|
Name |
Accession |
Description |
Interval |
E-value |
| Indigoidine_A |
pfam04227 |
Indigoidine synthase A like protein; Indigoidine is a blue pigment synthesized by Erwinia ... |
33-322 |
0e+00 |
|
Indigoidine synthase A like protein; Indigoidine is a blue pigment synthesized by Erwinia chrysanthemi implicated in pathogenicity and protection from oxidative stress. IdgA is involved in indigoidine biosynthesis, but its specific function is unknown. The recommended name for this protein is now pseudouridine-5'-phosphate glycosidase.
Pssm-ID: 461231 Cd Length: 289 Bit Score: 527.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 33 VKEALAHHRPVVALESTIITHGMPYPHNLSTAKEVEAIVRAEGSIPATIGILEGRIHVGLSSDELDFLAQSKTAlKVSRR 112
Cdd:pfam04227 2 VAEALAAGKPVVALESTIITHGLPYPQNLETALEVEAIVRENGAVPATIAILDGRPKVGLTDEELERLADAGGA-KVSRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 113 DLPYVISKGLSGGTTVSGTMIAANKAGIPVFVTGGIGGVHRDGENSLDVSADLTELGRTPIAVVSAGVKSILDIGRTLEY 192
Cdd:pfam04227 81 DLAYVLALGLDGGTTVAATMILAHLAGIRVFATGGIGGVHRGAEETMDISADLTELGRTPVAVVCAGVKSILDIPRTLEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 193 LETQGVCVATYGdSKSFPAFFSRQSGFTSPYNISSPQEAADLIASTFSLGLKSGLLLAVPIPEEHAATGQQIEDAIQTAV 272
Cdd:pfam04227 161 LETQGVPVVGYG-TDEFPAFYTRDSGFKSPYRVDSPEEAAAIIRAQWALGLGSGVLVANPIPEEHALDREEIDAAIEQAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 688616936 273 TEASSKGVTGRDVTPFILQRVSELTKGKSLQANIALIRNNARVGSQIAHA 322
Cdd:pfam04227 240 AEAEEQGITGKAVTPFLLARIAELTGGKSLEANIALVKNNARLAAQIAVA 289
|
|
| PsuG |
COG2313 |
Pseudouridine-5'-phosphate glycosidase (pseudoU degradation) [Nucleotide transport and ... |
25-327 |
6.17e-169 |
|
Pseudouridine-5'-phosphate glycosidase (pseudoU degradation) [Nucleotide transport and metabolism];
Pssm-ID: 441887 Cd Length: 303 Bit Score: 485.76 E-value: 6.17e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 25 SLFTIHPDVKEALAHHRPVVALESTIITHGMPYPHNLSTAKEVEAIVRAEGSIPATIGILEGRIHVGLSSDELDFLAQSK 104
Cdd:COG2313 2 KYLRISPEVAAALAAGRPVVALESTIISHGMPYPQNLETAREVEAIVREAGAVPATIAVLDGKIKVGLSDEELERLAQAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 105 TALKVSRRDLPYVISKGLSGGTTVSGTMIAANKAGIPVFVTGGIGGVHRDGENSLDVSADLTELGRTPIAVVSAGVKSIL 184
Cdd:COG2313 82 DVAKVSRRDLPVALARGRSGATTVAATMILAALAGIRVFATGGIGGVHRGAEETFDISADLQELARTPVAVVCAGAKSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 185 DIGRTLEYLETQGVCVATYGdSKSFPAFFSRQSGFTSPYNISSPQEAADLIASTFSLGLKSGLLLAVPIPEEHAATGQQI 264
Cdd:COG2313 162 DLPLTLEYLETLGVPVIGYG-TDEFPAFYSRSSGLPVPYRVDSPEEIAAILRAKWALGLPGGVLVANPIPEEDALDAEEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688616936 265 EDAIQTAVTEASSKGVTGRDVTPFILQRVSELTKGKSLQANIALIRNNARVGSQIAHALSKLN 327
Cdd:COG2313 241 DAAIAEALAEAEAQGIRGKAVTPFLLARIAELTGGRSLEANIALVKNNARLAAEIAVALAALA 303
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
351-667 |
1.05e-80 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 258.40 E-value: 1.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 351 KTIVIGGINVDFIAKgTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYC-KHMDTSA 429
Cdd:cd01941 1 EIVVIGAANIDLRGK-VSGSLVPGTSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESeKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 430 VARLQDQRTATYCAVITESGELSLGLGDMDIHQQIQEQYVSQFVDQLSSASLIVLDGNIPVSTINYVCRIAKKHAVPVWF 509
Cdd:cd01941 80 GIVFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 510 EPTDADKACKPFlsESWKALAFTSPNLTELCTMNHTLGLPTPAElprsledvlgcAPALSRPLLEHLHCVLVTLGSLGVL 589
Cdd:cd01941 160 EPTSAPKLKKLF--YLLHAIDLLTPNRAELEALAGALIENNEDE-----------NKAAKILLLPGIKNVIVTLGAKGVL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688616936 590 VCGEHEAGtvnlqprkqkrarlCAVHYPALTVssEETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAARRSLLT 667
Cdd:cd01941 227 LSSREGGV--------------ETKLFPAPQP--ETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
351-680 |
3.33e-36 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 138.09 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 351 KTIVIGGINVDFIAKGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCK--HMDTS 428
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRaeGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 429 AVARLQDQRTATYCAVITESGELSLgLGDMDIHQQIQEQYVSQfvDQLSSASLIVLDG-----NIPVSTINYVCRIAKKH 503
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTI-VFYRGANAELTPEDLDE--ALLAGADILHLGGitlasEPPREALLAALEAARAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 504 AVPVWFEPTDADKACKPFLSESWKALAFTS---PNLTELCTMnhtLGLPTPAELPRSLEDvLGCApalsrpllehlhCVL 580
Cdd:COG0524 158 GVPVSLDPNYRPALWEPARELLRELLALVDilfPNEEEAELL---TGETDPEEAAAALLA-RGVK------------LVV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 581 VTLGSLGVLVCGEHEagtvnlqprkqkrarlcAVHYPALTVsseETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLA 660
Cdd:COG0524 222 VTLGAEGALLYTGGE-----------------VVHVPAFPV---EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAA 281
|
330 340
....*....|....*....|
gi 688616936 661 ARRSLLTPHPIDPSLTADAI 680
Cdd:COG0524 282 AALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
354-661 |
1.34e-30 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 122.07 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 354 VIGGINVDFIakGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCK--HMDTSAVA 431
Cdd:pfam00294 4 VIGEANIDLI--GNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKkeGVDTDYVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 432 RLQDQRTATYCAVITESGELSLGLGDMDIHQQIQEQYVSQfVDQLSSASLIVLDG----NIPVSTINYVCRIAKKH--AV 505
Cdd:pfam00294 82 IDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEEN-EDLLENADLLYISGslplGLPEATLEELIEAAKNGgtFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 506 PVWFEPTDADKACkpfLSESWKALAFTSPNLTELCTM-NHTLGlptpaelprSLEDVLGCAPALSRPLLEHlhcVLVTLG 584
Cdd:pfam00294 161 PNLLDPLGAAREA---LLELLPLADLLKPNEEELEALtGAKLD---------DIEEALAALHKLLAKGIKT---VIVTLG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688616936 585 SLGVLVCGEHEagtvnlqprkqkrarlcavHYPALTVSSEETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAA 661
Cdd:pfam00294 226 ADGALVVEGDG-------------------EVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAA 283
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
353-644 |
9.76e-20 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 90.82 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 353 IVIGGINVDfIAKGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCK----HMDTS 428
Cdd:PRK09850 8 VIIGSANID-VAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNqsgvYVDKC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 429 AVarLQDQRTATYCAVITESGELSLGLGDMDIHQQIQEQYVSQFVDQLSSASLIVLDGNIPVSTINYVCRIAKKhaVPVW 508
Cdd:PRK09850 87 LI--VPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAAN--VPVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 509 FEPTDADKACKpfLSESWKALAFTSPNLTELCTMNhtlGLPTPAElprslEDVLGCAPALSrpllEH-LHCVLVTLGSLG 587
Cdd:PRK09850 163 VDPVSAWKCVK--VRDRLNQIHTLKPNRLEAETLS---GIALSGR-----EDVAKVAAWFH----QHgLNRLVLSMGGDG 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 688616936 588 VLVcgEHEAGTVNLQPrkqkrarlcavhyPALTvsseETVNVSGAGDsfagAMMVGI 644
Cdd:PRK09850 229 VYY--SDISGESGWSA-------------PIKT----NVINVTGAGD----AMMAGL 262
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
386-657 |
4.54e-08 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 55.30 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 386 GGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKH--MDTSAVARLQDQRTAtycAVITE---SGELSL-----GL 455
Cdd:TIGR04382 34 GGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRRegVDTSHVVTDPGRRTS---LVFLEikpPDEFPLlfyreNA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 456 GDMDIH-QQIQEQYVSQfvdqlssASLIVLDGNI----PV-STINYVCRIAKKHAVPVWFeptDADkackpFLSESWKAL 529
Cdd:TIGR04382 111 ADLALTpDDVDEDYIAS-------ARALLVSGTAlsqePSrEAVLKALEYARAAGVRVVL---DID-----YRPYLWKSP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 530 AFTSPNLTELC--------TMNHTLGLPTPAELPRSLEDVLGCAPALsrpllehlhcVLVTLGSLGVLVCGEHEAGtvnl 601
Cdd:TIGR04382 176 EEAGIYLRLVLplvdviigTREEFDIAGGEGDDEAAARALLDAGVEI----------LVVKRGPEGSLVYTGDGEG---- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 688616936 602 qprkqkrarlcaVHYPALTVsseETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMG 657
Cdd:TIGR04382 242 ------------VEVPGFPV---EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYG 282
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Indigoidine_A |
pfam04227 |
Indigoidine synthase A like protein; Indigoidine is a blue pigment synthesized by Erwinia ... |
33-322 |
0e+00 |
|
Indigoidine synthase A like protein; Indigoidine is a blue pigment synthesized by Erwinia chrysanthemi implicated in pathogenicity and protection from oxidative stress. IdgA is involved in indigoidine biosynthesis, but its specific function is unknown. The recommended name for this protein is now pseudouridine-5'-phosphate glycosidase.
Pssm-ID: 461231 Cd Length: 289 Bit Score: 527.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 33 VKEALAHHRPVVALESTIITHGMPYPHNLSTAKEVEAIVRAEGSIPATIGILEGRIHVGLSSDELDFLAQSKTAlKVSRR 112
Cdd:pfam04227 2 VAEALAAGKPVVALESTIITHGLPYPQNLETALEVEAIVRENGAVPATIAILDGRPKVGLTDEELERLADAGGA-KVSRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 113 DLPYVISKGLSGGTTVSGTMIAANKAGIPVFVTGGIGGVHRDGENSLDVSADLTELGRTPIAVVSAGVKSILDIGRTLEY 192
Cdd:pfam04227 81 DLAYVLALGLDGGTTVAATMILAHLAGIRVFATGGIGGVHRGAEETMDISADLTELGRTPVAVVCAGVKSILDIPRTLEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 193 LETQGVCVATYGdSKSFPAFFSRQSGFTSPYNISSPQEAADLIASTFSLGLKSGLLLAVPIPEEHAATGQQIEDAIQTAV 272
Cdd:pfam04227 161 LETQGVPVVGYG-TDEFPAFYTRDSGFKSPYRVDSPEEAAAIIRAQWALGLGSGVLVANPIPEEHALDREEIDAAIEQAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 688616936 273 TEASSKGVTGRDVTPFILQRVSELTKGKSLQANIALIRNNARVGSQIAHA 322
Cdd:pfam04227 240 AEAEEQGITGKAVTPFLLARIAELTGGKSLEANIALVKNNARLAAQIAVA 289
|
|
| PsuG |
COG2313 |
Pseudouridine-5'-phosphate glycosidase (pseudoU degradation) [Nucleotide transport and ... |
25-327 |
6.17e-169 |
|
Pseudouridine-5'-phosphate glycosidase (pseudoU degradation) [Nucleotide transport and metabolism];
Pssm-ID: 441887 Cd Length: 303 Bit Score: 485.76 E-value: 6.17e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 25 SLFTIHPDVKEALAHHRPVVALESTIITHGMPYPHNLSTAKEVEAIVRAEGSIPATIGILEGRIHVGLSSDELDFLAQSK 104
Cdd:COG2313 2 KYLRISPEVAAALAAGRPVVALESTIISHGMPYPQNLETAREVEAIVREAGAVPATIAVLDGKIKVGLSDEELERLAQAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 105 TALKVSRRDLPYVISKGLSGGTTVSGTMIAANKAGIPVFVTGGIGGVHRDGENSLDVSADLTELGRTPIAVVSAGVKSIL 184
Cdd:COG2313 82 DVAKVSRRDLPVALARGRSGATTVAATMILAALAGIRVFATGGIGGVHRGAEETFDISADLQELARTPVAVVCAGAKSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 185 DIGRTLEYLETQGVCVATYGdSKSFPAFFSRQSGFTSPYNISSPQEAADLIASTFSLGLKSGLLLAVPIPEEHAATGQQI 264
Cdd:COG2313 162 DLPLTLEYLETLGVPVIGYG-TDEFPAFYSRSSGLPVPYRVDSPEEIAAILRAKWALGLPGGVLVANPIPEEDALDAEEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688616936 265 EDAIQTAVTEASSKGVTGRDVTPFILQRVSELTKGKSLQANIALIRNNARVGSQIAHALSKLN 327
Cdd:COG2313 241 DAAIAEALAEAEAQGIRGKAVTPFLLARIAELTGGRSLEANIALVKNNARLAAEIAVALAALA 303
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
351-667 |
1.05e-80 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 258.40 E-value: 1.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 351 KTIVIGGINVDFIAKgTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYC-KHMDTSA 429
Cdd:cd01941 1 EIVVIGAANIDLRGK-VSGSLVPGTSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESeKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 430 VARLQDQRTATYCAVITESGELSLGLGDMDIHQQIQEQYVSQFVDQLSSASLIVLDGNIPVSTINYVCRIAKKHAVPVWF 509
Cdd:cd01941 80 GIVFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 510 EPTDADKACKPFlsESWKALAFTSPNLTELCTMNHTLGLPTPAElprsledvlgcAPALSRPLLEHLHCVLVTLGSLGVL 589
Cdd:cd01941 160 EPTSAPKLKKLF--YLLHAIDLLTPNRAELEALAGALIENNEDE-----------NKAAKILLLPGIKNVIVTLGAKGVL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688616936 590 VCGEHEAGtvnlqprkqkrarlCAVHYPALTVssEETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAARRSLLT 667
Cdd:cd01941 227 LSSREGGV--------------ETKLFPAPQP--ETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
351-680 |
3.33e-36 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 138.09 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 351 KTIVIGGINVDFIAKGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCK--HMDTS 428
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRaeGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 429 AVARLQDQRTATYCAVITESGELSLgLGDMDIHQQIQEQYVSQfvDQLSSASLIVLDG-----NIPVSTINYVCRIAKKH 503
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTI-VFYRGANAELTPEDLDE--ALLAGADILHLGGitlasEPPREALLAALEAARAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 504 AVPVWFEPTDADKACKPFLSESWKALAFTS---PNLTELCTMnhtLGLPTPAELPRSLEDvLGCApalsrpllehlhCVL 580
Cdd:COG0524 158 GVPVSLDPNYRPALWEPARELLRELLALVDilfPNEEEAELL---TGETDPEEAAAALLA-RGVK------------LVV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 581 VTLGSLGVLVCGEHEagtvnlqprkqkrarlcAVHYPALTVsseETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLA 660
Cdd:COG0524 222 VTLGAEGALLYTGGE-----------------VVHVPAFPV---EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAA 281
|
330 340
....*....|....*....|
gi 688616936 661 ARRSLLTPHPIDPSLTADAI 680
Cdd:COG0524 282 AALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
354-661 |
1.34e-30 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 122.07 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 354 VIGGINVDFIakGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCK--HMDTSAVA 431
Cdd:pfam00294 4 VIGEANIDLI--GNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKkeGVDTDYVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 432 RLQDQRTATYCAVITESGELSLGLGDMDIHQQIQEQYVSQfVDQLSSASLIVLDG----NIPVSTINYVCRIAKKH--AV 505
Cdd:pfam00294 82 IDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEEN-EDLLENADLLYISGslplGLPEATLEELIEAAKNGgtFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 506 PVWFEPTDADKACkpfLSESWKALAFTSPNLTELCTM-NHTLGlptpaelprSLEDVLGCAPALSRPLLEHlhcVLVTLG 584
Cdd:pfam00294 161 PNLLDPLGAAREA---LLELLPLADLLKPNEEELEALtGAKLD---------DIEEALAALHKLLAKGIKT---VIVTLG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688616936 585 SLGVLVCGEHEagtvnlqprkqkrarlcavHYPALTVSSEETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAA 661
Cdd:pfam00294 226 ADGALVVEGDG-------------------EVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAA 283
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
353-661 |
2.87e-25 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 106.48 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 353 IVIGGINVDFIAkgTTKKL-LFGQTNPG-SVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCK--HMDTS 428
Cdd:cd01174 3 VVVGSINVDLVT--RVDRLpKPGETVLGsSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLReeGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 429 AVARLQDQRTATycAVIT--ESGELSLGlgdmdIH----QQIQEQYVSQFVDQLSSASLIVLDGNIPVSTINYVCRIAKK 502
Cdd:cd01174 81 YVEVVVGAPTGT--AVITvdESGENRIV-----VVpganGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 503 HAVPVWFEPTDADkackPFLSESWKALAFTSPNLTELCTMnhtLGLPTPAElprsledvlGCAPALSRPLLEH-LHCVLV 581
Cdd:cd01174 154 AGVTVILNPAPAR----PLPAELLALVDILVPNETEAALL---TGIEVTDE---------EDAEKAARLLLAKgVKNVIV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 582 TLGSLGVLVCGEHEagtvnlqprkqkrarlcAVHYPALTVsseETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAA 661
Cdd:cd01174 218 TLGAKGALLASGGE-----------------VEHVPAFKV---KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAA 277
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
353-644 |
9.76e-20 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 90.82 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 353 IVIGGINVDfIAKGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCK----HMDTS 428
Cdd:PRK09850 8 VIIGSANID-VAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNqsgvYVDKC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 429 AVarLQDQRTATYCAVITESGELSLGLGDMDIHQQIQEQYVSQFVDQLSSASLIVLDGNIPVSTINYVCRIAKKhaVPVW 508
Cdd:PRK09850 87 LI--VPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAAN--VPVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 509 FEPTDADKACKpfLSESWKALAFTSPNLTELCTMNhtlGLPTPAElprslEDVLGCAPALSrpllEH-LHCVLVTLGSLG 587
Cdd:PRK09850 163 VDPVSAWKCVK--VRDRLNQIHTLKPNRLEAETLS---GIALSGR-----EDVAKVAAWFH----QHgLNRLVLSMGGDG 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 688616936 588 VLVcgEHEAGTVNLQPrkqkrarlcavhyPALTvsseETVNVSGAGDsfagAMMVGI 644
Cdd:PRK09850 229 VYY--SDISGESGWSA-------------PIKT----NVINVTGAGD----AMMAGL 262
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
353-678 |
5.55e-17 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 83.06 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 353 IVIGGINVDFiaKGTTKkLLFGQ--TNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKH--MDTS 428
Cdd:PRK09954 61 VVVGAINMDI--RGMAD-IRYPQaaSHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRagVNVS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 429 AVARLQDQRTATYCAVITESGELSLGLGDMDIHQQIQEQYVSQFVDQLSSASLIVLDGNIPVSTINYVCRIAKKhaVPVW 508
Cdd:PRK09954 138 GCIRLHGQSTSTYLAIANRQDETVLAINDTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLADE--IPVF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 509 FEPTDADKACKpflSESWKALAFT-SPNLTELCTMnhtLGLPTpaelpRSLEDVLGCAPALSRPLLEHLhcvLVTLGSLG 587
Cdd:PRK09954 216 VDTVSEFKAGK---IKHWLAHIHTlKPTQPELEIL---WGQAI-----TSDADRNAAVNALHQQGVQQI---FVYLPDES 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 588 VLvCGEHEAGTVNLQPrkqkrarlcavhyPALTvsseeTVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAARRSLLT 667
Cdd:PRK09954 282 VF-CSEKDGEQFLLTA-------------PAHT-----TVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAISRAS 342
|
330
....*....|.
gi 688616936 668 PHPIDPSLTAD 678
Cdd:PRK09954 343 GSLNNPTLSAD 353
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
351-661 |
9.71e-17 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 81.47 E-value: 9.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 351 KTIVIGGINVDFIAKGTTKKllfgqTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKH--MDTS 428
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRL-----EQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRRegVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 429 AVARLQDQRTATYCAVITESGELSLglgDMDIHQ----QIQEQYVSQFVdqLSSASLIVLDGnIPVS-------TINYVC 497
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERRV---LYYRAGsaasRLTPEDLDEAA--LAGADHLHLSG-ITLAlsesareALLEAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 498 RIAKKHAVPVWFEP---------TDADKACKPFLSESwkALAFtsPNLTELCTMnhtLGLPTPAELPRSLEDVLGCAPAl 568
Cdd:cd01166 150 EAAKARGVTVSFDLnyrpklwsaEEAREALEELLPYV--DIVL--PSEEEAEAL---LGDEDPTDAAERALALALGVKA- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 569 srpllehlhcVLVTLGSLGVLVCGEHEAGTVnlqprkqkrarlcavhyPALTVsseETVNVSGAGDSFAGAMMVGILQGL 648
Cdd:cd01166 222 ----------VVVKLGAEGALVYTGGGRVFV-----------------PAYPV---EVVDTTGAGDAFAAGFLAGLLEGW 271
|
330
....*....|...
gi 688616936 649 HTDSCVQMGLLAA 661
Cdd:cd01166 272 DLEEALRFANAAA 284
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
351-647 |
2.78e-13 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 71.13 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 351 KTIVIGGINVDFIAKGTTKKLLFGQtNPGsvcqsfgGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKH--MDTS 428
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFTK-APG-------GAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEagVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 429 AVARLQDQRTATYCAVITESGELSL-----GLGDMDIHQQIQEQYVSQ--FVDqLSSASLIVLDGnipVSTINYVCRIAK 501
Cdd:cd01167 73 GIQFDPAAPTTLAFVTLDADGERSFefyrgPAADLLLDTELNPDLLSEadILH-FGSIALASEPS---RSALLELLEAAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 502 KHAVPVWFEP-------TDADKAcKPFLSESWKALAFTSPNLTELCTMnhtLGLPTPAELPRSLedvlgcapalsrpLLE 574
Cdd:cd01167 149 KAGVLISFDPnlrpplwRDEEEA-RERIAELLELADIVKLSDEELELL---FGEEDPEEIAALL-------------LLF 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688616936 575 HLHCVLVTLGSLGVLVC-GEHEAgtvnlqprkqkrarlcavHYPALTVsseETVNVSGAGDSFAGAMMVGILQG 647
Cdd:cd01167 212 GLKLVLVTRGADGALLYtKGGVG------------------EVPGIPV---EVVDTTGAGDAFVAGLLAQLLSR 264
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
348-640 |
2.79e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 71.31 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 348 MDSKTIVIGGINVDFIAkGTTKKLLFGQTNPG-SVCQSFGGVGRNIADCLSRLGHKPLFISAIGKD-SHSDAVLNYCKH- 424
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLIG-YVDRMPQVGETLHGtSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDgFGSDTIKNFKRNg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 425 MDTSAVARLQDqrTATYCAVITESGELSlglgdmdiHQQI------QEQYVSQFVDQLSS-----ASLIVLDGNIPVSTI 493
Cdd:PTZ00292 93 VNTSFVSRTEN--SSTGLAMIFVDTKTG--------NNEIviipgaNNALTPQMVDAQTDniqniCKYLICQNEIPLETT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 494 NYVCRIAKKHAVPVWFEPTDADKAC-----KPFLseswKALAFTSPNLTElcTMNHTLGLPTPAELPRSLEDVLGCAPAl 568
Cdd:PTZ00292 163 LDALKEAKERGCYTVFNPAPAPKLAeveiiKPFL----KYVSLFCVNEVE--AALITGMEVTDTESAFKASKELQQLGV- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688616936 569 srpllehlHCVLVTLGSLGVLVCGEHEagtvnlqprkqkrarlCAVHYPALTVsseETVNVSGAGDSFAGAM 640
Cdd:PTZ00292 236 --------ENVIITLGANGCLIVEKEN----------------EPVHVPGKRV---KAVDTTGAGDCFVGSM 280
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
353-661 |
1.29e-12 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 68.88 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 353 IVIGGINVDFIAKGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKHM--DTSAV 430
Cdd:cd01942 3 AVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEgvDTSHV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 431 ARLQDQRTATycAVITESGELS----LGLGDMDihqqiqEQYVSQFVDQLSSASLIVLDGNIPVsTINYvcRIAKKHAVP 506
Cdd:cd01942 83 RVVDEDSTGV--AFILTDGDDNqiayFYPGAMD------ELEPNDEADPDGLADIVHLSSGPGL-IELA--RELAAGGIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 507 VWFEPTDADKacKPFLSESWKALAFTS---PNLTELCTMNHTLGLPTPAelprsledvlgcapalsrpLLEHLHCVLVTL 583
Cdd:cd01942 152 VSFDPGQELP--RLSGEELEEILERADilfVNDYEAELLKERTGLSEAE-------------------LASGVRVVVVTL 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688616936 584 GSLGVLVcgeHEAGTVnlqprkqkrarlcaVHYPAltVSSEETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAA 661
Cdd:cd01942 211 GPKGAIV---FEDGEE--------------VEVPA--VPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAA 269
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
386-661 |
4.28e-11 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 64.50 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 386 GGVGrNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKH--MDTSAVaRLQDQRTATYCAVITESGELsLGLGDMDIH-- 461
Cdd:cd01172 40 GGAA-NVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKegIDTDGI-VDEGRPTTTKTRVIARNQQL-LRVDREDDSpl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 462 -QQIQEQYVSQFVDQLSSASLIVL----DGNIPVSTINYVCRIAKKHAVPVWfeptdADKACKPFlSESWKALAFTsPNL 536
Cdd:cd01172 117 sAEEEQRLIERIAERLPEADVVILsdygKGVLTPRVIEALIAAARELGIPVL-----VDPKGRDY-SKYRGATLLT-PNE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 537 TELctmNHTLGLPTPAElpRSLEDVLgcapalsRPLLEHLHC--VLVTLGSLGVLVCGEHEAgtvnlqprkqkrarlcAV 614
Cdd:cd01172 190 KEA---REALGDEINDD--DELEAAG-------EKLLELLNLeaLLVTLGEEGMTLFERDGE----------------VQ 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 688616936 615 HYPALTVsseETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAA 661
Cdd:cd01172 242 HIPALAK---EVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAA 285
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
386-661 |
9.91e-11 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 63.68 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 386 GGVGrNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKH--MDTSAVARLQDQRTATYCAVITESGELslgL-----GDM 458
Cdd:COG2870 56 GGAA-NVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEagIDTDGLVVDPRRPTTTKTRVIAGGQQL---LrldfeDRF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 459 DIHQQIQEQYVSQFVDQLSSASLIVL----DGNIPVSTINYVCRIAKKHAVPVWFEPTDADkackpfLSESWKALAFTsP 534
Cdd:COG2870 132 PLSAELEARLLAALEAALPEVDAVILsdygKGVLTPELIQALIALARAAGKPVLVDPKGRD------FSRYRGATLLT-P 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 535 NLTELCTMnhtLGLPtpaelPRSLEDVLGCAPALsrplLEHLHC--VLVTLGSLGVLVCGEHEAgtvnlqprkqkrarlc 612
Cdd:COG2870 205 NLKEAEAA---VGIP-----IADEEELVAAAAEL----LERLGLeaLLVTRGEEGMTLFDADGP---------------- 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 688616936 613 AVHYPALTVsseETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAA 661
Cdd:COG2870 257 PHHLPAQAR---EVFDVTGAGDTVIATLALALAAGASLEEAAELANLAA 302
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
350-661 |
1.94e-09 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 59.50 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 350 SKTIVIGGINVDFIakgttkkLLF------GQTNPGSVCQ-SFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYC 422
Cdd:PRK11142 3 GKLVVLGSINADHV-------LNLesfprpGETLTGRHYQvAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 423 KH--MDTSAVARLQDQRTATYCAVITESGELSLGlgdmdIH----QQIQEQYVSQFVDQLSSASLIVLDGNIPVSTINYV 496
Cdd:PRK11142 76 AKdgIDTAPVSVIKGESTGVALIFVNDEGENSIG-----IHaganAALTPALVEAHRELIANADALLMQLETPLETVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 497 CRIAKKHAVPVWFEPTDAdkacKPFLSESWKALAFTSPNLTElctmnhtlglptpAELPR--SLEDVLGCAPAlsrplLE 574
Cdd:PRK11142 151 AKIAKQHGTKVILNPAPA----RELPDELLALVDIITPNETE-------------AEKLTgiRVEDDDDAAKA-----AQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 575 HLH-----CVLVTLGSLGVLVCGEHEAGTVnlqprkqkrarlcavhyPALTVSSEETVnvsGAGDSFAGAMMVGILQGLH 649
Cdd:PRK11142 209 VLHqkgieTVLITLGSRGVWLSENGEGQRV-----------------PGFRVQAVDTI---AAGDTFNGALVTALLEGKP 268
|
330
....*....|..
gi 688616936 650 TDSCVQMGLLAA 661
Cdd:PRK11142 269 LPEAIRFAHAAA 280
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
460-668 |
7.36e-09 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 57.84 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 460 IHQQIQEQYVSQFVDQLSSASLIVLDG----NIPVSTINYVCRIAKKHAVPVWFeptDADKACkpfLSESWKALAF-TSP 534
Cdd:COG1105 110 ISEEELEALLERLEELLKEGDWVVLSGslppGVPPDFYAELIRLARARGAKVVL---DTSGEA---LKAALEAGPDlIKP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 535 NLTELCTMnhtLGLPtpaelPRSLEDVLGCApalsRPLLEH-LHCVLVTLGSLGVLVCGEHEAgtvnlqprkqkrarlCA 613
Cdd:COG1105 184 NLEELEEL---LGRP-----LETLEDIIAAA----RELLERgAENVVVSLGADGALLVTEDGV---------------YR 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 688616936 614 VHYPALTVSSeeTVnvsGAGDSFAGAMMVGILQGLHTDSCVQMGLLAARRSLLTP 668
Cdd:COG1105 237 AKPPKVEVVS--TV---GAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSP 286
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
386-673 |
2.89e-08 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 56.08 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 386 GGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCK--HMDTSAVaRLQDQRTATyCAV-ITESGELSL--------G 454
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRaaGVDTRYQ-VQPDGPTGT-CAVlVTPDAERTMctylgaanE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 455 LGDMDIHQQIqeqyvsqfvdqLSSASLIVLDG---NIPVSTINYVCRIAKKHAVPVWFEPTDadkackPFLSESWK-ALA 530
Cdd:cd01168 133 LSPDDLDWSL-----------LAKAKYLYLEGyllTVPPEAILLAAEHAKENGVKIALNLSA------PFIVQRFKeALL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 531 FTSPNLTeLCTMNHTlglpTPAELPRS-LEDVLGCAPALSrplleHLHC--VLVTLGSLGVLVCGEHEagtvnlqprkqk 607
Cdd:cd01168 196 ELLPYVD-ILFGNEE----EAEALAEAeTTDDLEAALKLL-----ALRCriVVITQGAKGAVVVEGGE------------ 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688616936 608 rarlcavHYPALTVSSEETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAARRSLLTPHPIDP 673
Cdd:cd01168 254 -------VYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
386-657 |
4.54e-08 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 55.30 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 386 GGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKH--MDTSAVARLQDQRTAtycAVITE---SGELSL-----GL 455
Cdd:TIGR04382 34 GGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRRegVDTSHVVTDPGRRTS---LVFLEikpPDEFPLlfyreNA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 456 GDMDIH-QQIQEQYVSQfvdqlssASLIVLDGNI----PV-STINYVCRIAKKHAVPVWFeptDADkackpFLSESWKAL 529
Cdd:TIGR04382 111 ADLALTpDDVDEDYIAS-------ARALLVSGTAlsqePSrEAVLKALEYARAAGVRVVL---DID-----YRPYLWKSP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 530 AFTSPNLTELC--------TMNHTLGLPTPAELPRSLEDVLGCAPALsrpllehlhcVLVTLGSLGVLVCGEHEAGtvnl 601
Cdd:TIGR04382 176 EEAGIYLRLVLplvdviigTREEFDIAGGEGDDEAAARALLDAGVEI----------LVVKRGPEGSLVYTGDGEG---- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 688616936 602 qprkqkrarlcaVHYPALTVsseETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMG 657
Cdd:TIGR04382 242 ------------VEVPGFPV---EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYG 282
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
354-645 |
6.40e-08 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 53.25 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 354 VIGGINVDFIAKGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAigkdshsDAVlnyckhmdtsavarl 433
Cdd:cd00287 4 VVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVGA-------DAV--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 434 qdqrtatycavitesgelslglgdmdihqqiqeqyvsqFVDQLSSASLIVLDgnipvstinyVCRIAKKHAVPVWFEPtd 513
Cdd:cd00287 62 --------------------------------------VISGLSPAPEAVLD----------ALEEARRRGVPVVLDP-- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 514 ADKACKPFLSESWKALAFT---SPNLTELctmnHTLglptpaeLPRSLEDVLGCAPALSRPLLEHLHCVLVTLGSLGVLV 590
Cdd:cd00287 92 GPRAVRLDGEELEKLLPGVdilTPNEEEA----EAL-------TGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIV 160
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 688616936 591 CGEHEAgtvnlqprkqkrarlcAVHYPALTVsseETVNVSGAGDSFAGAMMVGIL 645
Cdd:cd00287 161 ATRGGT----------------EVHVPAFPV---KVVDTTGAGDAFLAALAAGLA 196
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
351-452 |
1.93e-06 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 50.11 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 351 KTIVIGGINVDFIakGTTKKLLF--GQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYCKHMDTS 428
Cdd:cd01947 1 KIAVVGHVEWDIF--LSLDAPPQpgGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDK 78
|
90 100
....*....|....*....|....
gi 688616936 429 AVARLQDQRTATYCAVITESGELS 452
Cdd:cd01947 79 HTVAWRDKPTRKTLSFIDPNGERT 102
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
355-647 |
1.90e-05 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 46.90 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 355 IGGINVDFIAKGTTKKLLFGQTNPGSVCQSFGGVGRNIADCLSRLGHKPLFISAIGKDSHSDAVLNYC-KH-MDTSAVAR 432
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELaAEgVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 433 LQDQRTATycAVITESGELSLGLGDMDIHQQIQEQYVSQfvDQLSSASLIVLDGN-IPVSTInyVCRIAKKHAVPVwfeP 511
Cdd:cd01945 85 APGARSPI--SSITDITGDRATISITAIDTQAAPDSLPD--AILGGADAVLVDGRqPEAALH--LAQEARARGIPI---P 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 512 TDADKACKPFLSEswkalaftspnLTELCtmnHTLGLPTPAelprsLEDVLGCAPALSRPLLEHLHC--VLVTLGSLGVL 589
Cdd:cd01945 156 LDLDGGGLRVLEE-----------LLPLA---DHAICSENF-----LRPNTGSADDEALELLASLGIpfVAVTLGEAGCL 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688616936 590 VCgeHEAGTVnlqprkqkrarlcaVHYPALtvsSEETVNVSGAGDSFAGAMMVGILQG 647
Cdd:cd01945 217 WL--ERDGEL--------------FHVPAF---PVEVVDTTGAGDVFHGAFAHALAEG 255
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
386-648 |
9.60e-05 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 44.83 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 386 GGVGRNIADCLSRLGHKPLFISAIGKDsHSDAVLNYCKH--MDTSAVARLQDQRTATycAVITESGELS--LGLGdMDIH 461
Cdd:cd01164 36 GGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEegIPDDFVEVAGETRINV--KIKEEDGTETeiNEPG-PEIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 462 QQIQEQYVSQFVDQLSSASLIVLDG----NIPVSTINYVCRIAKKHAVPVWFeptDADK-------ACKPFLseswkala 530
Cdd:cd01164 112 EEELEALLEKLKALLKKGDIVVLSGslppGVPADFYAELVRLAREKGARVIL---DTSGeallaalAAKPFL-------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 531 fTSPNLTELCTM-NHTLGlptpaelprSLEDVLgcaPALSRPLLEHLHCVLVTLGSLGVLVCGEHEAGTVNLqprkqkra 609
Cdd:cd01164 181 -IKPNREELEELfGRPLG---------DEEDVI---AAARKLIERGAENVLVSLGADGALLVTKDGVYRASP-------- 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 688616936 610 rlcavhyPALTVSSeeTVnvsGAGDSFAGAMMVGILQGL 648
Cdd:cd01164 240 -------PKVKVVS--TV---GAGDSMVAGFVAGLAQGL 266
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
507-661 |
6.20e-04 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 42.71 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688616936 507 VWfEPTDADkaCKPFLSESWKAL----AFTSPNLTELCTMnhtLGLPTPAELPRSLEDVLGCAPALSRPLLEHLHCVLVT 582
Cdd:cd01943 158 VW-EPLPDS--CDPENLEDLLQAlprvDVFSPNLEEAARL---LGLPTSEPSSDEEKEAVLQALLFSGILQDPGGGVVLR 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688616936 583 LGSLGVLVCgeheagtvnlqprkqKRARLCAVHYPALTVSSEETVNVSGAGDSFAGAMMVGIlqgLHTDSCVQMGLLAA 661
Cdd:cd01943 232 CGKLGCYVG---------------SADSGPELWLPAYHTKSTKVVDPTGGGNSFLGGFAAGL---ALTKSIDEACIYGS 292
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
625-670 |
6.37e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 42.03 E-value: 6.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 688616936 625 ETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAARRSLLTPHP 670
Cdd:PRK09813 214 TVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
616-662 |
4.12e-03 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 40.08 E-value: 4.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 688616936 616 YPALTVSSEETVNVSGAGDSFAGAMMVGILQGLHTDSCVQMGLLAAR 662
Cdd:PLN02548 269 FPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAAN 315
|
|
| |
