PRK09434 80 HRTSTVVVDLDDQGERSFTFMVRPSA-----DlFLQPQDLPPFRQGEWLHLCSIALSA-EP-SRSTTFEAMRRIKAAGGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 160 IVFDPNYRARLWQSEQETKGQYTIAFELADICLPGIEDLTTLYELHSAQAVMDYLAQ-FNISEVVVKNGPSSVFTKINGQ 238
Cdd:PRK09434 153 VSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADrYPIALLLVTLGAEGVLVHTRGQ 232
|
250 260
....*....|....*....|....*..
gi 1823256134 239 LFEHQITPVThVVDTTSAGDAFNGAYL 265
Cdd:PRK09434 233 VQHFPAPSVD-PVDTTGAGDAFVAGLL 258
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
32-275 |
2.69e-13 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 68.78 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 32 NSAVYLKRcfSSLECGVVSAIGTDALSIKMRQRFVEEGLATQLVFTHANKVPGIYYIETDEQGERSFtywrhdsaarkVV 111
Cdd:TIGR02152 36 NQAVAAAR--LGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRI-----------VV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 112 -----DFFNPSV----EEELASADMLFISG-ISLAVIEPAsrdlfwqiVQRIKKAGVKIVFDPNyRARLWQSEQetkgqy 181
Cdd:TIGR02152 103 vaganAELTPEDidaaEALIAESDIVLLQLeIPLETVLEA--------AKIAKKHGVKVILNPA-PAIKDLDDE------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 182 tiAFELADICLPG---IEDLT--TLYELHSAQAVMDYLAQFNISEVVVKNGPSSVFTKINGqlfEHQITPVTHV--VDTT 254
Cdd:TIGR02152 168 --LLSLVDIITPNeteAEILTgiEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKD---ESKLIPAFKVkaVDTT 242
|
250 260
....*....|....*....|.
gi 1823256134 255 SAGDAFNGAYLGARMAGMDEH 275
Cdd:TIGR02152 243 AAGDTFNGAFAVALAEGKSLE 263
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-273 |
3.62e-75 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 232.08 E-value: 3.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 3 KIFFLGECMVELKA------ISDSTLNQSFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLATQLVF 76
Cdd:cd01166 1 DVVTIGEVMVDLSPpgggrlEQADSFRKFFGGAEANVAVGLARL--GHRVALVTAVGDDPFGRFILAELRREGVDTSHVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 77 THANKVPGIYYIETDEQGERSFTYWRHDSAARKVV--DFFnpsvEEELASADMLFISGISLAvIEPASRDLFWQIVQRIK 154
Cdd:cd01166 79 VDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTpeDLD----EAALAGADHLHLSGITLA-LSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 155 KAGVKIVFDPNYRARLWqSEQETKGQYTIAFELADICLPGIEDLTTLYELHSAQAVMDYLAQFNIS--EVVVKNGPSSVF 232
Cdd:cd01166 154 ARGVTVSFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALGvkAVVVKLGAEGAL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1823256134 233 TKINGQLFEHQITPVtHVVDTTSAGDAFNGAYLGARMAGMD 273
Cdd:cd01166 233 VYTGGGRVFVPAYPV-EVVDTTGAGDAFAAGFLAGLLEGWD 272
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-273 |
1.96e-56 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 184.32 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 3 KIFFLGECMVELKAISDS-----------TLNQSFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLA 71
Cdd:COG0524 1 DVLVIGEALVDLVARVDRlpkggetvlagSFRRSPGGAAANVAVALARL--GARVALVGAVGDDPFGDFLLAELRAEGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 72 TQLVFTHANKVPGIYYIETDEQGERSFTYWRhdSAARkvvdFFNPSV--EEELASADMLFISGISLAviEPASRDLFWQI 149
Cdd:COG0524 79 TSGVRRDPGAPTGLAFILVDPDGERTIVFYR--GANA----ELTPEDldEALLAGADILHLGGITLA--SEPPREALLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 150 VQRIKKAGVKIVFDPNYRARLWQSEQETkgqYTIAFELADICLPGIEDLTTLYELHSAQAVMDYLAQFNISEVVVKNGPS 229
Cdd:COG0524 151 LEAARAAGVPVSLDPNYRPALWEPAREL---LRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1823256134 230 SVFTKINGQLFEHQITPVThVVDTTSAGDAFNGAYLGARMAGMD 273
Cdd:COG0524 228 GALLYTGGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLD 270
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-273 |
2.66e-34 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 126.69 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 3 KIFFLGECMVELKAISD---------STLNQSFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLATQ 73
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEglpgelvrvSTVEKGPGGKGANVAVALARL--GGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 74 LVFTHANKVPGIYYIETDEQGERSFTYWRHDSAARKVVDFFNPsvEEELASADMLFISGISLAVIEPASrdlfWQIVQRI 153
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEEN--EDLLENADLLYISGSLPLGLPEAT----LEELIEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 154 KKAGVKivFDPNYRARLWQseqeTKGQYTIAFELADICLPGIEDLTTLY--ELHSAQAVMDYLAQFN---ISEVVVKNGP 228
Cdd:pfam00294 153 AKNGGT--FDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALTgaKLDDIEEALAALHKLLakgIKTVIVTLGA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1823256134 229 SSVFTKINGQLFEHQITPVTHVVDTTSAGDAFNGAYLGARMAGMD 273
Cdd:pfam00294 227 DGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKS 271
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
45-265 |
7.94e-32 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 120.05 E-value: 7.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 45 ECGVVSAIGTDALSIKMRQRFVEEGLATQLVFTHANKVPGIYYIETDEQGERSFTYWRHDSAARkvvdFFNPSVEEELAS 124
Cdd:cd01167 44 KAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGPAADL----LLDTELNPDLLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 125 -ADMLFISGISLAViEPASRDLFWqIVQRIKKAGVKIVFDPNYRARLWQSEQETKGQYTIAFELADICLPGIEDLTTLYE 203
Cdd:cd01167 120 eADILHFGSIALAS-EPSRSALLE-LLEAAKKAGVLISFDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823256134 204 LHSAQAVMDYLAQFNISEVVVKNGP--SSVFTKinGQLFEHQITPVThVVDTTSAGDAFNGAYL 265
Cdd:cd01167 198 EEDPEEIAALLLLFGLKLVLVTRGAdgALLYTK--GGVGEVPGIPVE-VVDTTGAGDAFVAGLL 258
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-265 |
1.17e-27 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 108.87 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 1 MKKIFFLGECMVELKAISDSTLNQSFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLATQLVFTHAN 80
Cdd:PRK09434 2 MNKVWVLGDAVVDLIPEGENRYLKCPGGAPANVAVGIARL--GGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 81 KVPGIYYIETDEQGERSFTYWRHDSAarkvvD-FFNPSVEEELASADMLFISGISLAViEPaSRDLFWQIVQRIKKAGVK 159
Cdd:PRK09434 80 HRTSTVVVDLDDQGERSFTFMVRPSA-----DlFLQPQDLPPFRQGEWLHLCSIALSA-EP-SRSTTFEAMRRIKAAGGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 160 IVFDPNYRARLWQSEQETKGQYTIAFELADICLPGIEDLTTLYELHSAQAVMDYLAQ-FNISEVVVKNGPSSVFTKINGQ 238
Cdd:PRK09434 153 VSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADrYPIALLLVTLGAEGVLVHTRGQ 232
|
250 260
....*....|....*....|....*..
gi 1823256134 239 LFEHQITPVThVVDTTSAGDAFNGAYL 265
Cdd:PRK09434 233 VQHFPAPSVD-PVDTTGAGDAFVAGLL 258
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
25-273 |
1.98e-13 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 69.26 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 25 SFAGDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLATQLVFTHANKVPGIYYIETDEQGER-SFTYWrh 103
Cdd:cd01942 34 EFGGSAGNTAVALAKL--GLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQiAYFYP-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 104 dSAArkvvDFFNPSVEEELASAdmlfisgisLAVIEPASRDLFWQIVQRIKKAGVKIVFDPNYR-ARLWQSEQETkgqyt 182
Cdd:cd01942 110 -GAM----DELEPNDEADPDGL---------ADIVHLSSGPGLIELARELAAGGITVSFDPGQElPRLSGEELEE----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 183 iAFELADICLPGIEDLTTLYELH--SAQAVMDYLAqfnisEVVVKNGP--SSVFTkiNGQLFEHQITPVTHVVDTTSAGD 258
Cdd:cd01942 171 -ILERADILFVNDYEAELLKERTglSEAELASGVR-----VVVVTLGPkgAIVFE--DGEEVEVPAVPAVKVVDTTGAGD 242
|
250
....*....|....*
gi 1823256134 259 AFNGAYLGARMAGMD 273
Cdd:cd01942 243 AFRAGFLYGLLRGYD 257
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
32-275 |
2.69e-13 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 68.78 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 32 NSAVYLKRcfSSLECGVVSAIGTDALSIKMRQRFVEEGLATQLVFTHANKVPGIYYIETDEQGERSFtywrhdsaarkVV 111
Cdd:TIGR02152 36 NQAVAAAR--LGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRI-----------VV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 112 -----DFFNPSV----EEELASADMLFISG-ISLAVIEPAsrdlfwqiVQRIKKAGVKIVFDPNyRARLWQSEQetkgqy 181
Cdd:TIGR02152 103 vaganAELTPEDidaaEALIAESDIVLLQLeIPLETVLEA--------AKIAKKHGVKVILNPA-PAIKDLDDE------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 182 tiAFELADICLPG---IEDLT--TLYELHSAQAVMDYLAQFNISEVVVKNGPSSVFTKINGqlfEHQITPVTHV--VDTT 254
Cdd:TIGR02152 168 --LLSLVDIITPNeteAEILTgiEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKD---ESKLIPAFKVkaVDTT 242
|
250 260
....*....|....*....|.
gi 1823256134 255 SAGDAFNGAYLGARMAGMDEH 275
Cdd:TIGR02152 243 AAGDTFNGAFAVALAEGKSLE 263
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
49-273 |
3.19e-13 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 68.73 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 49 VSAIGTDALSIKMRQRFVEEGLATQLVFTHANKVPGIYYIETDEQGERSFTYwrHDSAARKV----VDffnpSVEEELAS 124
Cdd:cd01174 56 IGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVV--VPGANGELtpadVD----AALELIAA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 125 ADMLFISG-ISLAVIEpasrdlfwQIVQRIKKAGVKIVFDP----NYRARLWqseqetkgqytiafELADICLP------ 193
Cdd:cd01174 130 ADVLLLQLeIPLETVL--------AALRAARRAGVTVILNPaparPLPAELL--------------ALVDILVPneteaa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 194 ---GIEDLTtlyeLHSAQAVMDYLAQFNISEVVVKNGPSSVFTKINGQLFEHQITPVThVVDTTSAGDAFNGAYLGARMA 270
Cdd:cd01174 188 lltGIEVTD----EEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVK-AVDTTGAGDTFIGALAAALAR 262
|
...
gi 1823256134 271 GMD 273
Cdd:cd01174 263 GLS 265
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
24-273 |
4.01e-12 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 65.39 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 24 QSFAGDVYNSAVylkrCFSSL--ECGVVSAIGTDALSIKMRQRFVEEGLATQLVFTHANKVPGIYYIeTDEQGERSFTYW 101
Cdd:cd01945 33 VIGGGNAANAAV----AVARLggQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSI-TDITGDRATISI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 102 RHDSAARKVVDFfnPsvEEELASADMLFISGislaVIEPASRDlfwqIVQRIKKAGVKIVFDPNyRARLWQSEQetkgqy 181
Cdd:cd01945 108 TAIDTQAAPDSL--P--DAILGGADAVLVDG----RQPEAALH----LAQEARARGIPIPLDLD-GGGLRVLEE------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 182 tiAFELADICLPGIEDLTTLYELHSAQAVMdYLAQFNISEVVVKNGP-SSVFTKINGQLFeHQITPVTHVVDTTSAGDAF 260
Cdd:cd01945 169 --LLPLADHAICSENFLRPNTGSADDEALE-LLASLGIPFVAVTLGEaGCLWLERDGELF-HVPAFPVEVVDTTGAGDVF 244
|
250
....*....|...
gi 1823256134 261 NGAYLGARMAGMD 273
Cdd:cd01945 245 HGAFAHALAEGMP 257
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
94-265 |
3.81e-08 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 53.86 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 94 GERSFTYWRHDSAarkvvDFFnpSVEEEL-----ASADMLFISGISLaVIEPaSRDLFWQIVQRIKKAGVKIVFDPNYRA 168
Cdd:PLN02323 108 GEREFMFYRNPSA-----DML--LRESELdldliRKAKIFHYGSISL-ITEP-CRSAHLAAMKIAKEAGALLSYDPNLRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 169 RLWQSEQETKGQYTIAFELADICLPGIEDLTTLY--ELHSAQAVMDyLAQFNISEVVVKNGPSSV--FTKIngqlFEHQI 244
Cdd:PLN02323 179 PLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTggDDPDDDTVVK-LWHPNLKLLLVTEGEEGCryYTKD----FKGRV 253
|
170 180
....*....|....*....|...
gi 1823256134 245 TPVtHV--VDTTSAGDAFNGAYL 265
Cdd:PLN02323 254 EGF-KVkaVDTTGAGDAFVGGLL 275
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
122-267 |
6.96e-07 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 49.02 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 122 LASADMLFISGISLAVIEPAsrdlfwQIVQRIKKAGVKIVFDPNYRARLWqseqeTKGQYTIAFELADICLPGIEDLTTL 201
Cdd:cd00287 55 LVGADAVVISGLSPAPEAVL------DALEEARRRGVPVVLDPGPRAVRL-----DGEELEKLLPGVDILTPNEEEAEAL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1823256134 202 -----YELHSAQAVMDYLAQFNISEVVVKNGP--SSVFTkiNGQLFEHQITPVTHVVDTTSAGDAFNGAYLGA 267
Cdd:cd00287 124 tgrrdLEVKEAAEAAALLLSKGPKVVIVTLGEkgAIVAT--RGGTEVHVPAFPVKVVDTTGAGDAFLAALAAG 194
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
28-273 |
1.12e-06 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 48.89 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 28 GDVYNSAVYLKRcfSSLECGVVSAIGTDALSIKMRQRFVEEGLatQLVFTHANKVPGIYYIETDEQGERSFTYWRhdsaa 107
Cdd:cd01940 23 GNALNVAVYAKR--LGHESAYIGAVGNDDAGAHVRSTLKRLGV--DISHCRVKEGENAVADVELVDGDRIFGLSN----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 108 RKVVDFFNPSVE--EELASADMLFISGISlavIEPASRDLFWQIVqrikKAGVKIVFDPNYRarlWQSEqetkgqytiaf 185
Cdd:cd01940 94 KGGVAREHPFEAdlEYLSQFDLVHTGIYS---HEGHLEKALQALV----GAGALISFDFSDR---WDDD----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 186 eLADICLPGIEDLTTLYELHSAQAVMDYLAQF---NISEVVVKNGPSSVFTKINGQLFEHQITPVThVVDTTSAGDAFNG 262
Cdd:cd01940 153 -YLQLVCPYVDFAFFSASDLSDEEVKAKLKEAvsrGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVE-VVDTLGAGDSFIA 230
|
250
....*....|.
gi 1823256134 263 AYLGARMAGMD 273
Cdd:cd01940 231 GFLLSLLAGGT 241
|
|
| PLN02967 |
PLN02967 |
kinase |
122-275 |
8.01e-06 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 47.35 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 122 LASADMLFISGISLavIEPASRDLFWQIVQRIKKAGVKIVFDPNYRARLWQSEQETKGQYTIAFELADIC---------L 192
Cdd:PLN02967 333 LKEAKMFYFNTHSL--LDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWNLADIIevtkqelefL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 193 PGIE--------DLTTLYELHSAQAVMDYLAQFNISEVVVKNGPSSV--FTKingqlfEHQ----------ITPVTHvvD 252
Cdd:PLN02967 411 CGIEpteefdtkDNDKSKFVHYSPEVVAPLWHENLKVLFVTNGTSKIhyYTK------EHNgavhgmedapITPFTS--D 482
|
170 180
....*....|....*....|...
gi 1823256134 253 TTSAGDAFNGAYLgaRMAGMDEH 275
Cdd:PLN02967 483 MSASGDGIVAGLM--RMLTVQPH 503
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
28-273 |
1.23e-05 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 46.07 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 28 GDVYNSAVYLKRCFSSleCGVVSAIGTDALSIKMRQRFVEEGLATQLVFTHANKVpGIYYIETDEQGERsfTYWRHDSAA 107
Cdd:cd01168 56 GSAANTIRGAAALGGS--AAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPT-GTCAVLVTPDAER--TMCTYLGAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 108 RkvvdFFNPS--VEEELASADMLFISGISLAVIEPASRdlfwQIVQRIKKAGVKIVFD-------PNYRARLWQseqetk 178
Cdd:cd01168 131 N----ELSPDdlDWSLLAKAKYLYLEGYLLTVPPEAIL----LAAEHAKENGVKIALNlsapfivQRFKEALLE------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 179 gqytiAFELADIC---LPGIEDLTTLYELHSAQAVMDYLAQFNiSEVVVKNGPSSVFTKINGQLFEHQITPVTHVVDTTS 255
Cdd:cd01168 197 -----LLPYVDILfgnEEEAEALAEAETTDDLEAALKLLALRC-RIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNG 270
|
250
....*....|....*...
gi 1823256134 256 AGDAFNGAYLGARMAGMD 273
Cdd:cd01168 271 AGDAFAGGFLYGLVQGEP 288
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
52-272 |
5.18e-05 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 44.09 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 52 IGTDALSIKMRQRFVEEGLATQLVFTHANKVPGIYYIETDEQGERSFTYwrHDSA-ARKVVDFFNPSvEEELASADMLFI 130
Cdd:PRK11142 62 VGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGI--HAGAnAALTPALVEAH-RELIANADALLM 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 131 ---SGISlAVIEPAsrdlfwQIVqriKKAGVKIVFDPNyRARLWQSEqetkgqytiAFELADICLPG---IEDLT--TLY 202
Cdd:PRK11142 139 qleTPLE-TVLAAA------KIA---KQHGTKVILNPA-PARELPDE---------LLALVDIITPNeteAEKLTgiRVE 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823256134 203 ELHSAQAVMDYLAQFNISEVVVKNGPSSVFTKINGQlfeHQITPVTHV--VDTTSAGDAFNGAYLGARMAGM 272
Cdd:PRK11142 199 DDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGE---GQRVPGFRVqaVDTIAAGDTFNGALVTALLEGK 267
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
28-273 |
1.19e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 42.80 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 28 GDVYNSAVYLKRCfsSLECGVVSAIGTDALSIKMRQRFVEEGLATQLVFThANKVPGIYYIETDEqGERSFTYWRHDSAA 107
Cdd:PRK09813 24 GNAVNVAVYCTRY--GIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHT-KHGVTAQTQVELHD-NDRVFGDYTEGVMA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 108 RKVVDffnpsvEEE---LASADMlfisgISLAVIEPASRDLfwqivQRIKKAGVKIVFDpnYRARlWQSEqetkgqytia 184
Cdd:PRK09813 100 DFALS------EEDyawLAQYDI-----VHAAIWGHAEDAF-----PQLHAAGKLTAFD--FSDK-WDSP---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 185 feLADICLPGIEdlttlYELHSAQAVMDYLAQFniSEVVVKNGPSSVFTKI--NGQL-------FEHQITPVThVVDTTS 255
Cdd:PRK09813 151 --LWQTLVPHLD-----YAFASAPQEDEFLRLK--MKAIVARGAGVVIVTLgeNGSIawdgaqfWRQAPEPVT-VVDTMG 220
|
250
....*....|....*...
gi 1823256134 256 AGDAFNGAYLGARMAGMD 273
Cdd:PRK09813 221 AGDSFIAGFLCGWLAGMT 238
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
222-298 |
2.51e-03 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 39.24 E-value: 2.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823256134 222 VVVKNGPSSVFTKINGQLFEHQITPV--THVVDTTSAGDAFNGAYLGARMAGMDEHKAVQLAAKAAAVVIQQPGAITPK 298
Cdd:PTZ00247 260 VVFTQGPEPTLIATKDGVTSVPVPPLdqEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYPE 338
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
123-190 |
3.60e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 38.74 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823256134 123 ASADMLFISGISLAVIE--------------PASRDLFWQIVQRIKKAGVKIVFDPNYRARLWQSEQETKGQYTIAFELA 188
Cdd:PLN02543 249 AAEDSLLASELNLAVLKearmfhfnsevltsPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEA 328
|
..
gi 1823256134 189 DI 190
Cdd:PLN02543 329 DI 330
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
213-273 |
7.35e-03 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 37.29 E-value: 7.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823256134 213 YLAQFNISEVVVKNGPSSV--FTKINGQLFEHQITPVTH-VVDTTSAGDAFNGAYLGARMAGMD 273
Cdd:cd01941 207 ILLLPGIKNVIVTLGAKGVllSSREGGVETKLFPAPQPEtVVNVTGAGDAFVAGLVAGLLEGMS 270
|
|
| |
