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Conserved domains on  [gi|23396828|sp|Q9Y3Y4|]
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RecName: Full=Pygopus homolog 1

Protein Classification

pygopus homolog 1( domain architecture ID 10204332)

pygopus homolog 1 (PYGO1) functions as a context-dependent beta-catenin coactivator, and binds di- and trimethylated lysine 4 of histone H3 (H3K4me2/3)

Gene Symbol:  PYGO1
Gene Ontology:  GO:0005515|GO:0008270|GO:0035064

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHD_PYGO1 cd15635
PHD finger found in pygopus homolog 1 (PYGO1); PYGO1 is a homolog of Drosophila melanogaster ...
341-397 5.59e-41

PHD finger found in pygopus homolog 1 (PYGO1); PYGO1 is a homolog of Drosophila melanogaster protein pygopus (dPYGO), which is a fundamental Wnt signaling transcriptional component in Drosophila. It functions as a context-dependent beta-catenin coactivator, and binds di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts as an adaptor between Pygopus (Pygo) and Arm/beta-catenin. PYGO1 contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway.


:

Pssm-ID: 277105  Cd Length: 57  Bit Score: 139.46  E-value: 5.59e-41
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23396828 341 YPCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTCMA 397
Cdd:cd15635   1 YPCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTCMA 57
PTZ00395 super family cl33180
Sec24-related protein; Provisional
145-357 2.36e-05

Sec24-related protein; Provisional


The actual alignment was detected with superfamily member PTZ00395:

Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 46.99  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396828   145 AFNFGPHDNSSFGNPSYNNALSQNVNMPNQHFRQNPAENfsqiPPQNASQVSNPDLAS---NFVPGNNSNFTSPLESN-- 219
Cdd:PTZ00395  378 AWAGGPHSNASYNCAAYSNAAQSNAAQSNAGFSNAGYSN----PGNSNPGYNNAPNSNtpyNNPPNSNTPYSNPPNSNpp 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396828   220 HSFIPPPNT----FGQAKAPPPKQDFTQGATKNTNQNSSAHPPHLNMDDTVNQSNIELKNVNRNNAVNQENSRSSSTEAT 295
Cdd:PTZ00395  454 YSNLPYSNTpysnAPLSNAPPSSAKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAGNSVGNPFASRPFGSAPY 533
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23396828   296 NNNPA-----NGTQNKPRQPRGAADACTTEKSNKSSLHPNRHGHSSSDpvypcgicTNEVNDDQDAI 357
Cdd:PTZ00395  534 GGNAAttadpNGIAKREDHPEGGTNRQKYEQSDEESVESSSSENSSEN--------ENEVTDKGEEI 592
 
Name Accession Description Interval E-value
PHD_PYGO1 cd15635
PHD finger found in pygopus homolog 1 (PYGO1); PYGO1 is a homolog of Drosophila melanogaster ...
341-397 5.59e-41

PHD finger found in pygopus homolog 1 (PYGO1); PYGO1 is a homolog of Drosophila melanogaster protein pygopus (dPYGO), which is a fundamental Wnt signaling transcriptional component in Drosophila. It functions as a context-dependent beta-catenin coactivator, and binds di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts as an adaptor between Pygopus (Pygo) and Arm/beta-catenin. PYGO1 contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway.


Pssm-ID: 277105  Cd Length: 57  Bit Score: 139.46  E-value: 5.59e-41
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23396828 341 YPCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTCMA 397
Cdd:cd15635   1 YPCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTCMA 57
PTZ00395 PTZ00395
Sec24-related protein; Provisional
145-357 2.36e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 46.99  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396828   145 AFNFGPHDNSSFGNPSYNNALSQNVNMPNQHFRQNPAENfsqiPPQNASQVSNPDLAS---NFVPGNNSNFTSPLESN-- 219
Cdd:PTZ00395  378 AWAGGPHSNASYNCAAYSNAAQSNAAQSNAGFSNAGYSN----PGNSNPGYNNAPNSNtpyNNPPNSNTPYSNPPNSNpp 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396828   220 HSFIPPPNT----FGQAKAPPPKQDFTQGATKNTNQNSSAHPPHLNMDDTVNQSNIELKNVNRNNAVNQENSRSSSTEAT 295
Cdd:PTZ00395  454 YSNLPYSNTpysnAPLSNAPPSSAKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAGNSVGNPFASRPFGSAPY 533
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23396828   296 NNNPA-----NGTQNKPRQPRGAADACTTEKSNKSSLHPNRHGHSSSDpvypcgicTNEVNDDQDAI 357
Cdd:PTZ00395  534 GGNAAttadpNGIAKREDHPEGGTNRQKYEQSDEESVESSSSENSSEN--------ENEVTDKGEEI 592
 
Name Accession Description Interval E-value
PHD_PYGO1 cd15635
PHD finger found in pygopus homolog 1 (PYGO1); PYGO1 is a homolog of Drosophila melanogaster ...
341-397 5.59e-41

PHD finger found in pygopus homolog 1 (PYGO1); PYGO1 is a homolog of Drosophila melanogaster protein pygopus (dPYGO), which is a fundamental Wnt signaling transcriptional component in Drosophila. It functions as a context-dependent beta-catenin coactivator, and binds di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts as an adaptor between Pygopus (Pygo) and Arm/beta-catenin. PYGO1 contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway.


Pssm-ID: 277105  Cd Length: 57  Bit Score: 139.46  E-value: 5.59e-41
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23396828 341 YPCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTCMA 397
Cdd:cd15635   1 YPCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTCMA 57
PHD_PYGO2 cd15636
PHD finger found in pygopus homolog 2 (PYGO2); PYGO2 is a homolog of Drosophila melanogaster ...
342-395 1.32e-33

PHD finger found in pygopus homolog 2 (PYGO2); PYGO2 is a homolog of Drosophila melanogaster protein pygopus (dPYGO), which is a fundamental Wnt signaling transcriptional component in Drosophila. It functions as a context-dependent beta-catenin coactivator, as well as a histone methylation reader that binds di-and trimethylated lysine 4 of histone H3 (H3K4me2/3). Moreover, PYGO2 acts as a chromatin remodeler in a testis-specific and Wnt-unrelated manner. It also mediates chromatin regulation and links Wnt signaling and Notch signaling to suppress the luminal/alveolar differentiation competence of mammary stem and basal cells. Furthermore, PYGO2 plays a new role in rRNA transcription during cancer cell growth. It regulates mammary tumor initiation and heterogeneity in MMTV-Wnt1 mice. PYGO2 contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway.


Pssm-ID: 277106  Cd Length: 54  Bit Score: 119.78  E-value: 1.32e-33
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 23396828 342 PCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTC 395
Cdd:cd15636   1 PCGACRSEVNDDQDAILCEASCQKWFHRECTGMTESAYGLLTTEASAVWACDFC 54
PHD_PYGO cd15551
PHD finger found in PYGO proteins; The family includes Drosophila melanogaster protein pygopus ...
342-395 9.46e-31

PHD finger found in PYGO proteins; The family includes Drosophila melanogaster protein pygopus (dPYGO) and its two homologs, PYGO1 and PYGO2. dPYGO is a fundamental Wnt signaling transcriptional component in Drosophila. PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts an adaptor between Pygopus (Pygo) and Arm/beta-catenin. dPYGO and PYGO2 function as context-dependent beta-catenin coactivators, and they bind di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). Moreover, PYGO2 acts as a histone methylation reader, and a chromatin remodeler in a testis-specific and Wnt-unrelated manner. It also mediates chromatin regulation and links Wnt signaling and Notch signaling to suppress the luminal/alveolar differentiation competence of mammary stem and basal cells. PYGO2 also plays a new role in rRNA transcription during cancer cell growth. It regulates mammary tumor initiation and heterogeneity in MMTV-Wnt1 mice. All family members contain a plant homeodomain (PHD) finger.


Pssm-ID: 277026  Cd Length: 54  Bit Score: 112.07  E-value: 9.46e-31
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 23396828 342 PCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTC 395
Cdd:cd15551   1 PCGICNNEVNDDDDAILCESSCNKWFHRTCTGLTESAYDLLTSEESAEWVCDSC 54
PHD_dPYGO cd15637
PHD finger found in Drosophila melanogaster protein pygopus (dPYGO) and similar proteins; ...
342-395 8.79e-20

PHD finger found in Drosophila melanogaster protein pygopus (dPYGO) and similar proteins; dPYGO, also termed protein gammy legs, is a nuclear adapter protein encoded by pygopus (pygo). It is a fundamental Wnt signaling transcriptional component in Drosophila, and has both Wnt-related and Wnt-independent functions. It plays a critical role in aging-related cardiac dysfunction that is canonical Wnt signaling independent. dPYGO contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway.


Pssm-ID: 277107  Cd Length: 54  Bit Score: 82.22  E-value: 8.79e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 23396828 342 PCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTC 395
Cdd:cd15637   1 PCGKCHKEVHDNDQAILCESGCNFWFHRTCTGLTEAAFHMLTKEVYAEWVCDKC 54
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
342-395 8.07e-06

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 42.92  E-value: 8.07e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23396828 342 PCGICTNEVNDDQDA-ILCEaSCQKWFHRICTGMTETAYGLLtaeasAVWGCDTC 395
Cdd:cd15517   1 VCGICNLETAAVDELwVQCD-GCDKWFHQFCLGLSNERYADE-----DKFKCPNC 49
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
343-395 2.26e-05

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 41.53  E-value: 2.26e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 23396828 343 CGICTNEVNDDQDAILCEaSCQKWFHRICTGMTETaygllTAEASAVWGCDTC 395
Cdd:cd15489   2 CIVCGKGGDLGGELLQCD-GCGKWFHADCLGPPLS-----SFVPNGKWICPVC 48
PTZ00395 PTZ00395
Sec24-related protein; Provisional
145-357 2.36e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 46.99  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396828   145 AFNFGPHDNSSFGNPSYNNALSQNVNMPNQHFRQNPAENfsqiPPQNASQVSNPDLAS---NFVPGNNSNFTSPLESN-- 219
Cdd:PTZ00395  378 AWAGGPHSNASYNCAAYSNAAQSNAAQSNAGFSNAGYSN----PGNSNPGYNNAPNSNtpyNNPPNSNTPYSNPPNSNpp 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396828   220 HSFIPPPNT----FGQAKAPPPKQDFTQGATKNTNQNSSAHPPHLNMDDTVNQSNIELKNVNRNNAVNQENSRSSSTEAT 295
Cdd:PTZ00395  454 YSNLPYSNTpysnAPLSNAPPSSAKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAGNSVGNPFASRPFGSAPY 533
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23396828   296 NNNPA-----NGTQNKPRQPRGAADACTTEKSNKSSLHPNRHGHSSSDpvypcgicTNEVNDDQDAI 357
Cdd:PTZ00395  534 GGNAAttadpNGIAKREDHPEGGTNRQKYEQSDEESVESSSSENSSEN--------ENEVTDKGEEI 592
PHD3_KDM5B cd15687
PHD finger 3 found in lysine-specific demethylase 5B (KDM5B); KDM5B, also termed Cancer/testis ...
342-378 4.55e-04

PHD finger 3 found in lysine-specific demethylase 5B (KDM5B); KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277157  Cd Length: 50  Bit Score: 38.00  E-value: 4.55e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 23396828 342 PCGICTNEVNDDQDAILCEASCQKWFHRICTGMT-ETA 378
Cdd:cd15687   3 PAVSCLQPEGEEVDWVQCDGSCNRWFHQVCVGVSaEMA 40
PHD3_KMT2B cd15593
PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
343-395 3.04e-03

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger.


Pssm-ID: 277068  Cd Length: 57  Bit Score: 35.59  E-value: 3.04e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23396828 343 CGICTN--EVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTA-EASAVWGCDTC 395
Cdd:cd15593   2 CPICLKcyEDNDYESKMMQCAKCDHWVHAKCEGLSDELYEILSSlPDSVVYSCAPC 57
PHD1_PHF14 cd15561
PHD finger 1 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
343-395 8.56e-03

PHD finger 1 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the first PHD finger.


Pssm-ID: 277036  Cd Length: 56  Bit Score: 34.34  E-value: 8.56e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23396828 343 CGICTNEVNDDQDAIL-CEaSCQKWFHRICTGMTETAYGLLTAEASAV--WGCDTC 395
Cdd:cd15561   2 CCVCLGDRSNDADEIIeCD-KCGISVHEGCYGVIDESDSSSSASSSSTepWFCEPC 56
 
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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