|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04024 |
PRK04024 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
2-411 |
0e+00 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235203 Cd Length: 412 Bit Score: 677.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 2 KKRKGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFL 81
Cdd:PRK04024 1 KMMKILLIILDGLGDRPVKELGGKTPLEAANTPNMDKLAKEGICGLMDPISPGVRPGSDTAHLAILGYDPYKYYTGRGPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 82 EAVGVGLDLDRDDLAFRVNFATI-ENGIITDRRAGRIStEEAHELAKAIQEEVKL-PVEFIFVGATGHRAVLVLKGMAKG 159
Cdd:PRK04024 81 EALGVGLDLKPGDVAFRCNFATVdENGVVVDRRAGRIS-EETEELAKAINEKEEIdGVEIIFKSSTGHRAALVLRGPGLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 160 YRVGENDPHEAGKPPHEFTWEDE--ESRRVAEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKF 237
Cdd:PRK04024 160 DKVSDTDPHKEGKKVKESKPLDDspEAKKTAEILNELTKKAYEVLDDHPVNKERRKQGLPPANIILLRGAGEVPEIP-KF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 238 TEQWKVKAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAE 317
Cdd:PRK04024 239 TEKYGLKAACVAGTALIKGIARMVGMDVITVEGATGGKDTNYMAKAKAAVELLKEYDFVLLNIKGTDEAGHDGDFEGKVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 318 MIEKADRMIGYIVDNIDLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVP 397
Cdd:PRK04024 319 VIEKIDKMLGYILDNLDLDEVYIAVTGDHSTPVEVKDHSGDPVPILIYGPGVRVDDVEKFNELSAAKGGLGRIRGLDVMP 398
|
410
....*....|....
gi 2540962068 398 IMMDLMNRSEKFGA 411
Cdd:PRK04024 399 ILLDLMNRAEKFGA 412
|
|
| ApgM |
COG3635 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ... |
5-401 |
0e+00 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate transport and metabolism]; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 442852 Cd Length: 398 Bit Score: 535.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 5 KGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEAV 84
Cdd:COG3635 1 KYILLIGDGMADRPIEELGGKTPLEAARTPNMDRLAREGICGLMDTVPPGMPPGSDVANLSLLGYDPEKYYTGRGPLEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 85 GVGLDLDRDDLAFRVNFATI-ENGIITDRRAGRISTEEAHELAKAIQEEVKlPVEFIFVGATGHRAVLVLKGMAKGYRVG 163
Cdd:COG3635 81 GMGIELGPGDVAFRCNLVTLdEDGVMVDRSAGHISTEEAAELIEALNEELG-GVEVRFYPGVSYRHLLVLRGGGLSDKVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 164 ENDPHEAGKPPHEFTWEDEESRRVAEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKFTEQWKV 243
Cdd:COG3635 160 DTPPHDIGGKPIADYLPLPEGKKTAEILNELMEKSYEILADHPVNRKRVEEGKPPANSIWLWGAGKRPALP-PFKEKYGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 244 KAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAEMIEKAD 323
Cdd:COG3635 239 KGAVISAVDLIKGIGKLAGMDVIDVPGATGYLDTNYAGKAEAALEALKDYDFVYVHVEAPDEAGHDGDLEEKVKAIERID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 324 -RMIGYIVDNI-DLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVPIMMD 401
Cdd:COG3635 319 rRVVGPLLEGLeKFEDYRILVTPDHPTPISLRTHSGDPVPFLIYGPGVRPDDVTRFDERSAAKGGLGRIRGHELMPLLLN 398
|
|
| iPGM_like |
cd16011 |
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ... |
4-403 |
2.44e-179 |
|
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).
Pssm-ID: 293735 Cd Length: 368 Bit Score: 503.93 E-value: 2.44e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 4 RKGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEA 83
Cdd:cd16011 1 MKYVLLILDGLGDRPIPELGGKTPLEAAKTPNLDRLAAEGICGLMDPVPPGIAPGSDTAHLSLLGYDPEEYYTGRGPLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 84 VGVGLDLDRDDLAFRVNFATI--ENGIITDRRAGRISTEEAHELAKAIQEEVKlPVEFIFVGATGHRAVLVLKgmakgyr 161
Cdd:cd16011 81 LGAGIDLKPGDVAFRCNFATVddEDGIIVDRRAGRISTEEAAELIAILNLEFG-GVEVRFKPGVEHRHVLVLR------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 162 vgendpheagkppheftwedeesrrvAEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKFTEQW 241
Cdd:cd16011 153 --------------------------AELLNEFLEKAYEILKDHPVNKKRRAKGKPPANAILLRGAGKRPALP-PFEERY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 242 KVKAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAEMIEK 321
Cdd:cd16011 206 GLKGAVIAAVDLIKGIGRLAGMDVIEVPGATGYLDTDYEGKAEAALEALKDYDFVFVHVKAPDEAGHDGDPEAKVKAIER 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 322 ADRMIGYIVDN-IDLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVPIMM 400
Cdd:cd16011 286 IDKAIVGPLLElLDGEDFVIVVTPDHSTPCSLKTHSGDPVPFLIYGPGVRRDGVTRFDEISAAAGGLGRIRGHELMPLLL 365
|
...
gi 2540962068 401 DLM 403
Cdd:cd16011 366 NYA 368
|
|
| apgM |
TIGR00306 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ... |
7-401 |
6.27e-152 |
|
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally characterized in archaea as 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This model describes a set of proteins in the Archaea (two each in Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Archaeoglobus fulgidus) and in Aquifex aeolicus (1 member). [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273005 Cd Length: 396 Bit Score: 435.36 E-value: 6.27e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 7 LLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEAVGV 86
Cdd:TIGR00306 1 VLIIIDGLADRPLEELDGKTPLQVAKTPNMDRLAEEGICGLMRTIKEGIRPGSDTAHLSILGYDPYEEYTGRGPIEAAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 87 GLDLDRDDLAFRVNFATI-ENGIITDRRAGRISTEEAHELAKAIqEEVKLPVEFIFVGATGHRAVLVLKGMAKGYRVGEN 165
Cdd:TIGR00306 81 GVELKPGDVAFRCNLATVdEDFVIVDRRAGRISREEASKLIDEL-NRTELDGFVLFYSGTGHRNLLVIRGPGLSDKVSDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 166 DPHEAGKPPHEFT--WEDEESRRVAEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKFTEQWKV 243
Cdd:TIGR00306 160 DPKDIGKKVKAILplAGSEEAKKTAELLNELMLESAEVLQNHPINTKRAKKGKGPANMILPRGAGRMPRVE-SFKERYGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 244 KAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAEMIEKAD 323
Cdd:TIGR00306 239 RGAMIAEVDLIKGLARLIGMDVIRVEGATGGIDTDYRGKVRALILALEEYDFVLVHTKGPDEAGHDGDPELKVRAIEKID 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540962068 324 RMIGYIVDNIDLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVPIMMD 401
Cdd:TIGR00306 319 SKIVGPLLALDLDETRLILTADHSTPVEVKDHSADPVPIVIVGPGVRVDEVKSFNEFACRKGALGRIRGEDLMDILLD 396
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
4-402 |
8.48e-103 |
|
Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.
Pssm-ID: 396305 Cd Length: 410 Bit Score: 310.87 E-value: 8.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 4 RKGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLA------RWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRG 77
Cdd:pfam01676 1 KKVVLIVLDGWGDRPAEDLNAKTPLHIAKTPNMDKLAkeypeqLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 78 RGFLEAVGVGLDLDRDDLAFRVNFATIENGIITDRRAGRISTEEAHELAKAIQE---EVKLPVE---------------- 138
Cdd:pfam01676 81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIAlakEAGAIKVhllgdgddrpvgyild 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 139 ------FIFVGATGHRAVLVLKGMAKGYRVGENDPHEAGKPPHEFTWEDEESRRVAEILNDFVRQAHEVLERHPVNEERR 212
Cdd:pfam01676 161 gdavitINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLEGHGLKQLRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 213 KAGKPVANYLLVRGAGTYPDIPMKftEQWkvkaaavvavsLVKGvARAIGFDIYtpdgatgeYNTDEMAKARKVVELLKE 292
Cdd:pfam01676 241 AETEKYAHVTFFWGGGREPPFPGE--ERY-----------LIPS-PKVATYDLQ--------PEMSAMEITDKLLEALKE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 293 -YDFVFLHFKPTDAAGHDNNPRLKAEMIEKADRMIGYIVDNIDLEDVVIAITGDHSTPCEVM--NHSGDPVPVLIAGGGV 369
Cdd:pfam01676 299 kYDFVFVNFANTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKdtDHTREPVPILIYGKGV 378
|
410 420 430
....*....|....*....|....*....|...
gi 2540962068 370 RADhTESFGERECMRGGLGRIKGHDIVPIMMDL 402
Cdd:pfam01676 379 RPD-QVLFGEKFRERGGLADIAATILMLLGLKK 410
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04024 |
PRK04024 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
2-411 |
0e+00 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235203 Cd Length: 412 Bit Score: 677.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 2 KKRKGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFL 81
Cdd:PRK04024 1 KMMKILLIILDGLGDRPVKELGGKTPLEAANTPNMDKLAKEGICGLMDPISPGVRPGSDTAHLAILGYDPYKYYTGRGPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 82 EAVGVGLDLDRDDLAFRVNFATI-ENGIITDRRAGRIStEEAHELAKAIQEEVKL-PVEFIFVGATGHRAVLVLKGMAKG 159
Cdd:PRK04024 81 EALGVGLDLKPGDVAFRCNFATVdENGVVVDRRAGRIS-EETEELAKAINEKEEIdGVEIIFKSSTGHRAALVLRGPGLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 160 YRVGENDPHEAGKPPHEFTWEDE--ESRRVAEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKF 237
Cdd:PRK04024 160 DKVSDTDPHKEGKKVKESKPLDDspEAKKTAEILNELTKKAYEVLDDHPVNKERRKQGLPPANIILLRGAGEVPEIP-KF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 238 TEQWKVKAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAE 317
Cdd:PRK04024 239 TEKYGLKAACVAGTALIKGIARMVGMDVITVEGATGGKDTNYMAKAKAAVELLKEYDFVLLNIKGTDEAGHDGDFEGKVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 318 MIEKADRMIGYIVDNIDLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVP 397
Cdd:PRK04024 319 VIEKIDKMLGYILDNLDLDEVYIAVTGDHSTPVEVKDHSGDPVPILIYGPGVRVDDVEKFNELSAAKGGLGRIRGLDVMP 398
|
410
....*....|....
gi 2540962068 398 IMMDLMNRSEKFGA 411
Cdd:PRK04024 399 ILLDLMNRAEKFGA 412
|
|
| ApgM |
COG3635 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ... |
5-401 |
0e+00 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate transport and metabolism]; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 442852 Cd Length: 398 Bit Score: 535.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 5 KGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEAV 84
Cdd:COG3635 1 KYILLIGDGMADRPIEELGGKTPLEAARTPNMDRLAREGICGLMDTVPPGMPPGSDVANLSLLGYDPEKYYTGRGPLEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 85 GVGLDLDRDDLAFRVNFATI-ENGIITDRRAGRISTEEAHELAKAIQEEVKlPVEFIFVGATGHRAVLVLKGMAKGYRVG 163
Cdd:COG3635 81 GMGIELGPGDVAFRCNLVTLdEDGVMVDRSAGHISTEEAAELIEALNEELG-GVEVRFYPGVSYRHLLVLRGGGLSDKVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 164 ENDPHEAGKPPHEFTWEDEESRRVAEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKFTEQWKV 243
Cdd:COG3635 160 DTPPHDIGGKPIADYLPLPEGKKTAEILNELMEKSYEILADHPVNRKRVEEGKPPANSIWLWGAGKRPALP-PFKEKYGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 244 KAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAEMIEKAD 323
Cdd:COG3635 239 KGAVISAVDLIKGIGKLAGMDVIDVPGATGYLDTNYAGKAEAALEALKDYDFVYVHVEAPDEAGHDGDLEEKVKAIERID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 324 -RMIGYIVDNI-DLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVPIMMD 401
Cdd:COG3635 319 rRVVGPLLEGLeKFEDYRILVTPDHPTPISLRTHSGDPVPFLIYGPGVRPDDVTRFDERSAAKGGLGRIRGHELMPLLLN 398
|
|
| iPGM_like |
cd16011 |
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ... |
4-403 |
2.44e-179 |
|
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).
Pssm-ID: 293735 Cd Length: 368 Bit Score: 503.93 E-value: 2.44e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 4 RKGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEA 83
Cdd:cd16011 1 MKYVLLILDGLGDRPIPELGGKTPLEAAKTPNLDRLAAEGICGLMDPVPPGIAPGSDTAHLSLLGYDPEEYYTGRGPLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 84 VGVGLDLDRDDLAFRVNFATI--ENGIITDRRAGRISTEEAHELAKAIQEEVKlPVEFIFVGATGHRAVLVLKgmakgyr 161
Cdd:cd16011 81 LGAGIDLKPGDVAFRCNFATVddEDGIIVDRRAGRISTEEAAELIAILNLEFG-GVEVRFKPGVEHRHVLVLR------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 162 vgendpheagkppheftwedeesrrvAEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKFTEQW 241
Cdd:cd16011 153 --------------------------AELLNEFLEKAYEILKDHPVNKKRRAKGKPPANAILLRGAGKRPALP-PFEERY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 242 KVKAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAEMIEK 321
Cdd:cd16011 206 GLKGAVIAAVDLIKGIGRLAGMDVIEVPGATGYLDTDYEGKAEAALEALKDYDFVFVHVKAPDEAGHDGDPEAKVKAIER 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 322 ADRMIGYIVDN-IDLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVPIMM 400
Cdd:cd16011 286 IDKAIVGPLLElLDGEDFVIVVTPDHSTPCSLKTHSGDPVPFLIYGPGVRRDGVTRFDEISAAAGGLGRIRGHELMPLLL 365
|
...
gi 2540962068 401 DLM 403
Cdd:cd16011 366 NYA 368
|
|
| apgM |
TIGR00306 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ... |
7-401 |
6.27e-152 |
|
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally characterized in archaea as 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This model describes a set of proteins in the Archaea (two each in Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Archaeoglobus fulgidus) and in Aquifex aeolicus (1 member). [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273005 Cd Length: 396 Bit Score: 435.36 E-value: 6.27e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 7 LLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEAVGV 86
Cdd:TIGR00306 1 VLIIIDGLADRPLEELDGKTPLQVAKTPNMDRLAEEGICGLMRTIKEGIRPGSDTAHLSILGYDPYEEYTGRGPIEAAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 87 GLDLDRDDLAFRVNFATI-ENGIITDRRAGRISTEEAHELAKAIqEEVKLPVEFIFVGATGHRAVLVLKGMAKGYRVGEN 165
Cdd:TIGR00306 81 GVELKPGDVAFRCNLATVdEDFVIVDRRAGRISREEASKLIDEL-NRTELDGFVLFYSGTGHRNLLVIRGPGLSDKVSDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 166 DPHEAGKPPHEFT--WEDEESRRVAEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKFTEQWKV 243
Cdd:TIGR00306 160 DPKDIGKKVKAILplAGSEEAKKTAELLNELMLESAEVLQNHPINTKRAKKGKGPANMILPRGAGRMPRVE-SFKERYGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 244 KAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAEMIEKAD 323
Cdd:TIGR00306 239 RGAMIAEVDLIKGLARLIGMDVIRVEGATGGIDTDYRGKVRALILALEEYDFVLVHTKGPDEAGHDGDPELKVRAIEKID 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540962068 324 RMIGYIVDNIDLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVPIMMD 401
Cdd:TIGR00306 319 SKIVGPLLALDLDETRLILTADHSTPVEVKDHSADPVPIVIVGPGVRVDEVKSFNEFACRKGALGRIRGEDLMDILLD 396
|
|
| PRK04135 |
PRK04135 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
5-411 |
4.46e-122 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 179745 [Multi-domain] Cd Length: 395 Bit Score: 359.23 E-value: 4.46e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 5 KGLLIILDGLGDRPVKEfGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEAV 84
Cdd:PRK04135 9 KIVLLVLDGLGGLPHPE-NGKTELEAAKTPNLDALAKESDLGLLIPVLPGITPGSGPGHLGLFGYDPLKYQIGRGILEAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 85 GVGLDLDRDDLAFRVNFATIEN-GIITDRRAGRISTEEAHELAKAIQEEVKL--PVEFIFVGATGHRAVLVLKGMAKGYR 161
Cdd:PRK04135 88 GIGFELGEGDVAARGNFATVDGeGIIVDRRAGRPSTEENAKLVAKLSEAIKEieGVEVFFYPGKEHRFVVVFRGEGLSDK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 162 VGENDPHEAGKPPHEFTWEDEESRRVAEILNDFVRQAHEVLerhpvneerrkAGKPVANYLLVRGAGTYPDIPmKFTEQW 241
Cdd:PRK04135 168 VTDTDPQKTGVPPLEAKALDEESEKTARIVNEFLKRAAEVL-----------KDEPKANFALLRGFSKKPDFP-SFEEVY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 242 KVKAAAVVAVSLVKGVARAIGFDIYTpdgaTGEYNTDEMAKARKVvelLKEYDFVFLHFKPTDAAGHDNNPRLKAEMIEK 321
Cdd:PRK04135 236 KLKAAAIASYPMYRGLAKLVGMDVLP----TGQTLEDEIKTLKEN---WNDYDFFFLHVKKTDSYGEDGNFEEKVKVIEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 322 ADRMIGYIvdnIDLEDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVPIMMD 401
Cdd:PRK04135 309 VDALLPEI---LALKPDVLVITGDHSTPAVLKGHSWHPVPLLLYSKYCRPDLSQRFTERECARGGLGHIPAVDLMPLALA 385
|
410
....*....|
gi 2540962068 402 LMNRSEKFGA 411
Cdd:PRK04135 386 HALRLEKYGA 395
|
|
| PRK04200 |
PRK04200 |
cofactor-independent phosphoglycerate mutase; Provisional |
5-401 |
5.12e-111 |
|
cofactor-independent phosphoglycerate mutase; Provisional
Pssm-ID: 179781 Cd Length: 395 Bit Score: 331.07 E-value: 5.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 5 KGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLARWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEAV 84
Cdd:PRK04200 2 KYIILIGDGMADEPIEELGGKTPLQAAKTPNMDKMAREGRVGLAKTVPEGFPPGSDVANMSILGYDPRKYYTGRGPLEAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 85 GVGLDLDRDDLAFRVNFATIENGIITDRRAGRISTEEAHELAKAIQEEvkLPVEFI-FVGATGHRAVLVLKGMAKGyRVG 163
Cdd:PRK04200 82 SMGVELGPDDVAFRCNLVTLEDGKMKDYSAGHISSEEARELIEALNEE--LGSDRVkFYPGVSYRHLLVIKGGFTA-DLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 164 ENDPHE-AGKPPHEFTWEDEESrrvaEILNDFVRQAHEVLERHPVNEERRKAGKPVANYLLVRGAGTYPDIPmKFTEQWK 242
Cdd:PRK04200 159 CTPPHDiTGKPVADYLPRGEGS----AELNELMLSSQEILEDHPVNLKRIEEGKLPANSIWLWGQGYAPKMP-SFKEKYG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 243 VKAAAVVAVSLVKGVARAIGFDIYTPDGATGEYNTDEMAKARKVVELLKEYDFVFLHFKPTDAAGHDNNPRLKAEMIEKA 322
Cdd:PRK04200 234 LKGAVISAVDLLKGIGIYAGLDVIEVPGATGYLDTNYEGKAEAALEALKTHDFVFVHVEAPDEAGHEGDLEAKIKAIEDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 323 D-RMIGYIVDNIDL-EDVVIAITGDHSTPCEVMNHSGDPVPVLIAGGGVRADHTESFGERECMRGGLGRIKGHDIVPIMM 400
Cdd:PRK04200 314 DeRVVGPILEALKKyEDYRILVLPDHPTPIELKTHTADPVPFLIYGEGIEPDGVQTFDEKSARKGGLGLVEGCELMELLL 393
|
.
gi 2540962068 401 D 401
Cdd:PRK04200 394 K 394
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
4-402 |
8.48e-103 |
|
Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.
Pssm-ID: 396305 Cd Length: 410 Bit Score: 310.87 E-value: 8.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 4 RKGLLIILDGLGDRPVKEFGGKTPLEYANTPNMDGLA------RWGMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRG 77
Cdd:pfam01676 1 KKVVLIVLDGWGDRPAEDLNAKTPLHIAKTPNMDKLAkeypeqLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 78 RGFLEAVGVGLDLDRDDLAFRVNFATIENGIITDRRAGRISTEEAHELAKAIQE---EVKLPVE---------------- 138
Cdd:pfam01676 81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIAlakEAGAIKVhllgdgddrpvgyild 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 139 ------FIFVGATGHRAVLVLKGMAKGYRVGENDPHEAGKPPHEFTWEDEESRRVAEILNDFVRQAHEVLERHPVNEERR 212
Cdd:pfam01676 161 gdavitINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLEGHGLKQLRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 213 KAGKPVANYLLVRGAGTYPDIPMKftEQWkvkaaavvavsLVKGvARAIGFDIYtpdgatgeYNTDEMAKARKVVELLKE 292
Cdd:pfam01676 241 AETEKYAHVTFFWGGGREPPFPGE--ERY-----------LIPS-PKVATYDLQ--------PEMSAMEITDKLLEALKE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 293 -YDFVFLHFKPTDAAGHDNNPRLKAEMIEKADRMIGYIVDNIDLEDVVIAITGDHSTPCEVM--NHSGDPVPVLIAGGGV 369
Cdd:pfam01676 299 kYDFVFVNFANTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKdtDHTREPVPILIYGKGV 378
|
410 420 430
....*....|....*....|....*....|...
gi 2540962068 370 RADhTESFGERECMRGGLGRIKGHDIVPIMMDL 402
Cdd:pfam01676 379 RPD-QVLFGEKFRERGGLADIAATILMLLGLKK 410
|
|
| PhosphMutase |
pfam10143 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; This family represents 2, ... |
43-208 |
1.45e-70 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), a metalloenzyme found particularly in archaea and some eubacteria, which catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in the reaction: [(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate] (EC 5.4.2.12).
Pssm-ID: 462961 [Multi-domain] Cd Length: 171 Bit Score: 219.65 E-value: 1.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 43 GMLGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEAVGVGLDLDRDDLAFRVNFATI--ENGIITDRRAGRISTE 120
Cdd:pfam10143 3 GECGLMDTVPPGIAPGSDVAHLSILGYDPRKYYTGRGPLEALGIGIDLKPGDVAFRCNLVTVdeEDGIILDRRAGRISTE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 121 EAHELAKAIQEEVKlPVEFIFVGATGHRAVLVLKGMAKGYRVGENDP--HEAGKPPHEFTWEDEESRRVAEILNDFVRQA 198
Cdd:pfam10143 83 EARELIEALNEELG-GVEVRFYPGVSYRHLLVLRGEGLSDKITDTDPphDITGRPILEYLPLDPEAGKTAEVLNELMLKS 161
|
170
....*....|
gi 2540962068 199 HEVLERHPVN 208
Cdd:pfam10143 162 YEILKDHPVN 171
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
294-404 |
1.63e-09 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 58.37 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 294 DFVFLHFKPTDAAGHD---NNPRLKaEMIEKADRMIGYIVDNID----LEDVVIAITGDHS-TPceVMNHSGDPV----- 360
Cdd:cd16018 158 DLILLYFEEPDSAGHKygpDSPEVN-EALKRVDRRLGYLIEALKerglLDDTNIIVVSDHGmTD--VGTHGYDNElpdmr 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2540962068 361 PVLIA-GGGVRADHTesfgerecmrggLGRIKGHDIVPIMMDLMN 404
Cdd:cd16018 235 AIFIArGPAFKKGKK------------LGPFRNVDIYPLMCNLLG 267
|
|
| PRK12383 |
PRK12383 |
putative mutase; Provisional |
289-383 |
2.90e-07 |
|
putative mutase; Provisional
Pssm-ID: 237085 Cd Length: 406 Bit Score: 52.28 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 289 LLKEYD-----FVFLHFKPTDAAGHDNNPRLKAEMIEKADRMIGYIVDNIDLEDVVIaITGDHST-P-CEVMNHSGDPVP 361
Cdd:PRK12383 278 TLDEFNthptaFICTNIQETDLAGHAEDVARYAERLEVVDRNLARLLEAMTPDDCLV-VMADHGNdPtIGHSHHTREVVP 356
|
90 100
....*....|....*....|..
gi 2540962068 362 VLIAGGGVRAdhtESFGERECM 383
Cdd:PRK12383 357 LLVYQKGLQA---TQLGVRTTL 375
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
266-346 |
3.93e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 51.67 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 266 YTPDGAT---GEYNTDEMAkARKVVELLKEY--DFVFLHFKPTDAAGHD---NNPRLKAEmIEKADRMIGYIVDNID--- 334
Cdd:COG1524 152 YPYDGRKpllGNPAADRWI-AAAALELLREGrpDLLLVYLPDLDYAGHRygpDSPEYRAA-LREVDAALGRLLDALKarg 229
|
90
....*....|...
gi 2540962068 335 -LEDVVIAITGDH 346
Cdd:COG1524 230 lYEGTLVIVTADH 242
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
283-404 |
1.18e-06 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 50.49 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 283 ARKVVELLK--EYDFVFLHFKPTDAAGHDNNprLKAEM--IEKADRMIGYIVDNIDLEDVVIAITGDHSTpCEVM----- 353
Cdd:cd16010 371 TDKLIEAIKsgKYDFIVVNFANPDMVGHTGN--LEAAVkaVEAVDECLGRIVEAVLENGGTLLITADHGN-AEEMidpet 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2540962068 354 -----NHSGDPVPVLIAGGGVRADHTESfgerecmrGGLGrikghDIVPIMMDLMN 404
Cdd:cd16010 448 ggphtAHTTNPVPFIIVDPGLKRKLLKD--------GGLA-----DVAPTILDLLG 490
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
260-383 |
1.21e-06 |
|
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.
Pssm-ID: 293733 Cd Length: 382 Bit Score: 50.14 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 260 AIGF--DIYTPDGATGEY----NTDEMAKarkVVELLKEYD--FVFLHFKPTDA-AGHDNNPRLKAEMIEKADRMIGYIV 330
Cdd:cd16009 233 GIGKiaDIFAGRGITESIhtksNADGMEK---TLEALKEDFngLIFTNLVDFDMlYGHRRDPEGYAEALEEFDRRLPELL 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 331 DNIDLEDVVIaITGDH-------STpcevmNHSGDPVPVLIAGGGVRAdhtESFGERECM 383
Cdd:cd16009 310 AKLKEDDLLI-ITADHgndptigGT-----DHTREYVPLLVYGKGLKG---VNLGTRETF 360
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
275-376 |
2.42e-06 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 48.19 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 275 YNTDEMAKARKVVELLKE-YDFVFLHFKPTDAAGHDNNPRL--KAEMIEKADRMIGYIVD----NIDLEDVVIAITGDHS 347
Cdd:cd00016 101 YRTGVIGLLKAIDETSKEkPFVLFLHFDGPDGPGHAYGPNTpeYYDAVEEIDERIGKVLDalkkAGDADDTVIIVTADHG 180
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2540962068 348 TPCEVMN------------HSGDPVPVLIAGGGVRADHTES 376
Cdd:cd00016 181 GIDKGHGgdpkadgkadksHTGMRVPFIAYGPGVKKGGVKH 221
|
|
| ALP |
cd16012 |
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ... |
304-362 |
1.38e-05 |
|
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP.
Pssm-ID: 293736 Cd Length: 283 Bit Score: 46.27 E-value: 1.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540962068 304 DAAGHDNNP-RLKAEMIEkADRMIGYIVDNID-LEDVVIAITGDHSTpcevmNHSGDPVPV 362
Cdd:cd16012 201 DWAGHANDAaRAIEETLA-FDKAVKVALDFAKkDGDTLVIVTADHET-----GHTGEDVPV 255
|
|
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
260-381 |
2.34e-05 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 46.26 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 260 AIG--FDIYTPDGATGEY----NTDEMAKARKVVELLKEYDFVFLHFKPTDAA-GHDNNPRLKAEMIEKADRMIGYIVDN 332
Cdd:PRK05362 239 AVGkiADIFAGQGITEKVktksNMDGMDATIEEMKEAGDNGLVFTNLVDFDSLyGHRRDVAGYAAALEEFDARLPELLAA 318
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2540962068 333 IDLEDVVIaITGDH-------STpcevmNHSGDPVPVLIAGGGVRAdhtESFGERE 381
Cdd:PRK05362 319 LKEDDLLI-ITADHgndptwpGT-----DHTREYVPLLVYGPKFKG---GSLGHRE 365
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
293-377 |
8.78e-05 |
|
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293743 [Multi-domain] Cd Length: 292 Bit Score: 43.89 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540962068 293 YDFVFLHFKPTDAAGHDNNpRLKAEMIEKA----DRMIGYIVDNIDlEDVVIAITGDHStpcevMNHSGDpvpvliaGGG 368
Cdd:cd16019 153 WDFIILHFLGLDHLGHKHN-TTSSPELEKKldqmDNLIRDIYDRMD-NDTLLVVVSDHG-----MNNDGN-------HGG 218
|
....*....
gi 2540962068 369 VRADHTESF 377
Cdd:cd16019 219 SSTEETSSF 227
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
277-346 |
2.02e-04 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 43.18 E-value: 2.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540962068 277 TDEMAKARKVVELLKEYDFVFLHFKPTDAAGHD---NNPRLkAEMIEKADRMIGYIVDNID----LEDVVIAITGDH 346
Cdd:pfam01663 147 LQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRygpDSPEV-EDALRRVDRAIGDLLEALDerglFEDTNVIVVSDH 222
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
1-39 |
4.78e-03 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 38.93 E-value: 4.78e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2540962068 1 MKKRKGLLIILDGLGDRPVKEFGGktpLEYANTPNMDGL 39
Cdd:PRK05434 2 MMKKPVVLIILDGWGYREETEGNA---IALAKTPNLDRL 37
|
|
| |
