|
Name |
Accession |
Description |
Interval |
E-value |
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
209-464 |
8.15e-100 |
|
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]
:
Pssm-ID: 272955 Cd Length: 270 Bit Score: 300.07 E-value: 8.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 209 DTFLLEKSDLKLPLRDKkNAHKGDYGHAHILLGK--HSGAGLLSALSALSFGSGVVSVQALECEITS--SNKPLELVFCE 284
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDP-NSHKGQYGRVLIIGGSddYSGAPLLAALAALRAGAGLVTVAAPENVITLinSVSPELIVHRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 285 N--------FPNPLSAFALGMGL---EGFPKDFNKWLELA-PCVLDAGVFYHKEMLQALEKEVVLTPHPKEFLSLLKlvg 352
Cdd:TIGR00196 80 MwkvdedeeLLERYDVVVIGPGLgqdPSFKKAVEEVLELDkPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 353 iniSMLELLDNkLEIARDFSQKYPKVVLLLKGANTLIAHQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDAT 432
Cdd:TIGR00196 157 ---VNEIQGDR-LEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAA 232
|
250 260 270
....*....|....*....|....*....|....*
gi 526123214 433 INASLAHAIASLEFKNN---YALTPLDLIEKIKRL 464
Cdd:TIGR00196 233 CNAAFAHGLAGDLALKNhgaYGLTALDLIEKIPRV 267
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
1-201 |
1.69e-75 |
|
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]
:
Pssm-ID: 272956 [Multi-domain] Cd Length: 205 Bit Score: 235.38 E-value: 1.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 1 MLSVYEKVNALDKRALEEFNLSEDILMENAAMALERAVLQNASLGAKVIILCGSGDNGGDGYALARRLVGrFKTLVFEMK 80
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKG-FGVEVFLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 81 LAKSPMCQLQKERAKKVG-VVIKAWEEKNE--DLECDVLIDCVVGSNFKGEL-EPF-LNFESLSQKARFKIACDIPSGID 155
Cdd:TIGR00197 80 KEKRIECTEQAEVNLKALkVGGISIDEGNLvkPEDCDVIIDAILGTGFKGKLrEPFkTIVESINELPAPIVSVDIPSGLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 526123214 156 SK-GRVDKRAFKAHMTISMGAVKSCLLSDRAkDYIGELKVGHLGVFN 201
Cdd:TIGR00197 160 VDtGAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIPP 205
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
209-464 |
8.15e-100 |
|
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]
Pssm-ID: 272955 Cd Length: 270 Bit Score: 300.07 E-value: 8.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 209 DTFLLEKSDLKLPLRDKkNAHKGDYGHAHILLGK--HSGAGLLSALSALSFGSGVVSVQALECEITS--SNKPLELVFCE 284
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDP-NSHKGQYGRVLIIGGSddYSGAPLLAALAALRAGAGLVTVAAPENVITLinSVSPELIVHRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 285 N--------FPNPLSAFALGMGL---EGFPKDFNKWLELA-PCVLDAGVFYHKEMLQALEKEVVLTPHPKEFLSLLKlvg 352
Cdd:TIGR00196 80 MwkvdedeeLLERYDVVVIGPGLgqdPSFKKAVEEVLELDkPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 353 iniSMLELLDNkLEIARDFSQKYPKVVLLLKGANTLIAHQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDAT 432
Cdd:TIGR00196 157 ---VNEIQGDR-LEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAA 232
|
250 260 270
....*....|....*....|....*....|....*
gi 526123214 433 INASLAHAIASLEFKNN---YALTPLDLIEKIKRL 464
Cdd:TIGR00196 233 CNAAFAHGLAGDLALKNhgaYGLTALDLIEKIPRV 267
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
1-201 |
1.69e-75 |
|
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]
Pssm-ID: 272956 [Multi-domain] Cd Length: 205 Bit Score: 235.38 E-value: 1.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 1 MLSVYEKVNALDKRALEEFNLSEDILMENAAMALERAVLQNASLGAKVIILCGSGDNGGDGYALARRLVGrFKTLVFEMK 80
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKG-FGVEVFLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 81 LAKSPMCQLQKERAKKVG-VVIKAWEEKNE--DLECDVLIDCVVGSNFKGEL-EPF-LNFESLSQKARFKIACDIPSGID 155
Cdd:TIGR00197 80 KEKRIECTEQAEVNLKALkVGGISIDEGNLvkPEDCDVIIDAILGTGFKGKLrEPFkTIVESINELPAPIVSVDIPSGLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 526123214 156 SK-GRVDKRAFKAHMTISMGAVKSCLLSDRAkDYIGELKVGHLGVFN 201
Cdd:TIGR00197 160 VDtGAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIPP 205
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
236-463 |
1.84e-69 |
|
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).
Pssm-ID: 396007 Cd Length: 242 Bit Score: 221.08 E-value: 1.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 236 AHILLG--KHSGAGLLSALSALSFGSGVVSVQALECEITSSNKPLELVFCENFPNP---------LSAFALGMGLEGFPK 304
Cdd:pfam01256 1 VLVIGGskDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETssileklsrYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 305 ----DFNKWLELAPCVLDAGVFYHKE---MLQALEKEVVLTPHPKEFLSLLKLVGINismlelLDNKLEIARDFSQKYPK 377
Cdd:pfam01256 81 gkaaLEEVLAKDCPLVIDADALNLLAinnEKPAREGPTVLTPHPGEFERLCGLAGIL------GDDRLEAARELAQKLNG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 378 VVLLLKGANTLIAHQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDATINASLAHAIASLEFKNNYA--LTPL 455
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGvyMLPT 234
|
....*...
gi 526123214 456 DLIEKIKR 463
Cdd:pfam01256 235 LLSKIIPR 242
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
10-442 |
9.41e-59 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 200.87 E-value: 9.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 10 ALDKRALEEFNLSEDILMENAAMALERAVLQNASL-GAKVIILCGSGDNGGDGYALARRLVGR-FKTLVFEMKLAK--SP 85
Cdd:COG0062 11 ALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSaARRVLVLCGPGNNGGDGLVAARLLAEAgYNVTVFLLGDPEklSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 86 MCQLQKERAKKVGVVIKAWEEKNEDL-ECDVLIDCVVGSNFKGEL-EPFLN-FESLSQKARFKIACDIPSGIDS-KGRVD 161
Cdd:COG0062 91 DAAANLERLKAAGIPILELDDELPELaEADLIVDALFGTGLSRPLrGPYAElIEAINASGAPVLAVDIPSGLDAdTGEVL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 162 KRAFKAHMTISMGAVKSCLLSDRAKDYIGELKVGHLGVFNQIYEIPTDTFLLEKSDLKLPLRDKKNAHKGDYGHAHILLG 241
Cdd:COG0062 171 GAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKGGGGGVLVIG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 242 ---KHSGAGLLSALSALSFGSGVVSVQALECEITSSNKPLELVFCENFPNPLSAFAL-------------GMGLEGFPKD 305
Cdd:COG0062 251 gggGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLlaaavvvagggggGGGGAGGGLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 306 FNKWLELAPCVLDAGVFYHKEMLQALEKEVVLTPHPKEFLSLLKLVGINISMLELLDNKLEIARDFSQKYPKVVLLLKGA 385
Cdd:COG0062 331 LLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVAAAAVVAGAA 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 526123214 386 NTLIAHQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDATINASLAHAIA 442
Cdd:COG0062 411 GVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAA 467
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
226-461 |
4.06e-53 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 178.96 E-value: 4.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 226 KNAHKGDYGHAHILLGKH--SGAGLLSALSALSFGSGVVSVQALECEITS-SNKPLELVFC----------ENFPNPLSA 292
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRgyTGAAYLAALAALRAGAGLVTVATPPEAAAViKSYSPELMVHplletdieelLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 293 FALGMGL---EGFPKDFNKWLELA-PCVLDAGVFYHKEM---LQALEKEVVLTPHPKEFLSLLKLVGINISmlellDNKL 365
Cdd:cd01171 81 VVIGPGLgrdEEAAEILEKALAKDkPLVLDADALNLLADepsLIKRYGPVVLTPHPGEFARLLGALVEEIQ-----ADRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 366 EIARDFSQKYpKVVLLLKGANTLIAH-QGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDATINASLAHAIAS- 443
Cdd:cd01171 156 AAAREAAAKL-GATVVLKGAVTVIADpDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGd 234
|
250
....*....|....*....
gi 526123214 444 -LEFKNNYALTPLDLIEKI 461
Cdd:cd01171 235 lAAKKKGAGLTAADLVAEI 253
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
23-179 |
3.04e-34 |
|
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.
Pssm-ID: 427546 [Multi-domain] Cd Length: 168 Bit Score: 126.19 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 23 EDILMENAAMALERAVLQNAS-LGAKVIILCGSGDNGGDGYALARRLVGR-FKTLVFEM--KLAKSPMCQLQKERAKKVG 98
Cdd:pfam03853 1 SAVLMENAGRAAARVLKALLSpAGPKVLILCGPGNNGGDGLAAARHLANRgAKVTVLLLgpEEKLSEDARRQLDLFKKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 99 VVIKAW----EEKNEDLECDVLIDCVVGSNFKGEL-EPFLN-FESLSQKARFKIACDIPSGID-SKGRVDKRAFKAHMTI 171
Cdd:pfam03853 81 GKIVTDnpdeDLEKLLSPVDLIIDALLGTGLSGPLrGEYAAlIEWINQSGAPVLAVDIPSGLDaDTGAVLGTAVRADHTV 160
|
....*...
gi 526123214 172 SMGAVKSC 179
Cdd:pfam03853 161 TFGAPKPG 168
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
6-443 |
3.07e-33 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 131.34 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 6 EKVNALDKRALEEFNLSEDILME---NAAMALERAVLQNAslgAKVIILCGSGDNGGDGYALAR--RLVGRFKTLV-FEM 79
Cdd:PRK10565 21 DDIRRGEREAADALGLTLYELMLragEAAFQVARSAYPDA---RHWLVLCGHGNNGGDGYVVARlaQAAGIDVTLLaQES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 80 KLAKSPMCQLQKERAKKVGVVIKA----WEEKnedleCDVLIDCVVGSNFKgeLEPFLNFESLSQKARF----KIACDIP 151
Cdd:PRK10565 98 DKPLPEEAALAREAWLNAGGEIHAadivWPES-----VDLIVDALLGTGLR--QAPREPYAALIDQANAhpapVVALDIP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 152 SGIDSK-GRVDKRAFKAHMTISMGAVKSCLLSDRAKDYIGELKVGHLGVFNQIYEIPTDTFLLEKSDLKLPLRDKK-NAH 229
Cdd:PRK10565 171 SGLLAEtGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPRRpTSH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 230 KGDYGHAHILLGKH--SGAGLLSALSALSFGSGVVSVqaleceITSSNK--PLELVFCENFPNPLSAFALGMGLEgfpkd 305
Cdd:PRK10565 251 KGDHGRLLIIGGDHgtAGAIRMAGEAALRSGAGLVRV------LTRSENiaPLLTARPELMVHELTPDSLEESLE----- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 306 fnkWLELApcVLDAGVF---YHKEMLQALE-----------------------KEVVLTPHPKEFLSLLklvgiNISMLE 359
Cdd:PRK10565 320 ---WADVV--VIGPGLGqqeWGKKALQKVEnfrkpmlwdadalnllainpdkrHNRVITPHPGEAARLL-----GCSVAE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 360 LLDNKLEIARDFSQKYPKVVlLLKGANTLIA-HQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDATINASLA 438
Cdd:PRK10565 390 IESDRLLSARRLVKRYGGVV-VLKGAGTVIAaEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVA 468
|
....*
gi 526123214 439 HAIAS 443
Cdd:PRK10565 469 HGAAA 473
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
10-221 |
6.86e-13 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 70.26 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 10 ALDKRALEEFNLSEDILMENAAMALERAVLQ--NASLGAKVIILCGSGDNGGDGYALARRL--VGrFKTLVFEMKLAKSP 85
Cdd:PLN03049 22 AIDEHLMGPLGFSVDQLMELAGLSVASAIAEvySPSEYRRVLALCGPGNNGGDGLVAARHLhhFG-YKPSICYPKRTDKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 86 MCQLQKERAKKVGVVIKAWEEKNEDL--ECDVLIDCVVGSNFKGELEPflNFESLSQK------ARFKIACDIPSGID-S 156
Cdd:PLN03049 101 LYNGLVTQLESLSVPFLSVEDLPSDLssQFDIVVDAMFGFSFHGAPRP--PFDDLIQKlvraagPPPIVSVDIPSGWHvE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526123214 157 KGRVDKRAFKAHMTISMGAVKSCllsdrAKDYIGElkvGHL--GVFnqiyeIPtdTFLLEKSDLKLP 221
Cdd:PLN03049 179 EGDVNGEGLKPDMLVSLTAPKLC-----AKMFKGP---HHFlgGRF-----VP--PAIVEKFKLHLP 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
209-464 |
8.15e-100 |
|
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]
Pssm-ID: 272955 Cd Length: 270 Bit Score: 300.07 E-value: 8.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 209 DTFLLEKSDLKLPLRDKkNAHKGDYGHAHILLGK--HSGAGLLSALSALSFGSGVVSVQALECEITS--SNKPLELVFCE 284
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDP-NSHKGQYGRVLIIGGSddYSGAPLLAALAALRAGAGLVTVAAPENVITLinSVSPELIVHRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 285 N--------FPNPLSAFALGMGL---EGFPKDFNKWLELA-PCVLDAGVFYHKEMLQALEKEVVLTPHPKEFLSLLKlvg 352
Cdd:TIGR00196 80 MwkvdedeeLLERYDVVVIGPGLgqdPSFKKAVEEVLELDkPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 353 iniSMLELLDNkLEIARDFSQKYPKVVLLLKGANTLIAHQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDAT 432
Cdd:TIGR00196 157 ---VNEIQGDR-LEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAA 232
|
250 260 270
....*....|....*....|....*....|....*
gi 526123214 433 INASLAHAIASLEFKNN---YALTPLDLIEKIKRL 464
Cdd:TIGR00196 233 CNAAFAHGLAGDLALKNhgaYGLTALDLIEKIPRV 267
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
1-201 |
1.69e-75 |
|
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]
Pssm-ID: 272956 [Multi-domain] Cd Length: 205 Bit Score: 235.38 E-value: 1.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 1 MLSVYEKVNALDKRALEEFNLSEDILMENAAMALERAVLQNASLGAKVIILCGSGDNGGDGYALARRLVGrFKTLVFEMK 80
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKG-FGVEVFLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 81 LAKSPMCQLQKERAKKVG-VVIKAWEEKNE--DLECDVLIDCVVGSNFKGEL-EPF-LNFESLSQKARFKIACDIPSGID 155
Cdd:TIGR00197 80 KEKRIECTEQAEVNLKALkVGGISIDEGNLvkPEDCDVIIDAILGTGFKGKLrEPFkTIVESINELPAPIVSVDIPSGLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 526123214 156 SK-GRVDKRAFKAHMTISMGAVKSCLLSDRAkDYIGELKVGHLGVFN 201
Cdd:TIGR00197 160 VDtGAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIPP 205
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
236-463 |
1.84e-69 |
|
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).
Pssm-ID: 396007 Cd Length: 242 Bit Score: 221.08 E-value: 1.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 236 AHILLG--KHSGAGLLSALSALSFGSGVVSVQALECEITSSNKPLELVFCENFPNP---------LSAFALGMGLEGFPK 304
Cdd:pfam01256 1 VLVIGGskDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETssileklsrYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 305 ----DFNKWLELAPCVLDAGVFYHKE---MLQALEKEVVLTPHPKEFLSLLKLVGINismlelLDNKLEIARDFSQKYPK 377
Cdd:pfam01256 81 gkaaLEEVLAKDCPLVIDADALNLLAinnEKPAREGPTVLTPHPGEFERLCGLAGIL------GDDRLEAARELAQKLNG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 378 VVLLLKGANTLIAHQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDATINASLAHAIASLEFKNNYA--LTPL 455
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGvyMLPT 234
|
....*...
gi 526123214 456 DLIEKIKR 463
Cdd:pfam01256 235 LLSKIIPR 242
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
10-442 |
9.41e-59 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 200.87 E-value: 9.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 10 ALDKRALEEFNLSEDILMENAAMALERAVLQNASL-GAKVIILCGSGDNGGDGYALARRLVGR-FKTLVFEMKLAK--SP 85
Cdd:COG0062 11 ALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSaARRVLVLCGPGNNGGDGLVAARLLAEAgYNVTVFLLGDPEklSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 86 MCQLQKERAKKVGVVIKAWEEKNEDL-ECDVLIDCVVGSNFKGEL-EPFLN-FESLSQKARFKIACDIPSGIDS-KGRVD 161
Cdd:COG0062 91 DAAANLERLKAAGIPILELDDELPELaEADLIVDALFGTGLSRPLrGPYAElIEAINASGAPVLAVDIPSGLDAdTGEVL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 162 KRAFKAHMTISMGAVKSCLLSDRAKDYIGELKVGHLGVFNQIYEIPTDTFLLEKSDLKLPLRDKKNAHKGDYGHAHILLG 241
Cdd:COG0062 171 GAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKGGGGGVLVIG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 242 ---KHSGAGLLSALSALSFGSGVVSVQALECEITSSNKPLELVFCENFPNPLSAFAL-------------GMGLEGFPKD 305
Cdd:COG0062 251 gggGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLlaaavvvagggggGGGGAGGGLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 306 FNKWLELAPCVLDAGVFYHKEMLQALEKEVVLTPHPKEFLSLLKLVGINISMLELLDNKLEIARDFSQKYPKVVLLLKGA 385
Cdd:COG0062 331 LLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVAAAAVVAGAA 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 526123214 386 NTLIAHQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDATINASLAHAIA 442
Cdd:COG0062 411 GVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAA 467
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
209-464 |
1.64e-56 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];
Pssm-ID: 439833 Cd Length: 280 Bit Score: 188.79 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 209 DTFLLEKSDLK--LPLRdKKNAHKGDYGHAHILLGKH--SGAGLLSALSALSFGSGVVSVQALECEITS-SNKPLELVFC 283
Cdd:COG0063 1 DARLLTPADLRalLPPR-PPDSHKGSRGHVLVIGGSRgyPGAAVLAARAALRAGAGLVTVAVPESAAPAvAAALPELMVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 284 --------ENFPNPLSAFALGMGLeGFPKDFNKWLELA------PCVLDAG----VFYHKEMLQALEKEVVLTPHPKEFL 345
Cdd:COG0063 80 plpeedelLELLERADAVVIGPGL-GRDEETRELLRALleaadkPLVLDADalnlLAEDPELLAALPAPTVLTPHPGEFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 346 SLLklvgiNISMLELLDNKLEIARDFSQKYpKVVLLLKGANTLIAH-QGQVFINILGSVALAKAGSGDVLAGLILSLLSQ 424
Cdd:COG0063 159 RLL-----GCSVAEIQADRLEAAREAAKRY-GAVVVLKGAGTVIAApDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 526123214 425 NYTPLDATINASLAHAIASLEF--KNNYALTPLDLIEKIKRL 464
Cdd:COG0063 233 GLDPFEAAAAGVYLHGLAGDLAaeERGRGLLASDLIEALPAA 274
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
226-461 |
4.06e-53 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 178.96 E-value: 4.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 226 KNAHKGDYGHAHILLGKH--SGAGLLSALSALSFGSGVVSVQALECEITS-SNKPLELVFC----------ENFPNPLSA 292
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRgyTGAAYLAALAALRAGAGLVTVATPPEAAAViKSYSPELMVHplletdieelLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 293 FALGMGL---EGFPKDFNKWLELA-PCVLDAGVFYHKEM---LQALEKEVVLTPHPKEFLSLLKLVGINISmlellDNKL 365
Cdd:cd01171 81 VVIGPGLgrdEEAAEILEKALAKDkPLVLDADALNLLADepsLIKRYGPVVLTPHPGEFARLLGALVEEIQ-----ADRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 366 EIARDFSQKYpKVVLLLKGANTLIAH-QGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDATINASLAHAIAS- 443
Cdd:cd01171 156 AAAREAAAKL-GATVVLKGAVTVIADpDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGd 234
|
250
....*....|....*....
gi 526123214 444 -LEFKNNYALTPLDLIEKI 461
Cdd:cd01171 235 lAAKKKGAGLTAADLVAEI 253
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
23-179 |
3.04e-34 |
|
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.
Pssm-ID: 427546 [Multi-domain] Cd Length: 168 Bit Score: 126.19 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 23 EDILMENAAMALERAVLQNAS-LGAKVIILCGSGDNGGDGYALARRLVGR-FKTLVFEM--KLAKSPMCQLQKERAKKVG 98
Cdd:pfam03853 1 SAVLMENAGRAAARVLKALLSpAGPKVLILCGPGNNGGDGLAAARHLANRgAKVTVLLLgpEEKLSEDARRQLDLFKKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 99 VVIKAW----EEKNEDLECDVLIDCVVGSNFKGEL-EPFLN-FESLSQKARFKIACDIPSGID-SKGRVDKRAFKAHMTI 171
Cdd:pfam03853 81 GKIVTDnpdeDLEKLLSPVDLIIDALLGTGLSGPLrGEYAAlIEWINQSGAPVLAVDIPSGLDaDTGAVLGTAVRADHTV 160
|
....*...
gi 526123214 172 SMGAVKSC 179
Cdd:pfam03853 161 TFGAPKPG 168
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
6-443 |
3.07e-33 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 131.34 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 6 EKVNALDKRALEEFNLSEDILME---NAAMALERAVLQNAslgAKVIILCGSGDNGGDGYALAR--RLVGRFKTLV-FEM 79
Cdd:PRK10565 21 DDIRRGEREAADALGLTLYELMLragEAAFQVARSAYPDA---RHWLVLCGHGNNGGDGYVVARlaQAAGIDVTLLaQES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 80 KLAKSPMCQLQKERAKKVGVVIKA----WEEKnedleCDVLIDCVVGSNFKgeLEPFLNFESLSQKARF----KIACDIP 151
Cdd:PRK10565 98 DKPLPEEAALAREAWLNAGGEIHAadivWPES-----VDLIVDALLGTGLR--QAPREPYAALIDQANAhpapVVALDIP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 152 SGIDSK-GRVDKRAFKAHMTISMGAVKSCLLSDRAKDYIGELKVGHLGVFNQIYEIPTDTFLLEKSDLKLPLRDKK-NAH 229
Cdd:PRK10565 171 SGLLAEtGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPRRpTSH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 230 KGDYGHAHILLGKH--SGAGLLSALSALSFGSGVVSVqaleceITSSNK--PLELVFCENFPNPLSAFALGMGLEgfpkd 305
Cdd:PRK10565 251 KGDHGRLLIIGGDHgtAGAIRMAGEAALRSGAGLVRV------LTRSENiaPLLTARPELMVHELTPDSLEESLE----- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 306 fnkWLELApcVLDAGVF---YHKEMLQALE-----------------------KEVVLTPHPKEFLSLLklvgiNISMLE 359
Cdd:PRK10565 320 ---WADVV--VIGPGLGqqeWGKKALQKVEnfrkpmlwdadalnllainpdkrHNRVITPHPGEAARLL-----GCSVAE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 360 LLDNKLEIARDFSQKYPKVVlLLKGANTLIA-HQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDATINASLA 438
Cdd:PRK10565 390 IESDRLLSARRLVKRYGGVV-VLKGAGTVIAaEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVA 468
|
....*
gi 526123214 439 HAIAS 443
Cdd:PRK10565 469 HGAAA 473
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
10-221 |
6.86e-13 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 70.26 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 10 ALDKRALEEFNLSEDILMENAAMALERAVLQ--NASLGAKVIILCGSGDNGGDGYALARRL--VGrFKTLVFEMKLAKSP 85
Cdd:PLN03049 22 AIDEHLMGPLGFSVDQLMELAGLSVASAIAEvySPSEYRRVLALCGPGNNGGDGLVAARHLhhFG-YKPSICYPKRTDKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 86 MCQLQKERAKKVGVVIKAWEEKNEDL--ECDVLIDCVVGSNFKGELEPflNFESLSQK------ARFKIACDIPSGID-S 156
Cdd:PLN03049 101 LYNGLVTQLESLSVPFLSVEDLPSDLssQFDIVVDAMFGFSFHGAPRP--PFDDLIQKlvraagPPPIVSVDIPSGWHvE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526123214 157 KGRVDKRAFKAHMTISMGAVKSCllsdrAKDYIGElkvGHL--GVFnqiyeIPtdTFLLEKSDLKLP 221
Cdd:PLN03049 179 EGDVNGEGLKPDMLVSLTAPKLC-----AKMFKGP---HHFlgGRF-----VP--PAIVEKFKLHLP 230
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
8-177 |
7.85e-10 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 59.12 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 8 VNALDKRALEE-------FNLseDILMENAAMALERAVLQNASLG---------AKVIILCGSGDNGGDGYALARRLV-- 69
Cdd:PLN03050 9 LNAQDAAALDEelmstpgFSL--EQLMELAGLSVAEAVYEVADGEkasnppgrhPRVLLVCGPGNNGGDGLVAARHLAhf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 70 GRFKTLVFEmKLAKSPMCQLQKERAKKVGVVI------KAWEEKNEDLECDVLIDCVVGSNFKGE-LEPFLNFesLSQKA 142
Cdd:PLN03050 87 GYEVTVCYP-KQSSKPHYENLVTQCEDLGIPFvqaiggTNDSSKPLETTYDVIVDAIFGFSFHGApRAPFDTL--LAQMV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 526123214 143 RFK------IACDIPSGID-SKGRVDKRAFKAHMTISMGAVK 177
Cdd:PLN03050 164 QQQkspppiVSVDVPSGWDvDEGDVSGTGMRPDVLVSLTAPK 205
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
11-179 |
1.37e-09 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 60.34 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 11 LDKRALEEFNLSEDILMENAAMALERAVLQNASLG--AKVIILCGSGDNGGDGYALARRL--VGrFKTLVFEMKLAKSPM 86
Cdd:PLN02918 99 IDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGeySRVLAICGPGNNGGDGLVAARHLhhFG-YKPFVCYPKRTAKPL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 87 CQLQKERAKKVGVVIKAWEEKNEDL--ECDVLIDCVVGSNFKGELEP--------FLNFESLSQKARFK--IACDIPSGI 154
Cdd:PLN02918 178 YTGLVTQLESLSVPFVSVEDLPADLskDFDIIVDAMFGFSFHGAPRPpfddlirrLVSLQNYEQTLKHPviVSVDIPSGW 257
|
170 180
....*....|....*....|....*.
gi 526123214 155 D-SKGRVDKRAFKAHMTISMGAVKSC 179
Cdd:PLN02918 258 HvEEGDHEGGGIKPDMLVSLTAPKLC 283
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
361-443 |
1.64e-05 |
|
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.
Pssm-ID: 238575 [Multi-domain] Cd Length: 242 Bit Score: 45.99 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526123214 361 LDNKLEIARDFSQKYpKVVLLLKGANTLIAHQGQVFINILGSVALAK-AGSGDVLAGLILSLLSQNYTPLDATINASLAH 439
Cdd:cd01170 138 EEDALELAKALARKY-GAVVVVTGEVDYITDGERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVSAVLVY 216
|
....
gi 526123214 440 AIAS 443
Cdd:cd01170 217 GIAG 220
|
|
| |
