|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
221-500 |
6.21e-104 |
|
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: 312.06 E-value: 6.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 221 PWHFTQLRDAEVALPRRGKFGYKNTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCLT 300
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 301 DAQADFIsgLPDLGPYQAVGIGPGLGQEAATRAVLEQLLRTAKVPLIIDADALNLLGAHRELLDLLPENTVLTPHIGEFT 380
Cdd:COG0063 81 LPEEDEL--LELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 381 RLTEKARDD--YHRLDLLRAFTQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPL 458
Cdd:COG0063 159 RLLGCSVAEiqADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLA-QGLDPF 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 996009940 459 HAARLAVLAHGHAGDLAAAEtGEAGLIAGDLVAHIGPALQAL 500
Cdd:COG0063 238 EAAAAGVYLHGLAGDLAAEE-RGRGLLASDLIEALPAALREL 278
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
242-493 |
4.99e-72 |
|
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: 229.04 E-value: 4.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 242 YKNTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCLTDAQADFISGLPDLGPYQAVGI 321
Cdd:cd01171 4 HKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLERADAVVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 322 GPGLGQEAATRAVLEQLLRTaKVPLIIDADALNLLGAHRELLdLLPENTVLTPHIGEFTRLT--EKARDDYHRLDLLRAF 399
Cdd:cd01171 84 GPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPSLI-KRYGPVVLTPHPGEFARLLgaLVEEIQADRLAAAREA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 400 TQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPLHAARLAVLAHGHAGDLAAAET 479
Cdd:cd01171 162 AAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLA-QGLSPLEAAALAVYLHGLAGDLAAKKK 240
|
250
....*....|....
gi 996009940 480 GeAGLIAGDLVAHI 493
Cdd:cd01171 241 G-AGLTAADLVAEI 253
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
10-493 |
1.00e-61 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 209.92 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 10 RQLDQATMQAQGITSVELMERAAGALAGWLTQRYTHARagEILVLCGPGNNGGDGLALARLLHAAGYAVHVALLP----- 84
Cdd:PRK10565 24 RRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDAR--HWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQEsdkpl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 85 ---AAQHSADWqhnrqhLPSGvpvAELATNALPAIAPGALVIDALFGTGLARPLGGLEATVVAHLTQAKACVVAVDLPSG 161
Cdd:PRK10565 102 peeAALAREAW------LNAG---GEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 162 LLADGPQPdPGApVVRADYTLSFGLPKLAFLLPQNAEYVGEWHVLDIGLdQDFIDQADTPwhFTQLRDAEVA--LPRRGK 239
Cdd:PRK10565 173 LLAETGAT-PGA-VINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGL-DSWLAGQEAP--IQRFDAEQLSqwLKPRRP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 240 FGYKNTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMC--LTDAQADfisglPDLGPYQ 317
Cdd:PRK10565 248 TSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVheLTPDSLE-----ESLEWAD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 318 AVGIGPGLGQEAATRAVLeQLLRTAKVPLIIDADALNLLG--AHRElldllpENTVLTPHIGEFTRLTEKARDDYH--RL 393
Cdd:PRK10565 323 VVVIGPGLGQQEWGKKAL-QKVENFRKPMLWDADALNLLAinPDKR------HNRVITPHPGEAARLLGCSVAEIEsdRL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 394 DLLRAFTQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPLHAARLAVLAHGHAGD 473
Cdd:PRK10565 396 LSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLG-QKLSPYDAACAGCVAHGAAAD 474
|
490 500
....*....|....*....|
gi 996009940 474 LAAAETGEAGLIAGDLVAHI 493
Cdd:PRK10565 475 VLAARFGTRGMLATDLFSTL 494
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
233-497 |
2.69e-58 |
|
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: 194.14 E-value: 2.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 233 ALPRRGKFGYKNTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCLTDAQ-ADFISGLP 311
Cdd:TIGR00196 11 TLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMWkVDEDEELL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 312 DLgpYQAVGIGPGLGQEAATRAVLEQLLRTAKvPLIIDADALNllgaHRELLDLLPENTVLTPHIGEFTRLTEKARDDYH 391
Cdd:TIGR00196 91 ER--YDVVVIGPGLGQDPSFKKAVEEVLELDK-PVVLDADALN----LLTYNQKREGEVILTPHPGEFKRLLGVNEIQGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 392 RLDLLRAFTQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPLHAARLAVLAHGHA 471
Cdd:TIGR00196 164 RLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLA-QNLDPFDAACNAAFAHGLA 242
|
250 260
....*....|....*....|....*.
gi 996009940 472 GDLAAAETGEAGLIAGDLVAHIGPAL 497
Cdd:TIGR00196 243 GDLALKNHGAYGLTALDLIEKIPRVC 268
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
249-480 |
2.14e-48 |
|
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: 167.16 E-value: 2.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 249 ALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCltDAQADFISGLPDLGPYQAVGIGPGLGQE 328
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMV--HPLPETSSILEKLSRYDAVVIGPGLGRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 329 AATRAVLEQLLrTAKVPLIIDADALNLLGAHRELLDLlPENTVLTPHIGEFTRLTE---KARDDyhRLDLLRAFTQKYRC 405
Cdd:pfam01256 79 EKGKAALEEVL-AKDCPLVIDADALNLLAINNEKPAR-EGPTVLTPHPGEFERLCGlagILGDD--RLEAARELAQKLNG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 996009940 406 VVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPLHAARLAVLAHGHAGDLAAAETG 480
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLA-QNEDPYDAAIAAAWLHGAASDLAAENHG 228
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
26-190 |
7.07e-33 |
|
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: 122.72 E-value: 7.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 26 ELMERAAGALAGWLTQRYTHARAgEILVLCGPGNNGGDGLALARLLHAAGYAVHVALL--PAAQHSADWQHNRQHLPSGV 103
Cdd:pfam03853 3 VLMENAGRAAARVLKALLSPAGP-KVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLgpEEKLSEDARRQLDLFKKLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 104 PVAEL--ATNALPAIAPGALVIDALFGTGLARPLGGLEATVVAHLTQAKACVVAVDLPSGLLADGPQPDPGApvVRADYT 181
Cdd:pfam03853 82 KIVTDnpDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTA--VRADHT 159
|
....*....
gi 996009940 182 LSFGLPKLA 190
Cdd:pfam03853 160 VTFGAPKPG 168
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
2-211 |
2.13e-31 |
|
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: 120.21 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 2 KILTAAQTRQLDQATMQAQGITSVELMERAAGALAGWLTQRYTHAraGEILVLCGPGNNGGDGLALARLLHAAGYAVHVa 81
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLA--GHVIIFCGPGNNGGDGFVVARHLKGFGVEVFL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 82 LLPAAQHSADWQHNRQHLPSGVPVAELATNALPAIAPGALVIDALFGTGLARPLGGLEATVVAHLTQAKACVVAVDLPSG 161
Cdd:TIGR00197 78 LKKEKRIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 996009940 162 LLAD-GPQPDpgaPVVRADYTLSFGLPKLAfLLPQNAEYVGEWHVLDIGLD 211
Cdd:TIGR00197 158 LDVDtGAIEG---PAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIP 204
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
1-201 |
1.10e-11 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 64.90 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 1 MKILTAAQTRQLDQATMQAQGITSVELMERAAGALA----------GWLTQRYTHARageILVLCGPGNNGGDGLALARL 70
Cdd:PLN03050 6 TGYLNAQDAAALDEELMSTPGFSLEQLMELAGLSVAeavyevadgeKASNPPGRHPR---VLLVCGPGNNGGDGLVAARH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 71 LHAAGYAVHVaLLPAaqhsadwQHNRQHLPS--------GVPVAEL----ATNALPAIAPGALVIDALFGTGLARPLGGL 138
Cdd:PLN03050 83 LAHFGYEVTV-CYPK-------QSSKPHYENlvtqcedlGIPFVQAiggtNDSSKPLETTYDVIVDAIFGFSFHGAPRAP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 996009940 139 EATVVAHLTQAKA---CVVAVDLPSGLLADGpqPDPGAPVVRADYTLSFGLPKLAFLLPQNAEYVG 201
Cdd:PLN03050 155 FDTLLAQMVQQQKsppPIVSVDVPSGWDVDE--GDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
221-500 |
6.21e-104 |
|
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: 312.06 E-value: 6.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 221 PWHFTQLRDAEVALPRRGKFGYKNTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCLT 300
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 301 DAQADFIsgLPDLGPYQAVGIGPGLGQEAATRAVLEQLLRTAKVPLIIDADALNLLGAHRELLDLLPENTVLTPHIGEFT 380
Cdd:COG0063 81 LPEEDEL--LELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 381 RLTEKARDD--YHRLDLLRAFTQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPL 458
Cdd:COG0063 159 RLLGCSVAEiqADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLA-QGLDPF 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 996009940 459 HAARLAVLAHGHAGDLAAAEtGEAGLIAGDLVAHIGPALQAL 500
Cdd:COG0063 238 EAAAAGVYLHGLAGDLAAEE-RGRGLLASDLIEALPAALREL 278
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
1-500 |
2.76e-90 |
|
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: 284.84 E-value: 2.76e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 1 MKILTAAQTRQLDQATMQAQGITSVELMERAAGALAGWLTQRYTHaRAGEILVLCGPGNNGGDGLALARLLHAAGYAVHV 80
Cdd:COG0062 1 MKLLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPS-AARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 81 ALL-PAAQHSADWQHNRQHLPS-GVPVAELaTNALPAIAPGALVIDALFGTGLARPLGGLEATVVAHLTQAKACVVAVDL 158
Cdd:COG0062 80 FLLgDPEKLSGDAAANLERLKAaGIPILEL-DDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 159 PSGLLADGPQPDPGApvVRADYTLSFGLPKLAFLLPQNAEYVGEWHVLDIGLDQDFIDQADTPWHFTQLRDAEVALPRRG 238
Cdd:COG0062 159 PSGLDADTGEVLGAA--VRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 239 KFGYKnTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCLTDAQADFISGLPDLGPYQA 318
Cdd:COG0062 237 SHHKG-GGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 319 VGIGPGLGQEAATRAVLEQLLRTAKVPLIIDADALNLLGAHRELLDLLPENTVLTPHIGEFTRLTEKARDDYHRLDLLRA 398
Cdd:COG0062 316 GGGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 399 FTQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRADQRLGPLHAARLAVLAHGHAGDLAAAE 478
Cdd:COG0062 396 AAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALA 475
|
490 500
....*....|....*....|..
gi 996009940 479 TGEAGLIAGDLVAHIGPALQAL 500
Cdd:COG0062 476 AALLAAAAALIALLLAAALLLL 497
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
242-493 |
4.99e-72 |
|
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: 229.04 E-value: 4.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 242 YKNTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCLTDAQADFISGLPDLGPYQAVGI 321
Cdd:cd01171 4 HKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLERADAVVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 322 GPGLGQEAATRAVLEQLLRTaKVPLIIDADALNLLGAHRELLdLLPENTVLTPHIGEFTRLT--EKARDDYHRLDLLRAF 399
Cdd:cd01171 84 GPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPSLI-KRYGPVVLTPHPGEFARLLgaLVEEIQADRLAAAREA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 400 TQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPLHAARLAVLAHGHAGDLAAAET 479
Cdd:cd01171 162 AAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLA-QGLSPLEAAALAVYLHGLAGDLAAKKK 240
|
250
....*....|....
gi 996009940 480 GeAGLIAGDLVAHI 493
Cdd:cd01171 241 G-AGLTAADLVAEI 253
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
10-493 |
1.00e-61 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 209.92 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 10 RQLDQATMQAQGITSVELMERAAGALAGWLTQRYTHARagEILVLCGPGNNGGDGLALARLLHAAGYAVHVALLP----- 84
Cdd:PRK10565 24 RRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDAR--HWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQEsdkpl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 85 ---AAQHSADWqhnrqhLPSGvpvAELATNALPAIAPGALVIDALFGTGLARPLGGLEATVVAHLTQAKACVVAVDLPSG 161
Cdd:PRK10565 102 peeAALAREAW------LNAG---GEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 162 LLADGPQPdPGApVVRADYTLSFGLPKLAFLLPQNAEYVGEWHVLDIGLdQDFIDQADTPwhFTQLRDAEVA--LPRRGK 239
Cdd:PRK10565 173 LLAETGAT-PGA-VINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGL-DSWLAGQEAP--IQRFDAEQLSqwLKPRRP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 240 FGYKNTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMC--LTDAQADfisglPDLGPYQ 317
Cdd:PRK10565 248 TSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVheLTPDSLE-----ESLEWAD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 318 AVGIGPGLGQEAATRAVLeQLLRTAKVPLIIDADALNLLG--AHRElldllpENTVLTPHIGEFTRLTEKARDDYH--RL 393
Cdd:PRK10565 323 VVVIGPGLGQQEWGKKAL-QKVENFRKPMLWDADALNLLAinPDKR------HNRVITPHPGEAARLLGCSVAEIEsdRL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 394 DLLRAFTQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPLHAARLAVLAHGHAGD 473
Cdd:PRK10565 396 LSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLG-QKLSPYDAACAGCVAHGAAAD 474
|
490 500
....*....|....*....|
gi 996009940 474 LAAAETGEAGLIAGDLVAHI 493
Cdd:PRK10565 475 VLAARFGTRGMLATDLFSTL 494
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
233-497 |
2.69e-58 |
|
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: 194.14 E-value: 2.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 233 ALPRRGKFGYKNTFGHALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCLTDAQ-ADFISGLP 311
Cdd:TIGR00196 11 TLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMWkVDEDEELL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 312 DLgpYQAVGIGPGLGQEAATRAVLEQLLRTAKvPLIIDADALNllgaHRELLDLLPENTVLTPHIGEFTRLTEKARDDYH 391
Cdd:TIGR00196 91 ER--YDVVVIGPGLGQDPSFKKAVEEVLELDK-PVVLDADALN----LLTYNQKREGEVILTPHPGEFKRLLGVNEIQGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 392 RLDLLRAFTQKYRCVVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPLHAARLAVLAHGHA 471
Cdd:TIGR00196 164 RLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLA-QNLDPFDAACNAAFAHGLA 242
|
250 260
....*....|....*....|....*.
gi 996009940 472 GDLAAAETGEAGLIAGDLVAHIGPAL 497
Cdd:TIGR00196 243 GDLALKNHGAYGLTALDLIEKIPRVC 268
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
249-480 |
2.14e-48 |
|
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: 167.16 E-value: 2.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 249 ALLLAGSRGKMGAAVLSAGACLRGGVGLLTAHLPGGGYDIFQTTRPEAMCltDAQADFISGLPDLGPYQAVGIGPGLGQE 328
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMV--HPLPETSSILEKLSRYDAVVIGPGLGRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 329 AATRAVLEQLLrTAKVPLIIDADALNLLGAHRELLDLlPENTVLTPHIGEFTRLTE---KARDDyhRLDLLRAFTQKYRC 405
Cdd:pfam01256 79 EKGKAALEEVL-AKDCPLVIDADALNLLAINNEKPAR-EGPTVLTPHPGEFERLCGlagILGDD--RLEAARELAQKLNG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 996009940 406 VVVLKGAYTAVGAPDGQVYLNSTGNPGMGTGGSGDVLTGLVLALRAdQRLGPLHAARLAVLAHGHAGDLAAAETG 480
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLA-QNEDPYDAAIAAAWLHGAASDLAAENHG 228
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
26-190 |
7.07e-33 |
|
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: 122.72 E-value: 7.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 26 ELMERAAGALAGWLTQRYTHARAgEILVLCGPGNNGGDGLALARLLHAAGYAVHVALL--PAAQHSADWQHNRQHLPSGV 103
Cdd:pfam03853 3 VLMENAGRAAARVLKALLSPAGP-KVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLgpEEKLSEDARRQLDLFKKLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 104 PVAEL--ATNALPAIAPGALVIDALFGTGLARPLGGLEATVVAHLTQAKACVVAVDLPSGLLADGPQPDPGApvVRADYT 181
Cdd:pfam03853 82 KIVTDnpDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTA--VRADHT 159
|
....*....
gi 996009940 182 LSFGLPKLA 190
Cdd:pfam03853 160 VTFGAPKPG 168
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
2-211 |
2.13e-31 |
|
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: 120.21 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 2 KILTAAQTRQLDQATMQAQGITSVELMERAAGALAGWLTQRYTHAraGEILVLCGPGNNGGDGLALARLLHAAGYAVHVa 81
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLA--GHVIIFCGPGNNGGDGFVVARHLKGFGVEVFL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 82 LLPAAQHSADWQHNRQHLPSGVPVAELATNALPAIAPGALVIDALFGTGLARPLGGLEATVVAHLTQAKACVVAVDLPSG 161
Cdd:TIGR00197 78 LKKEKRIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 996009940 162 LLAD-GPQPDpgaPVVRADYTLSFGLPKLAfLLPQNAEYVGEWHVLDIGLD 211
Cdd:TIGR00197 158 LDVDtGAIEG---PAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIP 204
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
1-201 |
1.10e-11 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 64.90 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 1 MKILTAAQTRQLDQATMQAQGITSVELMERAAGALA----------GWLTQRYTHARageILVLCGPGNNGGDGLALARL 70
Cdd:PLN03050 6 TGYLNAQDAAALDEELMSTPGFSLEQLMELAGLSVAeavyevadgeKASNPPGRHPR---VLLVCGPGNNGGDGLVAARH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 71 LHAAGYAVHVaLLPAaqhsadwQHNRQHLPS--------GVPVAEL----ATNALPAIAPGALVIDALFGTGLARPLGGL 138
Cdd:PLN03050 83 LAHFGYEVTV-CYPK-------QSSKPHYENlvtqcedlGIPFVQAiggtNDSSKPLETTYDVIVDAIFGFSFHGAPRAP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 996009940 139 EATVVAHLTQAKA---CVVAVDLPSGLLADGpqPDPGAPVVRADYTLSFGLPKLAFLLPQNAEYVG 201
Cdd:PLN03050 155 FDTLLAQMVQQQKsppPIVSVDVPSGWDVDE--GDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
4-206 |
3.74e-10 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 61.79 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 4 LTAAQTRQLDQATMQAQGITSVELMERAAGALAGWLTQRYTHARAGEILVLCGPGNNGGDGLALARLLHAAGYAVHVAlL 83
Cdd:PLN03049 15 LSQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPSEYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSIC-Y 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 84 PAAQHSADWQHNRQHLPS-GVPVaeLATNALPAIAPGA--LVIDALFG---TGLARPLGGleaTVVAHLTQAKAC--VVA 155
Cdd:PLN03049 94 PKRTDKPLYNGLVTQLESlSVPF--LSVEDLPSDLSSQfdIVVDAMFGfsfHGAPRPPFD---DLIQKLVRAAGPppIVS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 996009940 156 VDLPSGLlaDGPQPDPGAPVVRADYTLSFGLPKLAfllpqNAEYVGEWHVL 206
Cdd:PLN03049 169 VDIPSGW--HVEEGDVNGEGLKPDMLVSLTAPKLC-----AKMFKGPHHFL 212
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
4-189 |
5.90e-09 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 58.41 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 4 LTAAQTRQLDQATMQAQGITSVELMERAAGALAGWLTQRYTHARAGEILVLCGPGNNGGDGLALARLLHAAGYAVHVAlL 83
Cdd:PLN02918 91 LTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFVC-Y 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 84 PaaqhsadwQHNRQHLPSGVpVAELATNALPAIA----PGAL------VIDALFG---TGLARPLGGLEATVVAHL---- 146
Cdd:PLN02918 170 P--------KRTAKPLYTGL-VTQLESLSVPFVSvedlPADLskdfdiIVDAMFGfsfHGAPRPPFDDLIRRLVSLqnye 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 996009940 147 -TQAKACVVAVDLPSGL-LADGPQPDPGapvVRADYTLSFGLPKL 189
Cdd:PLN02918 241 qTLKHPVIVSVDIPSGWhVEEGDHEGGG---IKPDMLVSLTAPKL 282
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
392-483 |
5.82e-07 |
|
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: 50.62 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 392 RLDLLRAFTQKYRCVVVLKGA--YTAVGApdgQVYLNSTGNPGMG--TGgSGDVLTGLVLALRADQRlGPLHAARLAVLA 467
Cdd:cd01170 141 ALELAKALARKYGAVVVVTGEvdYITDGE---RVVVVKNGHPLLTkiTG-TGCLLGAVIAAFLAVGD-DPLEAAVSAVLV 215
|
90
....*....|....*.
gi 996009940 468 HGHAGDLAAAETGEAG 483
Cdd:cd01170 216 YGIAGELAAERAKGPG 231
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
393-481 |
3.09e-04 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 42.48 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996009940 393 LDLLRAFTQKYRCVVVLKGA--YTAVGapdGQVYLNSTGNPGMGT-GGSGDVLTGLV---LALRADqrlgPLHAARLAVL 466
Cdd:PRK09355 146 VEIAKAAAKKYGTVVVVTGEvdYITDG---ERVVSVHNGHPLMTKvTGTGCLLSAVVaafAAVEKD----YLEAAAAACA 218
|
90
....*....|....*
gi 996009940 467 AHGHAGDLAAAETGE 481
Cdd:PRK09355 219 VYGIAGELAAERSEK 233
|
|
| |
