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Conserved domains on  [gi|1254064715|ref|NP_001343878|]
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dihydropyrimidinase-related protein 5 isoform b [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 10-87 2.70e-31

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


The actual alignment was detected with superfamily member cd01314:

Pssm-ID: 469705 [Multi-domain]  Cd Length: 447  Bit Score: 113.47  E-value: 2.70e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTK 87
Cdd:cd01314     1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTR 78
 
Name Accession Description Interval E-value
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 10-87 2.70e-31

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 113.47  E-value: 2.70e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTK 87
Cdd:cd01314     1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTR 78
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 10-87 9.73e-29

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937 [Multi-domain]  Cd Length: 454  Bit Score: 106.70  E-value: 9.73e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTK 87
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTK 78
PRK08323 PRK08323
phenylhydantoinase; Validated
 9-87 2.16e-27

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 102.94  E-value: 2.16e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1254064715   9 RILIKGGKVVNDDCTHEADVYIESGIIQQVGRelmiPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTK 87
Cdd:PRK08323    2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGA----NLGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTR 76
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 11-87 4.89e-22

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 88.22  E-value: 4.89e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1254064715  11 LIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMnaTCVDDFYHGTK 87
Cdd:COG0044     1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTR 75
Amidohydro_3 pfam07969
Amidohydrolase family;
49-95 3.50e-05

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 40.59  E-value: 3.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1254064715  49 KVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKQVFRFTVE 95
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAVVKGQAG 47
 
Name Accession Description Interval E-value
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 10-87 2.70e-31

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 113.47  E-value: 2.70e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTK 87
Cdd:cd01314     1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTR 78
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 10-87 9.73e-29

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937 [Multi-domain]  Cd Length: 454  Bit Score: 106.70  E-value: 9.73e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTK 87
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTK 78
PRK08323 PRK08323
phenylhydantoinase; Validated
 9-87 2.16e-27

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 102.94  E-value: 2.16e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1254064715   9 RILIKGGKVVNDDCTHEADVYIESGIIQQVGRelmiPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTK 87
Cdd:PRK08323    2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGA----NLGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTR 76
PLN02942 PLN02942
dihydropyrimidinase
 7-86 4.81e-26

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 99.53  E-value: 4.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254064715   7 SVRILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGT 86
Cdd:PLN02942    4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 11-87 4.89e-22

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 88.22  E-value: 4.89e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1254064715  11 LIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMnaTCVDDFYHGTK 87
Cdd:COG0044     1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTR 75
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 12-86 4.51e-19

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 80.13  E-value: 4.51e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1254064715  12 IKGGKVVNDDCTHEADVYIESGIIQQVGRELmiPGGAKVIDATGKLVIPGGIDTSTHFHQ-TFMNATCVDDFYHGT 86
Cdd:PRK13404    8 IRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQpSGDGIMMADDFYTGT 81
PRK09236 PRK09236
dihydroorotase; Reviewed
 9-69 4.22e-14

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 66.05  E-value: 4.22e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254064715   9 RILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHF 69
Cdd:PRK09236    3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHF 63
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 3-69 1.91e-12

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 61.13  E-value: 1.91e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254064715   3 ANSASVRILIKGGKVV---NDDCTHEADVYIESGIIQQVGR--ELMIPGGAKVIDATGKLVIPGGIDTSTHF 69
Cdd:COG1228     3 APAQAGTLLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHL 74
PRK02382 PRK02382
dihydroorotase; Provisional
 10-71 2.11e-12

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 61.21  E-value: 2.11e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQ 71
Cdd:PRK02382    4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFRE 65
PRK06189 PRK06189
allantoinase; Provisional
 10-71 2.76e-12

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 60.87  E-value: 2.76e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPgGAKVIDATGKLVIPGGIDTSTHFHQ 71
Cdd:PRK06189    5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSP-AREIIDADGLYVFPGMIDVHVHFNE 65
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
10-68 3.41e-12

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 60.25  E-value: 3.41e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254064715  10 ILIKGGKVVNDDCTHEA--DVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:PRK09237    1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 9-74 5.81e-12

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 59.84  E-value: 5.81e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254064715   9 RILIKGGKVVNDDCTHE----ADVYIESGIIQQVGRELMIP---GGAKVIDATGKLVIPGGIDTSTHFHQTFM 74
Cdd:COG0402     1 DLLIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLPQTLL 73
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 11-87 1.10e-11

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 59.23  E-value: 1.10e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1254064715  11 LIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTK 87
Cdd:cd01315     3 VIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINE--PGRTEWEGFETGTK 77
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 10-74 2.93e-11

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 57.98  E-value: 2.93e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254064715  10 ILIKGGKVVNDDCTHE---ADVYIESGIIQQVGR--ELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFM 74
Cdd:cd01298     1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPalPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLL 70
pyrC PRK09357
dihydroorotase; Validated
 9-69 1.06e-10

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 56.36  E-value: 1.06e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254064715   9 RILIKGGKVVNDDCTHE-ADVYIESGIIQQVGRELmIPGGAKVIDATGKLVIPGGIDTSTHF 69
Cdd:PRK09357    2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENI-EAEGAEVIDATGLVVAPGLVDLHVHL 62
PRK08204 PRK08204
hypothetical protein; Provisional
 9-81 1.69e-10

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 55.78  E-value: 1.69e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1254064715   9 RILIKGGKVVNDDCTH----EADVYIESGIIQQVGRELMiPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDD 81
Cdd:PRK08204    3 RTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPSIE-APDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADW 78
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 10-75 4.51e-10

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 54.61  E-value: 4.51e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254064715  10 ILIKGGKVVndDCT----HEADVYIESGIIQQVGRELmIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMN 75
Cdd:cd01297     2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPIL-STSAREVIDAAGLVVAPGFIDVHTHYDGQVFW 68
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
9-72 5.72e-10

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 54.24  E-value: 5.72e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1254064715   9 RILIKGGKVVNDDCTHE---ADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK07228    2 TILIKNAGIVTMNAKREivdGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQT 68
PRK09060 PRK09060
dihydroorotase; Validated
 11-69 9.27e-10

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 53.39  E-value: 9.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254064715  11 LIKGGKVVNDDCTHEADVYIESGIIQQVGrELMIPGGAKVIDATGKLVIPGGIDTSTHF 69
Cdd:PRK09060    8 ILKGGTVVNPDGEGRADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHF 65
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
10-68 1.03e-09

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 440842  Cd Length: 554  Bit Score: 53.27  E-value: 1.03e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254064715  10 ILIKGGKVVndDCTHE-----ADVYIESG-IIQQVGRelmiPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:COG1229     3 LIIKNGRVY--DPANGidgevMDIAIKDGkIVEEPSD----PKDAKVIDASGKVVMAGGVDIHTH 61
PRK07575 PRK07575
dihydroorotase; Provisional
 9-69 1.65e-09

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 52.75  E-value: 1.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254064715   9 RILIKGGKVVNDDCTHE-ADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHF 69
Cdd:PRK07575    4 SLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHF 65
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 10-68 1.86e-09

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 52.88  E-value: 1.86e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254064715  10 ILIKGGKVVNDDCTH--EADVYIESGIIQQVGRELMIPGGaKVIDATGKLVIPGGIDTSTH 68
Cdd:PRK08393    3 ILIKNGYVIYGENLKviRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTH 62
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
11-77 2.36e-09

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 52.41  E-value: 2.36e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254064715  11 LIKGGKVVNDDCTHE-ADVYIESGIIQQVGRelMIPGGAKVIDATGKLVIPGGIDtsTHFH----QTFMNAT 77
Cdd:COG1820     1 AITNARIFTGDGVLEdGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFID--LHVHggggVDFMDGT 68
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 9-72 5.57e-09

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 51.39  E-value: 5.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254064715   9 RILIKGGKVV---NDDCTHEAD--VYIESGIIQQVGRELMIPG-GAKVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK08203    2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHFYQT 71
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 10-77 3.13e-08

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 49.11  E-value: 3.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH--FHQTFMNAT 77
Cdd:cd00854     1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHggGGADFMDGT 70
PRK09061 PRK09061
D-glutamate deacylase; Validated
 1-71 4.15e-08

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 48.92  E-value: 4.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254064715   1 MLANSASVRILIKGGKVVNDDCTHEA--DVYIESGIIQQVGRELMipGGAKVIDATGKLVIPGGIDTSTHFHQ 71
Cdd:PRK09061   12 MPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAHGQS 82
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 27-71 6.80e-08

Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 48.09  E-value: 6.80e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1254064715  27 DVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQ 71
Cdd:cd01307     1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQ 45
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 10-74 2.04e-07

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 46.80  E-value: 2.04e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254064715  10 ILIKGGKVVNDDCTHE---ADVYIESGIIQQVGRelMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFM 74
Cdd:PRK06380    3 ILIKNAWIVTQNEKREilqGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTAS 68
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 10-72 3.42e-07

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 46.28  E-value: 3.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1254064715  10 ILIKGGKVVNDDC--THEADVYIESGIIQQVGRElmIPGGA-KVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK06038    4 IIIKNAYVLTMDAgdLKKGSVVIEDGTITEVSES--TPGDAdTVIDAKGSVVMPGLVNTHTHAAMT 67
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
1-80 4.08e-07

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 45.95  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254064715   1 MLANSASVRILIKGGKV--VNDDC-THEAdVYIESGIIQQVG--RELM--IPGGAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:COG1574     1 MKLAAAAADLLLTNGRIytMDPAQpVAEA-VAVRDGRIVAVGsdAEVRalAGPATEVIDLGGKTVLPGFIDAHVHLLGGG 79


                  ....*..
gi 1254064715  74 MNATCVD 80
Cdd:COG1574    80 LALLGVD 86
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
10-70 5.49e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 45.86  E-value: 5.49e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1254064715  10 ILIKGGKVVNDdCTHE---ADVYIESGIIQQVGRElmIPGGAKVIDATGKLVIPGGIDtsTHFH 70
Cdd:COG1001     7 LVIKNGRLVNV-FTGEileGDIAIAGGRIAGVGDY--IGEATEVIDAAGRYLVPGFID--GHVH 65
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 33-68 5.62e-07

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 45.77  E-value: 5.62e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1254064715  33 GIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:cd01309     2 GKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
PRK07203 PRK07203
putative aminohydrolase SsnA;
10-73 8.03e-07

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 45.31  E-value: 8.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254064715  10 ILIKGGKVVNDDCTH----EADVYIESGIIQQVGRELMIPG---GAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:PRK07203    2 LLIGNGTAITRDPAKpvieDGAIAIEGNVIVEIGTTDELKAkypDAEFIDAKGKLIMPGLINSHNHIYSGL 72
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
 12-68 9.11e-07

Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.


Pssm-ID: 238629 [Multi-domain]  Cd Length: 541  Bit Score: 45.10  E-value: 9.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254064715  12 IKGGKVVndDCTHE-----ADVYIESGIIQQvgrELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:cd01304     1 IKNGTVY--DPLNGingekMDIFIRDGKIVE---SSSGAKPAKVIDASGKVVMAGGVDMHSH 57
PRK09228 PRK09228
guanine deaminase; Provisional
 24-74 1.60e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 44.41  E-value: 1.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1254064715  24 HEAD--VYIESGIIQQVG--RELM--IPGGAKVIDATGKLVIPGGIDTSTHFHQTFM 74
Cdd:PRK09228   28 YIEDglLLVEDGRIVAAGpyAELRaqLPADAEVTDYRGKLILPGFIDTHIHYPQTDM 84
PRK05985 PRK05985
cytosine deaminase; Provisional
 26-73 3.96e-06

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 43.38  E-value: 3.96e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1254064715  26 ADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:PRK05985   17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTF 64
PRK04250 PRK04250
dihydroorotase; Provisional
 15-69 6.36e-06

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 42.83  E-value: 6.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1254064715  15 GKVVNDDCTHEADVYIESGIIQQVGRELMipGGAKVIDATGKLVIPGGIDTSTHF 69
Cdd:PRK04250    4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHL 56
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 28-69 7.76e-06

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 42.25  E-value: 7.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1254064715  28 VYIESGIIQQVGRELMIPG----GAKVIDATGKLVIPGGIDTSTHF 69
Cdd:cd01296     1 IAIRDGRIAAVGPAASLPApgpaAAEEIDAGGRAVTPGLVDCHTHL 46
PRK09059 PRK09059
dihydroorotase; Validated
 27-64 7.83e-06

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 42.33  E-value: 7.83e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1254064715  27 DVYIESGIIQQVGRELM---IPGGAKVIDATGKLVIPGGID 64
Cdd:PRK09059   24 TVLIEDGVIVAAGKGAGnqgAPEGAEIVDCAGKAVAPGLVD 64
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 26-70 1.30e-05

Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 41.85  E-value: 1.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1254064715  26 ADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDtsTHFH 70
Cdd:cd01293    15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVD--PHIH 57
PRK07627 PRK07627
dihydroorotase; Provisional
 9-71 1.49e-05

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 41.59  E-value: 1.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254064715   9 RILIKGGKVVNDDCTHE--ADVYIESGIIQQVGRelmIPGG---AKVIDATGKLVIPGGIDTSTHFHQ 71
Cdd:PRK07627    2 KIHIKGGRLIDPAAGTDrqADLYVAAGKIAAIGQ---APAGfnaDKTIDASGLIVCPGLVDLSARLRE 66
PRK08044 PRK08044
allantoinase AllB;
10-68 2.42e-05

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 40.99  E-value: 2.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254064715  10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELmiPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:PRK08044    5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTH 61
Amidohydro_3 pfam07969
Amidohydrolase family;
49-95 3.50e-05

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 40.59  E-value: 3.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1254064715  49 KVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKQVFRFTVE 95
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAVVKGQAG 47
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 9-64 1.27e-04

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 39.01  E-value: 1.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254064715   9 RILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAkvIDATGKLVIPGGID 64
Cdd:PRK15446    3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVD 56
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 11-70 1.94e-04

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 38.52  E-value: 1.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254064715  11 LIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAK--VIDATGKLVIPGGIDtsTHFH 70
Cdd:cd01308     3 LIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENvtVVDLHGKILVPGFID--QHVH 62
PRK07572 PRK07572
cytosine deaminase; Validated
 26-77 5.39e-04

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 37.31  E-value: 5.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1254064715  26 ADVYIESGIIQQVGRELMIPGGAkVIDATGKLVIPGGIDtsTHFHqtfMNAT 77
Cdd:PRK07572   18 IDIGIAGGRIAAVEPGLQAEAAE-EIDAAGRLVSPPFVD--PHFH---MDAT 63
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 47-69 6.23e-04

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 36.83  E-value: 6.23e-04
                          10        20
                  ....*....|....*....|...
gi 1254064715  47 GAKVIDATGKLVIPGGIDTSTHF 69
Cdd:cd01317     1 DAEVIDAEGKILAPGLVDLHVHL 23
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 27-80 1.63e-03

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 35.75  E-value: 1.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1254064715  27 DVYIESGIIQQVGR--ELM--IPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVD 80
Cdd:cd01300     1 AVAVRDGRIVAVGSdaEAKalKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLD 58
ureC PRK13207
urease subunit alpha; Reviewed
 26-69 6.05e-03

urease subunit alpha; Reviewed


Pssm-ID: 237305 [Multi-domain]  Cd Length: 568  Bit Score: 34.38  E-value: 6.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1254064715  26 ADVYIESGIIQQVGR----------ELMIPGGAKVIDATGKLVIPGGIDTSTHF 69
Cdd:PRK13207   85 ADIGIKDGRIVAIGKagnpdiqdgvDIIIGPGTEVIAGEGLIVTAGGIDTHIHF 138
 
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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