|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
210-454 |
5.31e-82 |
|
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: 255.43 E-value: 5.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 210 LEPAEVGAAWPFPGAEDDKYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVRYAGP--CTREVLAYSPEVIATRD--- 284
Cdd:COG0063 5 LTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPesAAPAVAAALPELMVIPLpee 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 285 ---LADAGRVQSWVVGPGMGTDEAGRRTLRTVLE-SDVPVLVDADGLTLLADDPDLVRLRSAPTLLTPHSGEFARLTGKE 360
Cdd:COG0063 85 delLELLERADAVVIGPGLGRDEETRELLRALLEaADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLGCS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 361 PGP---DRTASVRALAADWGAHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGA 437
Cdd:COG0063 165 VAEiqaDRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAGV 244
|
250
....*....|....*..
gi 1082341532 438 RAHSLAANLAARGDPEG 454
Cdd:COG0063 245 YLHGLAGDLAAEERGRG 261
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
224-450 |
1.11e-67 |
|
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: 217.48 E-value: 1.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 224 AEDDKYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVRYAGP--CTREVLAYSPEVIAT--------RDLADAGRVQS 293
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPpeAAAVIKSYSPELMVHplletdieELLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 294 WVVGPGMGTDEAGRRTLRTVLESDVPVLVDADGLTLLADDPDLvRLRSAPTLLTPHSGEFARLTGKEPG---PDRTASVR 370
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSL-IKRYGPVVLTPHPGEFARLLGALVEeiqADRLAAAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 371 ALAADWGAHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAANLAARG 450
Cdd:cd01171 160 EAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKK 239
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
234-448 |
2.03e-53 |
|
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: 179.87 E-value: 2.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 234 VGVVAGSESYPGASVLCTSAAITATSGLVRYAGPCTR--EVLAYSPEVIA------TRDLADAGRVQSWVVGPGMGTDEA 305
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAiaVLKSPLPEVMVhplpetSSILEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 306 GRRTLRTVLESDVPVLVDADGLTLLADDPDLVRlRSAPTLLTPHSGEFARLTGKEP--GPDRTASVRALAADWGAHVLLK 383
Cdd:pfam01256 81 GKAALEEVLAKDCPLVIDADALNLLAINNEKPA-REGPTVLTPHPGEFERLCGLAGilGDDRLEAARELAQKLNGTILLK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082341532 384 GRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAANLAA 448
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAA 224
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
7-449 |
1.11e-51 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 182.95 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 7 ADEVRSAEAPLMASLPEG--ALMRRAAHglagvvASELRVRTGAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAV 84
Cdd:PRK10565 20 ADDIRRGEREAADALGLTlyELMLRAGE------AAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 85 LLN-----PEKAHKSgLAAFRAVGGRIADPadDLGLP---DLVIDGIVGIS-GKGPLRPDAA--DLVRRIEVPIVSADLP 153
Cdd:PRK10565 94 AQEsdkplPEEAALA-REAWLNAGGEIHAA--DIVWPesvDLIVDALLGTGlRQAPREPYAAliDQANAHPAPVVALDIP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 154 SGVDPDTGAVEGPAVHASVTVSFGALKRVHALGAAH--CGRVELVPIGLSLGPAGMSAleP-----AEVGAAWPFP-GAE 225
Cdd:PRK10565 171 SGLLAETGATPGAVINADHTVTFIALKPGLLTGKARdvVGQLHFDSLGLDSWLAGQEA--PiqrfdAEQLSQWLKPrRPT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 226 DDKYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVR------YAGPctreVLAYSPEVIA---TRDLADAGrvQSW-- 294
Cdd:PRK10565 249 SHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRvltrseNIAP----LLTARPELMVhelTPDSLEES--LEWad 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 295 --VVGPGMGTDEAGRRTLRTVLESDVPVLVDADGLTLLADDPDLVRLRsaptLLTPHSGEFARLTG---KEPGPDRTASV 369
Cdd:PRK10565 323 vvVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNR----VITPHPGEAARLLGcsvAEIESDRLLSA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 370 RALAADWGAHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAAN-LAA 448
Cdd:PRK10565 399 RRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADvLAA 478
|
.
gi 1082341532 449 R 449
Cdd:PRK10565 479 R 479
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
228-448 |
3.01e-42 |
|
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: 151.38 E-value: 3.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 228 KYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVRYAGP-CTREVLA-YSPEVIATRDLADAG-------RVQSWVVGP 298
Cdd:TIGR00196 21 KGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPeNVITLINsVSPELIVHRLMWKVDedeelleRYDVVVIGP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 299 GMGTDEAGRRTLRTVLESDVPVLVDADGLTLLADDPDlvrlRSAPTLLTPHSGEFARLTGK-EPGPDRTASVRALAADWG 377
Cdd:TIGR00196 101 GLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQK----REGEVILTPHPGEFKRLLGVnEIQGDRLEAAQDIAQKLQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082341532 378 AHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAANLAA 448
Cdd:TIGR00196 177 AVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDLAL 247
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
23-181 |
4.73e-38 |
|
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: 136.59 E-value: 4.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 23 EGALMRRAAHGLAGVVAselrvRTGAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAVLLNPE----KAHKSGLAA 98
Cdd:pfam03853 1 SAVLMENAGRAAARVLK-----ALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEeklsEDARRQLDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 99 FRAVGGRIA--DPADDLGL----PDLVIDGIVGISGKGPLRPDAADLVRRI---EVPIVSADLPSGVDPDTGAVEGPAVH 169
Cdd:pfam03853 76 FKKLGGKIVtdNPDEDLEKllspVDLIIDALLGTGLSGPLRGEYAALIEWInqsGAPVLAVDIPSGLDADTGAVLGTAVR 155
|
170
....*....|..
gi 1082341532 170 ASVTVSFGALKR 181
Cdd:pfam03853 156 ADHTVTFGAPKP 167
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
21-200 |
2.92e-26 |
|
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: 105.96 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 21 LPEGALMRRAAHGLAGvvaselRVRTGAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAV-----LLNPEKAH--- 92
Cdd:TIGR00197 21 LTLDLLMENAGKAVAQ------AVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLkkekrIECTEQAEvnl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 93 -KSGLAAFRAVGGRIADPADDlglpDLVIDGIVGISGKGPLRPDAADLVRRI---EVPIVSADLPSGVDPDTGAVEGPAV 168
Cdd:TIGR00197 95 kALKVGGISIDEGNLVKPEDC----DVIIDAILGTGFKGKLREPFKTIVESInelPAPIVSVDIPSGLDVDTGAIEGPAV 170
|
170 180 190
....*....|....*....|....*....|...
gi 1082341532 169 HASVTVSFGALKRVHALG-AAHCGRVELVPIGL 200
Cdd:TIGR00197 171 NADLTITFHAIKPCLLSDrADVTGELKVGGIGI 203
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
26-180 |
1.27e-08 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 57.17 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 26 LMRRAAHGLAGVVASELRvrtgAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAVLlnPEKAHK---SGLAA---- 98
Cdd:PLN03049 38 LMELAGLSVASAIAEVYS----PSEYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSICY--PKRTDKplyNGLVTqles 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 99 ----FRAVGGRIADPADDLglpDLVIDGIVGISGKGPLRPDAADLVRRI-----EVPIVSADLPSGVDPDTGAVEGPAVH 169
Cdd:PLN03049 112 lsvpFLSVEDLPSDLSSQF---DIVVDAMFGFSFHGAPRPPFDDLIQKLvraagPPPIVSVDIPSGWHVEEGDVNGEGLK 188
|
170
....*....|.
gi 1082341532 170 ASVTVSFGALK 180
Cdd:PLN03049 189 PDMLVSLTAPK 199
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
210-454 |
5.31e-82 |
|
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: 255.43 E-value: 5.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 210 LEPAEVGAAWPFPGAEDDKYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVRYAGP--CTREVLAYSPEVIATRD--- 284
Cdd:COG0063 5 LTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPesAAPAVAAALPELMVIPLpee 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 285 ---LADAGRVQSWVVGPGMGTDEAGRRTLRTVLE-SDVPVLVDADGLTLLADDPDLVRLRSAPTLLTPHSGEFARLTGKE 360
Cdd:COG0063 85 delLELLERADAVVIGPGLGRDEETRELLRALLEaADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLGCS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 361 PGP---DRTASVRALAADWGAHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGA 437
Cdd:COG0063 165 VAEiqaDRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAGV 244
|
250
....*....|....*..
gi 1082341532 438 RAHSLAANLAARGDPEG 454
Cdd:COG0063 245 YLHGLAGDLAAEERGRG 261
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
224-450 |
1.11e-67 |
|
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: 217.48 E-value: 1.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 224 AEDDKYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVRYAGP--CTREVLAYSPEVIAT--------RDLADAGRVQS 293
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPpeAAAVIKSYSPELMVHplletdieELLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 294 WVVGPGMGTDEAGRRTLRTVLESDVPVLVDADGLTLLADDPDLvRLRSAPTLLTPHSGEFARLTGKEPG---PDRTASVR 370
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSL-IKRYGPVVLTPHPGEFARLLGALVEeiqADRLAAAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 371 ALAADWGAHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAANLAARG 450
Cdd:cd01171 160 EAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKK 239
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
234-448 |
2.03e-53 |
|
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: 179.87 E-value: 2.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 234 VGVVAGSESYPGASVLCTSAAITATSGLVRYAGPCTR--EVLAYSPEVIA------TRDLADAGRVQSWVVGPGMGTDEA 305
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAiaVLKSPLPEVMVhplpetSSILEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 306 GRRTLRTVLESDVPVLVDADGLTLLADDPDLVRlRSAPTLLTPHSGEFARLTGKEP--GPDRTASVRALAADWGAHVLLK 383
Cdd:pfam01256 81 GKAALEEVLAKDCPLVIDADALNLLAINNEKPA-REGPTVLTPHPGEFERLCGLAGilGDDRLEAARELAQKLNGTILLK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082341532 384 GRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAANLAA 448
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAA 224
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
7-449 |
1.11e-51 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 182.95 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 7 ADEVRSAEAPLMASLPEG--ALMRRAAHglagvvASELRVRTGAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAV 84
Cdd:PRK10565 20 ADDIRRGEREAADALGLTlyELMLRAGE------AAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 85 LLN-----PEKAHKSgLAAFRAVGGRIADPadDLGLP---DLVIDGIVGIS-GKGPLRPDAA--DLVRRIEVPIVSADLP 153
Cdd:PRK10565 94 AQEsdkplPEEAALA-REAWLNAGGEIHAA--DIVWPesvDLIVDALLGTGlRQAPREPYAAliDQANAHPAPVVALDIP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 154 SGVDPDTGAVEGPAVHASVTVSFGALKRVHALGAAH--CGRVELVPIGLSLGPAGMSAleP-----AEVGAAWPFP-GAE 225
Cdd:PRK10565 171 SGLLAETGATPGAVINADHTVTFIALKPGLLTGKARdvVGQLHFDSLGLDSWLAGQEA--PiqrfdAEQLSQWLKPrRPT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 226 DDKYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVR------YAGPctreVLAYSPEVIA---TRDLADAGrvQSW-- 294
Cdd:PRK10565 249 SHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRvltrseNIAP----LLTARPELMVhelTPDSLEES--LEWad 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 295 --VVGPGMGTDEAGRRTLRTVLESDVPVLVDADGLTLLADDPDLVRLRsaptLLTPHSGEFARLTG---KEPGPDRTASV 369
Cdd:PRK10565 323 vvVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNR----VITPHPGEAARLLGcsvAEIESDRLLSA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 370 RALAADWGAHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAAN-LAA 448
Cdd:PRK10565 399 RRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADvLAA 478
|
.
gi 1082341532 449 R 449
Cdd:PRK10565 479 R 479
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
5-475 |
2.47e-45 |
|
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: 165.43 E-value: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 5 YTADEVRSAEAPLMASL--PEGALMRRAAHGLAGVVASELRVRtgavaGRAVTILVGSGDNGGDALWAGAMLRRRGVAAT 82
Cdd:COG0062 4 LTAAQMRALDRAAIEALgiPGLVLMERAGRAVARAIRRRFPSA-----ARRVLVLCGPGNNGGDGLVAARLLAEAGYNVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 83 AVLLNPEKaHKSGLAA-----FRAVGGRI---ADPADDLGLPDLVIDGIVGISGKGPLRPDAADLVRRI---EVPIVSAD 151
Cdd:COG0062 79 VFLLGDPE-KLSGDAAanlerLKAAGIPIlelDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAInasGAPVLAVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 152 LPSGVDPDTGAVEGPAVHASVTVSFGALKRVHAL--GAAHCGRVELVPIGLS----LGPAGMSALEPAEVGAAWPFPGAE 225
Cdd:COG0062 158 IPSGLDADTGEVLGAAVRADLTVTFGAPKPGLLLgpGRDYCGELVVADIGIGipaaAEAPAALLLLADLLALLLPPRRRS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 226 DDKYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVRYAGP--------CTREVLAYSPEVIATRDLADAGRVQSWVVG 297
Cdd:COG0062 238 HHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPpaaaaallAALPEAMALALDDDEELLLLLAAAVVVAGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 298 PGMGTDEAGRRTLRTVLESDVPVLVDADGLTLLADDPD----LVRLRSAPTLLTPHSGEFARLTGKEPGPDRTASVRALA 373
Cdd:COG0062 318 GGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAalllLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 374 ADWGAHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAANLAARGDPE 453
Cdd:COG0062 398 AAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477
|
490 500
....*....|....*....|..
gi 1082341532 454 GPSGGRAAAPISALVLLAQLRE 475
Cdd:COG0062 478 LLAAAAALIALLLAAALLLLLA 499
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
228-448 |
3.01e-42 |
|
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: 151.38 E-value: 3.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 228 KYSQGVVGVVAGSESYPGASVLCTSAAITATSGLVRYAGP-CTREVLA-YSPEVIATRDLADAG-------RVQSWVVGP 298
Cdd:TIGR00196 21 KGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPeNVITLINsVSPELIVHRLMWKVDedeelleRYDVVVIGP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 299 GMGTDEAGRRTLRTVLESDVPVLVDADGLTLLADDPDlvrlRSAPTLLTPHSGEFARLTGK-EPGPDRTASVRALAADWG 377
Cdd:TIGR00196 101 GLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQK----REGEVILTPHPGEFKRLLGVnEIQGDRLEAAQDIAQKLQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082341532 378 AHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVLSGIVGSLMAAGIAPNRAAAMGARAHSLAANLAA 448
Cdd:TIGR00196 177 AVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDLAL 247
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
23-181 |
4.73e-38 |
|
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: 136.59 E-value: 4.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 23 EGALMRRAAHGLAGVVAselrvRTGAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAVLLNPE----KAHKSGLAA 98
Cdd:pfam03853 1 SAVLMENAGRAAARVLK-----ALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEeklsEDARRQLDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 99 FRAVGGRIA--DPADDLGL----PDLVIDGIVGISGKGPLRPDAADLVRRI---EVPIVSADLPSGVDPDTGAVEGPAVH 169
Cdd:pfam03853 76 FKKLGGKIVtdNPDEDLEKllspVDLIIDALLGTGLSGPLRGEYAALIEWInqsGAPVLAVDIPSGLDADTGAVLGTAVR 155
|
170
....*....|..
gi 1082341532 170 ASVTVSFGALKR 181
Cdd:pfam03853 156 ADHTVTFGAPKP 167
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
21-200 |
2.92e-26 |
|
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: 105.96 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 21 LPEGALMRRAAHGLAGvvaselRVRTGAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAV-----LLNPEKAH--- 92
Cdd:TIGR00197 21 LTLDLLMENAGKAVAQ------AVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLkkekrIECTEQAEvnl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 93 -KSGLAAFRAVGGRIADPADDlglpDLVIDGIVGISGKGPLRPDAADLVRRI---EVPIVSADLPSGVDPDTGAVEGPAV 168
Cdd:TIGR00197 95 kALKVGGISIDEGNLVKPEDC----DVIIDAILGTGFKGKLREPFKTIVESInelPAPIVSVDIPSGLDVDTGAIEGPAV 170
|
170 180 190
....*....|....*....|....*....|...
gi 1082341532 169 HASVTVSFGALKRVHALG-AAHCGRVELVPIGL 200
Cdd:TIGR00197 171 NADLTITFHAIKPCLLSDrADVTGELKVGGIGI 203
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
26-180 |
1.27e-08 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 57.17 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 26 LMRRAAHGLAGVVASELRvrtgAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAVLlnPEKAHK---SGLAA---- 98
Cdd:PLN03049 38 LMELAGLSVASAIAEVYS----PSEYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSICY--PKRTDKplyNGLVTqles 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 99 ----FRAVGGRIADPADDLglpDLVIDGIVGISGKGPLRPDAADLVRRI-----EVPIVSADLPSGVDPDTGAVEGPAVH 169
Cdd:PLN03049 112 lsvpFLSVEDLPSDLSSQF---DIVVDAMFGFSFHGAPRPPFDDLIQKLvraagPPPIVSVDIPSGWHVEEGDVNGEGLK 188
|
170
....*....|.
gi 1082341532 170 ASVTVSFGALK 180
Cdd:PLN03049 189 PDMLVSLTAPK 199
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
54-180 |
7.76e-08 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 53.34 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 54 VTILVGSGDNGGDALWAGAMLRRRGVAATAVLlnPEKAHKS------------GLAAFRAVGGRIADPADDLGLPDLVID 121
Cdd:PLN03050 63 VLLVCGPGNNGGDGLVAARHLAHFGYEVTVCY--PKQSSKPhyenlvtqcedlGIPFVQAIGGTNDSSKPLETTYDVIVD 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082341532 122 GIVGISGKG-PLRPDAADLV-----RRIEVPIVSADLPSGVDPDTGAVEGPAVHASVTVSFGALK 180
Cdd:PLN03050 141 AIFGFSFHGaPRAPFDTLLAqmvqqQKSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPK 205
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
19-483 |
4.59e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 49.49 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 19 ASLPEGALMRRAAHGLAGVVASELRVRTGAVAGRAVTILVGSGDNGGDALWAGAMLRRRGVAATAVLLNPEKAHKSGLAA 98
Cdd:COG3321 861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 99 FRAVGGRIADPADDLGLPDLVIDGIVGISGKGPLRPDAADLVRRIEVPIVSADLPSGVD---PDTGAVEGPAVHASVTVS 175
Cdd:COG3321 941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAaalALLAAAALLLAAAAAAAA 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 176 FGALKRVHALGAAHCGRVELVPIGLSLGPAGMSALEPAEVGAAWPFPGAEDDKYSQGVVGVVAGSESYPGASVLCTSAAI 255
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 256 TATSGLVRYAGPCTREVLAYSPEVIATRDLADAGRVQSWVVGPGMGTDEAGRRTLRTVLESDVPVLVDADGLTLLADDPD 335
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALA 1180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 336 LVRLRSAPTLLTPHSGEFARLTGKEPGPDRTASVRALAADWGAHVLLKGRATVIAEPGGDVFVNEAGGSWSATAGAGDVL 415
Cdd:COG3321 1181 LAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALA 1260
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082341532 416 SGIVGSLMAAGIAPNRAAAMGARAHSLAANLAARGDPEGPSGGRAAAPISALVLLAQLRESIRILRAG 483
Cdd:COG3321 1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAA 1328
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
54-180 |
2.72e-05 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 46.47 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082341532 54 VTILVGSGDNGGDALWAGAMLRRRGVAATavLLNPEKAHK---SGLAA--------FRAVGGRIADPADDLglpDLVIDG 122
Cdd:PLN02918 138 VLAICGPGNNGGDGLVAARHLHHFGYKPF--VCYPKRTAKplyTGLVTqleslsvpFVSVEDLPADLSKDF---DIIVDA 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082341532 123 IVGISGKGPLRPDAADLVRRI-----------EVPIVSADLPSGVDPDTGAVEGPAVHASVTVSFGALK 180
Cdd:PLN02918 213 MFGFSFHGAPRPPFDDLIRRLvslqnyeqtlkHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPK 281
|
|
| |
