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Conserved domains on  [gi|445999332|ref|WP_000077187|]
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MULTISPECIES: phosphopentomutase [Streptococcus]

Protein Classification

phosphopentomutase( domain architecture ID 10012347)

phosphopentomutase catalyzes the interconversion of alpha-D-ribose 5-phosphate and alpha-D-ribose 1-phosphate

CATH:  3.30.70.1250
EC:  5.4.2.7
Gene Ontology:  GO:0008973|GO:0030145|GO:0006015
PubMed:  21193409
SCOP:  4003235

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05362 PRK05362
phosphopentomutase; Provisional
 4-403 0e+00

phosphopentomutase; Provisional


:

Pssm-ID: 235430  Cd Length: 394  Bit Score: 695.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   4 FDRIHLVVLDSVGIGAAPDANDFvnagvPDGASDTLGHISK--TVGLAVPNMAKIGLGNIPRPQALKTVPAEENPSGYAT 81
Cdd:PRK05362   1 MKRVFLIVLDSVGIGAAPDAAKF-----GDEGADTLGHIAEarKGGLKLPNLAKLGLGNIATGTPIAGVPANAEPIGYYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  82 KLQEVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGR-KVIreANKPYSGTAVIDDFGPRQMETGELII 160
Cdd:PRK05362  76 KAQEVSSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRpGIL--GNKHASGTEIIDELGEEHMKTGKPIV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 161 YTSADPVLQIAAHEDIIPLEELYRICEYARSITMERPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKLDQA 240
Cdd:PRK05362 154 YTSADSVFQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVGEPGNFTRTGNRHDYALKPPAPTVLDKLKEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 241 GIDTYAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlSEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDER 320
Cdd:PRK05362 234 GGEVIAVGKIADIFAGQGITEKV-KTKSNMDGMDATIEEMK-EAGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDAR 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 321 LPEIISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPVGHFADISATVADNFGVDTAMIGESFLQ 400
Cdd:PRK05362 312 LPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGGSLGHRETFADIGATIADNFGVEPMEYGKSFLD 391


                 ...
gi 445999332 401 DLV 403
Cdd:PRK05362 392 ELK 394
 
Name Accession Description Interval E-value
PRK05362 PRK05362
phosphopentomutase; Provisional
 4-403 0e+00

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 695.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   4 FDRIHLVVLDSVGIGAAPDANDFvnagvPDGASDTLGHISK--TVGLAVPNMAKIGLGNIPRPQALKTVPAEENPSGYAT 81
Cdd:PRK05362   1 MKRVFLIVLDSVGIGAAPDAAKF-----GDEGADTLGHIAEarKGGLKLPNLAKLGLGNIATGTPIAGVPANAEPIGYYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  82 KLQEVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGR-KVIreANKPYSGTAVIDDFGPRQMETGELII 160
Cdd:PRK05362  76 KAQEVSSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRpGIL--GNKHASGTEIIDELGEEHMKTGKPIV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 161 YTSADPVLQIAAHEDIIPLEELYRICEYARSITMERPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKLDQA 240
Cdd:PRK05362 154 YTSADSVFQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVGEPGNFTRTGNRHDYALKPPAPTVLDKLKEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 241 GIDTYAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlSEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDER 320
Cdd:PRK05362 234 GGEVIAVGKIADIFAGQGITEKV-KTKSNMDGMDATIEEMK-EAGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDAR 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 321 LPEIISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPVGHFADISATVADNFGVDTAMIGESFLQ 400
Cdd:PRK05362 312 LPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGGSLGHRETFADIGATIADNFGVEPMEYGKSFLD 391


                 ...
gi 445999332 401 DLV 403
Cdd:PRK05362 392 ELK 394
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
4-400 0e+00

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 649.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   4 FDRIHLVVLDSVGIGAAPDANDFvnagvPDGASDTLGHISKTVG-LAVPNMAKIGLGNIPRpqaLKTVPAEENPSGYATK 82
Cdd:COG1015    1 MKRAILIVLDSVGIGEAPDAAKF-----GDEGANTLGHIAEAVGgLNLPNLARLGLGNIAP---LAGLPPVEEPLGAYGK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  83 LQEVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGRKVIreANKPYSGTAVIDDFGPRQMETGELIIYT 162
Cdd:COG1015   73 MAEVSAGKDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVL--GNKPASGTEIIEELGEEHMRTGKPIVYT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 163 SADPVLQIAAHEDIIPLEELYRICEYARSITMErPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKLDQAGI 242
Cdd:COG1015  151 SADSVFQIAAHEEVFPLEELYRLCEIARELLDG-EYAVGRVIARPFVGEPGNFVRTANRHDYALKPPGPTLLDRLKEAGG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 243 DTYAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlsEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDERLP 322
Cdd:COG1015  230 DVIAVGKISDIFAGRGITESV-KTKGNADGMDKTLEAMD--EAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLP 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445999332 323 EIISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPV-GHFADISATVADNFGVDTAMIGESFLQ 400
Cdd:COG1015  307 ELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTrETFADIGATIADHFGVPPPGHGTSFLS 385
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 6-398 0e+00

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: 591.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   6 RIHLVVLDSVGIGAAPDANDFvnagvPDGASDTLGHISKTV-GLAVPNMAKIGLGNIPRpqaLKTVPAEENPSGYATKLQ 84
Cdd:cd16009    2 RVILIVLDSFGIGAMPDAAKF-----GDEGANTLGHIAEAVpGLNLPNLEKLGLGNIVG---IEGGPPKENPIAAYGKMR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  85 EVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGRKVIReaNKPYSGTAVIDDFGPRQMETGELIIYTSA 164
Cdd:cd16009   74 EASAGKDTTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLG--NKPASGTEIIKELGEEHLKTGAPIVYTSA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 165 DPVLQIAAHEDIIPLEELYRICEYARSITMErPALLGRIIARPYVGEPG-NFTRTANRHDYAVSPFEDTVLNKLDQAGID 243
Cdd:cd16009  152 DSVFQIAAHEEVIPLEELYRICEIAREILDG-EYKVGRVIARPFVGETGvYFKRTSNRHDYALVPPGKTVLDILKEAGIP 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 244 TYAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlsEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDERLPE 323
Cdd:cd16009  231 VIGIGKIADIFAGRGITESI-HTKSNADGMEKTLEALK--EDFNGLIFTNLVDFDMLYGHRRDPEGYAEALEEFDRRLPE 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445999332 324 IISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPVGHFADISATVADNFGVDTAMIGESF 398
Cdd:cd16009  308 LLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLKGVNLGTRETFADIGATIADNFGVEPPENGTSF 382
deoB TIGR01696
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ...
 6-397 7.63e-174

phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 162494  Cd Length: 381  Bit Score: 490.17  E-value: 7.63e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332    6 RIHLVVLDSVGIGAAPDANDFVNAGvpdgaSDTLGHISKTV-GLAVPNMAKIGLGNIPRPqalKTVPAEENPSGYATKLQ 84
Cdd:TIGR01696   1 RVFLIVMDSVGIGEAPDAADFGDEG-----AHTLGHIAEACaKLNLPNLTKLGLGKIHEP---AGVDGNEEPIAYYAKAH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   85 EVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGRKVIreANKPYSGTAVIDDFGPRQMETGELIIYTSA 164
Cdd:TIGR01696  73 EASSGKDTMTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYL--GNKPASGTVILDELGEEHMKTGKLIVYTSA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  165 DPVLQIAAHEDIIPLEELYRICEYARSITMERPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKLDQAGIDT 244
Cdd:TIGR01696 151 DSVLQIAAHEETFPLEELYEICEIARELTTDPKYNIGRIIARPFVGEPGNFQRTGNRHDYALKPFAPTVLQKLKDEGHDV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  245 YAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlsEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDERLPEI 324
Cdd:TIGR01696 231 ISIGKIADIYDGEGITKKV-RTTSNMDGMDATIKEMK--EDFTGISFTNLVDFDALWGHRRDVAGYAAALELFDRRLPEL 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445999332  325 ISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPVGH-FADISATVADNFGVDTAMIGES 397
Cdd:TIGR01696 308 FSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKPGHSLGHREtFADIGATIADNFGTSDPEYGKS 381
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 6-390 4.42e-65

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: 213.42  E-value: 4.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332    6 RIHLVVLDSVGIGAAPDANdfvnagvpdgaSDTLGHISKTvglavPNMAKIglgniprpqaLKTVPAEEN-PSGYA-TKL 83
Cdd:pfam01676   2 KVVLIVLDGWGDRPAEDLN-----------AKTPLHIAKT-----PNMDKL----------AKEYPEQLIgASGLAvGLP 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   84 QEVSLGKDTmtGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGRKVIREANKPYSGtaVIDDFGPRQMETGELIIYTS 163
Cdd:pfam01676  56 EGQMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHL--HGLGLDSGGGVHSHIEHLLA 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  164 ADPVLQIAAHEDIIPLEEL------YRICEYARSITMERPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKL 237
Cdd:pfam01676 132 LIALAKEAGAIKVHLLGDGddrpvgYILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKL 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  238 DQAGIDTYAVGKINDIFNGSGIN------------------------------------------HDMGHNKSNSHGIDT 275
Cdd:pfam01676 212 PSAGAFVPEEGKNTDGEVLEGHGlkqlriaetekyahvtffwgggreppfpgeerylipspkvatYDLQPEMSAMEITDK 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  276 LIKTMgLSEFEkgFSFTNLVDFDALyGHRRDPHGYRDCLHEFDERLPEIISAMRDKD-LLLITADHGNDPTYAGTDHTRE 354
Cdd:pfam01676 292 LLEAL-KEKYD--FVFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDTDHTRE 367

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 445999332  355 YIPLLAYSPSFT------GNGLIPVGHFADISATVADNFGVD 390
Cdd:pfam01676 368 PVPILIYGKGVRpdqvlfGEKFRERGGLADIAATILMLLGLK 409
 
Name Accession Description Interval E-value
PRK05362 PRK05362
phosphopentomutase; Provisional
 4-403 0e+00

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 695.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   4 FDRIHLVVLDSVGIGAAPDANDFvnagvPDGASDTLGHISK--TVGLAVPNMAKIGLGNIPRPQALKTVPAEENPSGYAT 81
Cdd:PRK05362   1 MKRVFLIVLDSVGIGAAPDAAKF-----GDEGADTLGHIAEarKGGLKLPNLAKLGLGNIATGTPIAGVPANAEPIGYYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  82 KLQEVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGR-KVIreANKPYSGTAVIDDFGPRQMETGELII 160
Cdd:PRK05362  76 KAQEVSSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRpGIL--GNKHASGTEIIDELGEEHMKTGKPIV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 161 YTSADPVLQIAAHEDIIPLEELYRICEYARSITMERPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKLDQA 240
Cdd:PRK05362 154 YTSADSVFQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVGEPGNFTRTGNRHDYALKPPAPTVLDKLKEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 241 GIDTYAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlSEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDER 320
Cdd:PRK05362 234 GGEVIAVGKIADIFAGQGITEKV-KTKSNMDGMDATIEEMK-EAGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDAR 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 321 LPEIISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPVGHFADISATVADNFGVDTAMIGESFLQ 400
Cdd:PRK05362 312 LPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGGSLGHRETFADIGATIADNFGVEPMEYGKSFLD 391


                 ...
gi 445999332 401 DLV 403
Cdd:PRK05362 392 ELK 394
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
4-400 0e+00

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 649.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   4 FDRIHLVVLDSVGIGAAPDANDFvnagvPDGASDTLGHISKTVG-LAVPNMAKIGLGNIPRpqaLKTVPAEENPSGYATK 82
Cdd:COG1015    1 MKRAILIVLDSVGIGEAPDAAKF-----GDEGANTLGHIAEAVGgLNLPNLARLGLGNIAP---LAGLPPVEEPLGAYGK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  83 LQEVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGRKVIreANKPYSGTAVIDDFGPRQMETGELIIYT 162
Cdd:COG1015   73 MAEVSAGKDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVL--GNKPASGTEIIEELGEEHMRTGKPIVYT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 163 SADPVLQIAAHEDIIPLEELYRICEYARSITMErPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKLDQAGI 242
Cdd:COG1015  151 SADSVFQIAAHEEVFPLEELYRLCEIARELLDG-EYAVGRVIARPFVGEPGNFVRTANRHDYALKPPGPTLLDRLKEAGG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 243 DTYAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlsEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDERLP 322
Cdd:COG1015  230 DVIAVGKISDIFAGRGITESV-KTKGNADGMDKTLEAMD--EAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLP 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445999332 323 EIISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPV-GHFADISATVADNFGVDTAMIGESFLQ 400
Cdd:COG1015  307 ELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTrETFADIGATIADHFGVPPPGHGTSFLS 385
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 6-398 0e+00

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: 591.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   6 RIHLVVLDSVGIGAAPDANDFvnagvPDGASDTLGHISKTV-GLAVPNMAKIGLGNIPRpqaLKTVPAEENPSGYATKLQ 84
Cdd:cd16009    2 RVILIVLDSFGIGAMPDAAKF-----GDEGANTLGHIAEAVpGLNLPNLEKLGLGNIVG---IEGGPPKENPIAAYGKMR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  85 EVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGRKVIReaNKPYSGTAVIDDFGPRQMETGELIIYTSA 164
Cdd:cd16009   74 EASAGKDTTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLG--NKPASGTEIIKELGEEHLKTGAPIVYTSA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 165 DPVLQIAAHEDIIPLEELYRICEYARSITMErPALLGRIIARPYVGEPG-NFTRTANRHDYAVSPFEDTVLNKLDQAGID 243
Cdd:cd16009  152 DSVFQIAAHEEVIPLEELYRICEIAREILDG-EYKVGRVIARPFVGETGvYFKRTSNRHDYALVPPGKTVLDILKEAGIP 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 244 TYAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlsEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDERLPE 323
Cdd:cd16009  231 VIGIGKIADIFAGRGITESI-HTKSNADGMEKTLEALK--EDFNGLIFTNLVDFDMLYGHRRDPEGYAEALEEFDRRLPE 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445999332 324 IISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPVGHFADISATVADNFGVDTAMIGESF 398
Cdd:cd16009  308 LLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLKGVNLGTRETFADIGATIADNFGVEPPENGTSF 382
deoB TIGR01696
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ...
 6-397 7.63e-174

phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 162494  Cd Length: 381  Bit Score: 490.17  E-value: 7.63e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332    6 RIHLVVLDSVGIGAAPDANDFVNAGvpdgaSDTLGHISKTV-GLAVPNMAKIGLGNIPRPqalKTVPAEENPSGYATKLQ 84
Cdd:TIGR01696   1 RVFLIVMDSVGIGEAPDAADFGDEG-----AHTLGHIAEACaKLNLPNLTKLGLGKIHEP---AGVDGNEEPIAYYAKAH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   85 EVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGRKVIreANKPYSGTAVIDDFGPRQMETGELIIYTSA 164
Cdd:TIGR01696  73 EASSGKDTMTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYL--GNKPASGTVILDELGEEHMKTGKLIVYTSA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  165 DPVLQIAAHEDIIPLEELYRICEYARSITMERPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKLDQAGIDT 244
Cdd:TIGR01696 151 DSVLQIAAHEETFPLEELYEICEIARELTTDPKYNIGRIIARPFVGEPGNFQRTGNRHDYALKPFAPTVLQKLKDEGHDV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  245 YAVGKINDIFNGSGINHDMgHNKSNSHGIDTLIKTMGlsEFEKGFSFTNLVDFDALYGHRRDPHGYRDCLHEFDERLPEI 324
Cdd:TIGR01696 231 ISIGKIADIYDGEGITKKV-RTTSNMDGMDATIKEMK--EDFTGISFTNLVDFDALWGHRRDVAGYAAALELFDRRLPEL 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445999332  325 ISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIPVGH-FADISATVADNFGVDTAMIGES 397
Cdd:TIGR01696 308 FSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKPGHSLGHREtFADIGATIADNFGTSDPEYGKS 381
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 6-390 4.42e-65

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: 213.42  E-value: 4.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332    6 RIHLVVLDSVGIGAAPDANdfvnagvpdgaSDTLGHISKTvglavPNMAKIglgniprpqaLKTVPAEEN-PSGYA-TKL 83
Cdd:pfam01676   2 KVVLIVLDGWGDRPAEDLN-----------AKTPLHIAKT-----PNMDKL----------AKEYPEQLIgASGLAvGLP 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   84 QEVSLGKDTmtGHWEIMGLNITEPFDTFWNGFPEDIITKIEDFSGRKVIREANKPYSGtaVIDDFGPRQMETGELIIYTS 163
Cdd:pfam01676  56 EGQMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHL--HGLGLDSGGGVHSHIEHLLA 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  164 ADPVLQIAAHEDIIPLEEL------YRICEYARSITMERPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFEDTVLNKL 237
Cdd:pfam01676 132 LIALAKEAGAIKVHLLGDGddrpvgYILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKL 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  238 DQAGIDTYAVGKINDIFNGSGIN------------------------------------------HDMGHNKSNSHGIDT 275
Cdd:pfam01676 212 PSAGAFVPEEGKNTDGEVLEGHGlkqlriaetekyahvtffwgggreppfpgeerylipspkvatYDLQPEMSAMEITDK 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  276 LIKTMgLSEFEkgFSFTNLVDFDALyGHRRDPHGYRDCLHEFDERLPEIISAMRDKD-LLLITADHGNDPTYAGTDHTRE 354
Cdd:pfam01676 292 LLEAL-KEKYD--FVFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDTDHTRE 367

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 445999332  355 YIPLLAYSPSFT------GNGLIPVGHFADISATVADNFGVD 390
Cdd:pfam01676 368 PVPILIYGKGVRpdqvlfGEKFRERGGLADIAATILMLLGLK 409
PRK12383 PRK12383
putative mutase; Provisional
 6-402 3.37e-43

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 155.51  E-value: 3.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332   6 RIHLVVLDSVGIGAAPDANDfVNAGvpDGASDTLGHISKTVG-LAVPNMAKIGLGNIpRPQAlKTVPAEENPSGYAT-KL 83
Cdd:PRK12383   3 RFVVLVIDSFGVGAMKDVTL-VRPQ--DAGANTCGHILSQLPhLQLPTLEKLGLINA-LGYA-PGDMQPSPSATWGVaEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332  84 QEvsLGKDTMTGHWEIMGlniTEPFDTFWNGFpEDIITKIEDF---SGRKV-IREANKPY---SGTAVIDDfgprQMEtg 156
Cdd:PRK12383  78 QH--EGADTFMGHQEIMG---TRPLPPLRMPF-SDVIDRVEQAlesAGYQVeRRGDGLQFllvNQAVAIGD----NLE-- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 157 eliiytsADP--VLQIAAHEDIIPLEELYRICEYARS-ITMERPALLG-------RIIARPYVGEPG----NFTRTAN-- 220
Cdd:PRK12383 146 -------ADLgqVYNVTANLSVISFDDALKIGRIVREqVQVGRVIVFGglltdsqRILDAAESKEGRfigiNAPKSGVyd 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 221 -----RH-DYAVSPfEDTVLNKLDQAGIDTYAVGKINDIfngsgINHDMGHNKSNSHGIDTLIKTM--GLSEFEKGFSFT 292
Cdd:PRK12383 219 ngyqvVHlGYGVDP-KVQVPQKLYEAGVPVVLVGKVADI-----VNNPYGVSWQNLVDTQRVMDITldEFNTHPTAFICT 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 293 NLVDFDaLYGHRRDPHGYRDCLHEFDERLPEIISAMRDKDLLLITADHGNDPTYAGTDHTREYIPLLAYSPSFTGNGLIP 372
Cdd:PRK12383 293 NIQETD-LAGHAEDVARYAERLEVVDRNLARLLEAMTPDDCLVVMADHGNDPTIGHSHHTREVVPLLVYQKGLQATQLGV 371

                        410       420       430
                 ....*....|....*....|....*....|
gi 445999332 373 VGHFADISATVADNFGVDTAMIGESFLQDL 402
Cdd:PRK12383 372 RTTLSDVGATVCEFFGAPPPQNGRSFLSSL 401
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 209-387 1.47e-12

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: 66.68  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 209 VGEPGNFTRTANRHDYAVSPFEDTVLNKLDQAGIDTYAVGkindifngsgiNHDMGHNKSNSHgidtliktmglsefeKG 288
Cdd:cd00016   68 YTGNGSADPELPSRAAGKDEDGPTIPELLKQAGYRTGVIG-----------LLKAIDETSKEK---------------PF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 289 FSFTNLVDFD-ALYGHRRDPHGYRDCLHEFDERLPEIISAMRDK-----DLLLITADHGNDP----------TYAGTDHT 352
Cdd:cd00016  122 VLFLHFDGPDgPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAgdaddTVIIVTADHGGIDkghggdpkadGKADKSHT 201

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 445999332 353 REYIPLLAYSPSFTGNGLIP-VGHFADISATVADNF 387
Cdd:cd00016  202 GMRVPFIAYGPGVKKGGVKHeLISQYDIAPTLADLL 237
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 227-399 1.77e-07

uncharacterized sulfatase subfamily; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 52.17  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 227 SPFEDTVLNKLDQAGIDTYAVGKINDIFNGSGINHdmghnksnshGIDTLIKTMGLSEFEKGFSFT-------NLVDF-D 298
Cdd:cd16148   73 EPDDPTLAEILRKAGYYTAAVSSNPHLFGGPGFDR----------GFDTFEDFRGQEGDPGEEGDEraervtdRALEWlD 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 299 ALYGHRR--------DPHG---YRDCLHEFDERLPEIISAMRDKDLL-----LITADHG---NDPTYAGTDHTREY---- 355
Cdd:cd16148  143 RNADDDPfflflhyfDPHEpylYDAEVRYVDEQIGRLLDKLKELGLLedtlvIVTSDHGeefGEHGLYWGHGSNLYdeql 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 445999332 356 -IPLLAYSPSFTGNGLI--PVGHfADISATVADNFGVDTA--MIGESFL 399
Cdd:cd16148  223 hVPLIIRWPGKEPGKRVdaLVSH-IDIAPTLLDLLGVEPPdySDGRSLL 270
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
 302-363 1.37e-05

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: 46.70  E-value: 1.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445999332 302 GHRRDPHGYRDCLHEFDERLPEIISA--MRDKDLLLITADHgndPTYAGT-DHTREYIPLLAYSP 363
Cdd:cd16011  271 GHDGDPEAKVKAIERIDKAIVGPLLEllDGEDFVIVVTPDH---STPCSLkTHSGDPVPFLIYGP 332
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 231-341 5.25e-04

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 41.66  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 231 DTVLNKLDQAGIDTYAVG----------KINDIFNGSGINHDMGHNKSNSHGIDTLIKTmgLSEFEKGFSFTNLVDFDAl 300
Cdd:COG1524  119 PTIFERARAAGLTTAAVFwpsfegsgliDAARPYPYDGRKPLLGNPAADRWIAAAALEL--LREGRPDLLLVYLPDLDY- 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 445999332 301 YGHRRDPHG--YRDCLHEFDERLPEIISAMRDKD-----LLLITADHG 341
Cdd:COG1524  196 AGHRYGPDSpeYRAALREVDAALGRLLDALKARGlyegtLVIVTADHG 243
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 318-400 4.12e-03

Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440460  Cd Length: 511  Bit Score: 39.27  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 318 DERLPEIISAMRDKD-LLLITADHGN-----DPTYAG--TDHTREYIPLLAYSPSFtGNGLIPVGHFADISATVADNFGV 389
Cdd:COG0696  419 DECLGRVVDAVLAAGgTLLITADHGNaeqmiDPDTGGphTAHTTNPVPFILVGGDK-GVKLREDGRLADIAPTILELMGL 497

                         90
                 ....*....|...
gi 445999332 390 D--TAMIGESFLQ 400
Cdd:COG0696  498 PqpAEMTGKSLIE 510
ALP cd16012
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ...
 302-368 6.01e-03

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: 38.18  E-value: 6.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445999332 302 GHRRDPHGyrdCLHE---FDERLPEIIS-AMRDKD-LLLITADHgndptyaGTDHTREYIPLLAYSPS---FTGN 368
Cdd:cd16012  204 GHANDAAR---AIEEtlaFDKAVKVALDfAKKDGDtLVIVTADH-------ETGHTGEDVPVFAYGPGaelFGGV 268
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 237-401 9.41e-03

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 38.10  E-value: 9.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 237 LDQAGIDTYAV-------GKINDIFNGSGINH-----DMGHNKSNSHGI---DTLIKTMG-LSEFEKGFsFTNLV----- 295
Cdd:COG1368  318 LKKQGYETSFFhggdgsfWNRDSFYKNLGFDEfydreDFDDPFDGGWGVsdeDLFDKALEeLEKLKKPF-FAFLItlsnh 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445999332 296 ---DFDALYGHRRD-----PHGYRDCLHEFDERLPEIISAMRDKD-----LLLITADHG---NDPTYAGTDHTREYIPLL 359
Cdd:COG1368  397 gpyTLPEEDKKIPDygkttLNNYLNAVRYADQALGEFIEKLKKSGwydntIFVIYGDHGprsPGKTDYENPLERYRVPLL 476

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 445999332 360 AYSPSFTGNGLI--PVGHFaDISATVADNFGVDTA---MIGESFLQD 401
Cdd:COG1368  477 IYSPGLKKPKVIdtVGSQI-DIAPTLLDLLGIDYPsyyAFGRDLLSP 522
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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