|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
14-490 |
5.36e-142 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 417.54 E-value: 5.36e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 14 RTLDAQATTLLGGDGYTLMQRAGQAAWQWLLERWPQARRIVVVCGTGNNGGDGYVLARLAHRAGRQVGVVHLPEHGPASD 93
Cdd:PRK10565 24 RRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKPLPE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 94 LAQRACTDYLAVGGAIELFPYPLAQA-DVIVDALFGIGLNRAPDDATAGLIDAINAADVPVFALDVPSGIDADHGVAFGA 172
Cdd:PRK10565 104 EAALAREAWLNAGGEIHAADIVWPESvDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 173 AVRAALTLQFIVPHLGLYTGDALEHAGEREVASLEVPVSAFDGLAPAAHgWNGDAVAAQLRPRRRNTHKGESGRVLCVGG 252
Cdd:PRK10565 184 VINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQR-FDAEQLSQWLKPRRPTSHKGDHGRLLIIGG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 253 NLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARAMQADDDIATLaEAADAVALGPGLGQDAWAQALWR 332
Cdd:PRK10565 263 DHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESL-EWADVVVIGPGLGQQEWGKKALQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 333 AALGAATAMVIDADGLNLLAANDvAARGPRILTPHPGEAGRLLGLSTRQIQRDRPAAAAALAKRYDAVVVLKGAGTVVAS 412
Cdd:PRK10565 342 KVENFRKPMLWDADALNLLAINP-DKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1548924281 413 PGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALL-HACAGDAAAHAGERGLLPTDLLPELRRLAN 490
Cdd:PRK10565 421 EPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAhGAAADVLAARFGTRGMLATDLFSTLQRIVN 499
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
219-491 |
1.56e-94 |
|
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: 287.79 E-value: 1.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 219 AAHGWNGDAVAAQLRPRRRNTHKGESGRVLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARA 298
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 299 MQADDDIATLAEAADAVALGPGLGQDAWAQALWRAALGAAT-AMVIDADGLNLLAANDV---AARGPRILTPHPGEAGRL 374
Cdd:COG0063 81 LPEEDELLELLERADAVVIGPGLGRDEETRELLRALLEAADkPLVLDADALNLLAEDPEllaALPAPTVLTPHPGEFARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 375 LGLSTRQIQRDRPAAAAALAKRYDAVVVLKGAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAA 454
Cdd:COG0063 161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1548924281 455 SLGALLHACAGDAAAHAGERGLLPTDLLPELRRLANA 491
Cdd:COG0063 241 AAGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRE 277
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
237-486 |
5.43e-79 |
|
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: 247.14 E-value: 5.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 237 RNTHKGESGRVLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARA--MQADDDIATLAEAADA 314
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPllETDIEELLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 315 VALGPGLGQDAWAQALWRAALGAATAMVIDADGLNLLAANDVAARGPR--ILTPHPGEAGRLLGLSTRQIQRDRPAAAAA 392
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYGpvVLTPHPGEFARLLGALVEEIQADRLAAARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 393 LAKRYDAVVVLKGAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALLHACAGDAAAHAG 472
Cdd:cd01171 161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240
|
250
....*....|....
gi 1548924281 473 ERGLLPTDLLPELR 486
Cdd:cd01171 241 GAGLTAADLVAEIP 254
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
223-490 |
2.90e-66 |
|
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: 214.56 E-value: 2.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 223 WNGDAVAAQLRPRRRNTHKGESGRVLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARA-MQA 301
Cdd:TIGR00196 3 FLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRlMWK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 302 DDDIATLAEAADAVALGPGLGQDAWAQALWRAALGAATAMVIDADGLNLLAANDVAaRGPRILTPHPGEAGRLLGLStrQ 381
Cdd:TIGR00196 83 VDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKR-EGEVILTPHPGEFKRLLGVN--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 382 IQRDRPAAAAALAKRYDAVVVLKGAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALL- 460
Cdd:TIGR00196 160 IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAh 239
|
250 260 270
....*....|....*....|....*....|
gi 1548924281 461 HACAGDAAAHAGERGLLPTDLLPELRRLAN 490
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCK 269
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
247-487 |
2.74e-54 |
|
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: 182.56 E-value: 2.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 247 VLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARAMQADDDIATLAEAADAVALGPGLGQDAW 326
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 327 AQALWRAALGAATAMVIDADGLNLLAANDVAA--RGPRILTPHPGEAGRLLGLSTrQIQRDRPAAAAALAKRYDAVVVLK 404
Cdd:pfam01256 81 GKAALEEVLAKDCPLVIDADALNLLAINNEKParEGPTVLTPHPGEFERLCGLAG-ILGDDRLEAARELAQKLNGTILLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 405 GAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALLHACAGDAAAHAGERGLLPTDLLPE 484
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGVYMLPTLLSKI 239
|
...
gi 1548924281 485 LRR 487
Cdd:pfam01256 240 IPR 242
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
14-490 |
5.36e-142 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 417.54 E-value: 5.36e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 14 RTLDAQATTLLGGDGYTLMQRAGQAAWQWLLERWPQARRIVVVCGTGNNGGDGYVLARLAHRAGRQVGVVHLPEHGPASD 93
Cdd:PRK10565 24 RRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKPLPE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 94 LAQRACTDYLAVGGAIELFPYPLAQA-DVIVDALFGIGLNRAPDDATAGLIDAINAADVPVFALDVPSGIDADHGVAFGA 172
Cdd:PRK10565 104 EAALAREAWLNAGGEIHAADIVWPESvDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 173 AVRAALTLQFIVPHLGLYTGDALEHAGEREVASLEVPVSAFDGLAPAAHgWNGDAVAAQLRPRRRNTHKGESGRVLCVGG 252
Cdd:PRK10565 184 VINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQR-FDAEQLSQWLKPRRPTSHKGDHGRLLIIGG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 253 NLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARAMQADDDIATLaEAADAVALGPGLGQDAWAQALWR 332
Cdd:PRK10565 263 DHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESL-EWADVVVIGPGLGQQEWGKKALQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 333 AALGAATAMVIDADGLNLLAANDvAARGPRILTPHPGEAGRLLGLSTRQIQRDRPAAAAALAKRYDAVVVLKGAGTVVAS 412
Cdd:PRK10565 342 KVENFRKPMLWDADALNLLAINP-DKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1548924281 413 PGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALL-HACAGDAAAHAGERGLLPTDLLPELRRLAN 490
Cdd:PRK10565 421 EPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAhGAAADVLAARFGTRGMLATDLFSTLQRIVN 499
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
219-491 |
1.56e-94 |
|
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: 287.79 E-value: 1.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 219 AAHGWNGDAVAAQLRPRRRNTHKGESGRVLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARA 298
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 299 MQADDDIATLAEAADAVALGPGLGQDAWAQALWRAALGAAT-AMVIDADGLNLLAANDV---AARGPRILTPHPGEAGRL 374
Cdd:COG0063 81 LPEEDELLELLERADAVVIGPGLGRDEETRELLRALLEAADkPLVLDADALNLLAEDPEllaALPAPTVLTPHPGEFARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 375 LGLSTRQIQRDRPAAAAALAKRYDAVVVLKGAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAA 454
Cdd:COG0063 161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1548924281 455 SLGALLHACAGDAAAHAGERGLLPTDLLPELRRLANA 491
Cdd:COG0063 241 AAGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRE 277
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
7-495 |
3.78e-86 |
|
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: 273.67 E-value: 3.78e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 7 LYDTAAARTLDAQATTLLGGDGYTLMQRAGQAAWQWLLERWP-QARRIVVVCGTGNNGGDGYVLARLAHRAGRQVGVVHL 85
Cdd:COG0062 3 LLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 86 PEHGPASDLAQRACTDYLAVGGAIELF---PYPLAQADVIVDALFGIGLNRAPDDATAGLIDAINAADVPVFALDVPSGI 162
Cdd:COG0062 83 GDPEKLSGDAAANLERLKAAGIPILELddeLPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 163 DADHGVAFGAAVRAALTLQFIVPHLGLYTGDALEHAGEREVASLeVPVSAFDGLAPAAHGWNGDAVAAQLRPRRRNTHKG 242
Cdd:COG0062 163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADI-GIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 243 ESGRVLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARAMQADDDIATLAEAADAVALGPGLG 322
Cdd:COG0062 242 GGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 323 QDAWAQALWRAALGAATAMVIDADGLNLLAANDVAARgPRILTPHPGEAGRLLGLSTRQIQRDRPAAAAALAKRYDAVVV 402
Cdd:COG0062 322 GGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALL-LLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 403 LKGAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALLHACAGDAAAHAGERGLLPTDLL 482
Cdd:COG0062 401 AAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLA 480
|
490
....*....|...
gi 1548924281 483 PELRRLANAGAIA 495
Cdd:COG0062 481 AAAALIALLLAAA 493
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
237-486 |
5.43e-79 |
|
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: 247.14 E-value: 5.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 237 RNTHKGESGRVLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARA--MQADDDIATLAEAADA 314
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPllETDIEELLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 315 VALGPGLGQDAWAQALWRAALGAATAMVIDADGLNLLAANDVAARGPR--ILTPHPGEAGRLLGLSTRQIQRDRPAAAAA 392
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYGpvVLTPHPGEFARLLGALVEEIQADRLAAARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 393 LAKRYDAVVVLKGAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALLHACAGDAAAHAG 472
Cdd:cd01171 161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240
|
250
....*....|....
gi 1548924281 473 ERGLLPTDLLPELR 486
Cdd:cd01171 241 GAGLTAADLVAEIP 254
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
223-490 |
2.90e-66 |
|
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: 214.56 E-value: 2.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 223 WNGDAVAAQLRPRRRNTHKGESGRVLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARA-MQA 301
Cdd:TIGR00196 3 FLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRlMWK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 302 DDDIATLAEAADAVALGPGLGQDAWAQALWRAALGAATAMVIDADGLNLLAANDVAaRGPRILTPHPGEAGRLLGLStrQ 381
Cdd:TIGR00196 83 VDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKR-EGEVILTPHPGEFKRLLGVN--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 382 IQRDRPAAAAALAKRYDAVVVLKGAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALL- 460
Cdd:TIGR00196 160 IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAh 239
|
250 260 270
....*....|....*....|....*....|
gi 1548924281 461 HACAGDAAAHAGERGLLPTDLLPELRRLAN 490
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCK 269
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
247-487 |
2.74e-54 |
|
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: 182.56 E-value: 2.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 247 VLCVGGNLGSGGAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARAMQADDDIATLAEAADAVALGPGLGQDAW 326
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 327 AQALWRAALGAATAMVIDADGLNLLAANDVAA--RGPRILTPHPGEAGRLLGLSTrQIQRDRPAAAAALAKRYDAVVVLK 404
Cdd:pfam01256 81 GKAALEEVLAKDCPLVIDADALNLLAINNEKParEGPTVLTPHPGEFERLCGLAG-ILGDDRLEAARELAQKLNGTILLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 405 GAGTVVASPGHLPRIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALLHACAGDAAAHAGERGLLPTDLLPE 484
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGVYMLPTLLSKI 239
|
...
gi 1548924281 485 LRR 487
Cdd:pfam01256 240 IPR 242
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
31-188 |
2.64e-40 |
|
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: 142.75 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 31 LMQRAGQAAWQWLLERW-PQARRIVVVCGTGNNGGDGYVLARLAHRAGRQVGVVHLPEHGPASDLAQRACTDYLAVGGAI 109
Cdd:pfam03853 4 LMENAGRAAARVLKALLsPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 110 ------ELFPYPLAQADVIVDALFGIGLNRAPDDATAGLIDAINAADVPVFALDVPSGIDADHGVAFGAAVRAALTLQFI 183
Cdd:pfam03853 84 vtdnpdEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFG 163
|
....*
gi 1548924281 184 VPHLG 188
Cdd:pfam03853 164 APKPG 168
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
10-209 |
1.84e-39 |
|
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: 141.78 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 10 TAAARTLDAQATTLLGGDGYTLMQRAGQAAWQWLLERWPQARRIVVVCGTGNNGGDGYVLARLAHRAGRQVGVVHLPEHG 89
Cdd:TIGR00197 5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 90 PASDLAQRACTDYLAVGGAIELFPYP-LAQADVIVDALFGIGLNRAPDDATAGLIDAINAADVPVFALDVPSGIDADHGV 168
Cdd:TIGR00197 85 ECTEQAEVNLKALKVGGISIDEGNLVkPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTGA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1548924281 169 AFGAAVRAALTLQFIVPHLGLYTGDAlEHAGEREVASLEVP 209
Cdd:TIGR00197 165 IEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIP 204
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
5-188 |
4.26e-18 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 83.77 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 5 LALYDTAAARTLDAQattLLGGDGYT---LMQRAG----QAAWQWLLERWPQA-----RRIVVVCGTGNNGGDGYVLAR- 71
Cdd:PLN03050 6 TGYLNAQDAAALDEE---LMSTPGFSleqLMELAGlsvaEAVYEVADGEKASNppgrhPRVLLVCGPGNNGGDGLVAARh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 72 LAHrAGRQVGVVHLPEHG-PASDLAQRACTD----YLAVGGAIELFPYPLAQA-DVIVDALFGI---GLNRAPDDATAGL 142
Cdd:PLN03050 83 LAH-FGYEVTVCYPKQSSkPHYENLVTQCEDlgipFVQAIGGTNDSSKPLETTyDVIVDAIFGFsfhGAPRAPFDTLLAQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1548924281 143 IDAINAADVPVFALDVPSGIDADHGVAFGAAVRAALTLQFIVPHLG 188
Cdd:PLN03050 162 MVQQQKSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLS 207
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
22-187 |
1.73e-13 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 72.19 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 22 TLLGGDGYT---LMQRAGQAAWQWLLERWP--QARRIVVVCGTGNNGGDGYVLARLAHRAGRQVGVVHlPEHGPASdLAQ 96
Cdd:PLN03049 26 HLMGPLGFSvdqLMELAGLSVASAIAEVYSpsEYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSICY-PKRTDKP-LYN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 97 RACTDYLAVGG---AIELFPYPLA-QADVIVDALFGI---GLNRAP-DDATAGLIDAINAAdvPVFALDVPSGIDADHGV 168
Cdd:PLN03049 104 GLVTQLESLSVpflSVEDLPSDLSsQFDIVVDAMFGFsfhGAPRPPfDDLIQKLVRAAGPP--PIVSVDIPSGWHVEEGD 181
|
170
....*....|....*....
gi 1548924281 169 AFGAAVRAALTLQFIVPHL 187
Cdd:PLN03049 182 VNGEGLKPDMLVSLTAPKL 200
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
22-187 |
7.64e-10 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 61.11 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 22 TLLGGDGYT---LMQRAGQAAWQWLLERWP--QARRIVVVCGTGNNGGDGYVLARLAHRAGRQVGVVHlPEHGPASdLAQ 96
Cdd:PLN02918 102 TLMGPLGFSvdqLMELAGLSVAASIAEVYKpgEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFVCY-PKRTAKP-LYT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 97 RACT--DYLAVGG-AIELFPYPLAQA-DVIVDALFGIGLNRAPDDATAGLIDAI-------NAADVPVF-ALDVPSGIDA 164
Cdd:PLN02918 180 GLVTqlESLSVPFvSVEDLPADLSKDfDIIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeQTLKHPVIvSVDIPSGWHV 259
|
170 180
....*....|....*....|...
gi 1548924281 165 DHGVAFGAAVRAALTLQFIVPHL 187
Cdd:PLN02918 260 EEGDHEGGGIKPDMLVSLTAPKL 282
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
109-495 |
1.32e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 44.86 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 109 IELFPYPLAQADVIVDALFGIGLNRAPDDATAGLIDAINAADVPVFALDVPSGI-----------DADHGVAFGAAVRAA 177
Cdd:COG3321 861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAaaaalalaaaaLAALLALVALAAAAA 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 178 LTLQFIVPHLGLYTGDALEHAGEREVASLEVPVSAFDGLAPAAHGWNGDAVAAQLRPRRRNTHKGESGRVLCVGGNLGSG 257
Cdd:COG3321 941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 258 GAIMLTAEAALRSGAGLVQVATRAEHVTPLLARCPEAMARAMQADDDIATLAEAADAVALGPGLGQDAWAQALWRAALGA 337
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548924281 338 ATAMVIDADGLNLLAANDVAARGPRILTPHPGEAGRLLGLSTRQIQRDRPAAAAALAKRYDAVVVLKGAGTVVASPGHLP 417
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALA 1180
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1548924281 418 RIIDAGNPGMAVGGMGDLLTGVIAALLAQGFSPFDAASLGALLHACAGDAAAHAGERGLLPTDLLPELRRLANAGAIA 495
Cdd:COG3321 1181 LAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAA 1258
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
395-460 |
1.79e-04 |
|
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: 42.91 E-value: 1.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1548924281 395 KRYDAVVVLKGAGTVVASPGHLpRIIDAGNPGMA-VGGMGDLLTGVIAALLAQGFSPFDAAsLGALL 460
Cdd:cd01170 150 RKYGAVVVVTGEVDYITDGERV-VVVKNGHPLLTkITGTGCLLGAVIAAFLAVGDDPLEAA-VSAVL 214
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
395-454 |
1.98e-03 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 40.17 E-value: 1.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1548924281 395 KRYDAVVVLKGAGTVVASpGHLPRIIDAGNPGMA-VGGMGDLLTGVIAALLAQGFSPFDAA 454
Cdd:PRK09355 154 KKYGTVVVVTGEVDYITD-GERVVSVHNGHPLMTkVTGTGCLLSAVVAAFAAVEKDYLEAA 213
|
|
|