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Conserved domains on  [gi|53749168|gb|AAU90069|]
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At4g01000 [Arabidopsis thaliana]

Protein Classification

Ubl1_cv_Nsp3_N-like and Telomere_Sde2_2 domain-containing protein( domain architecture ID 13219224)

Ubl1_cv_Nsp3_N-like and Telomere_Sde2_2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 10-156 3.40e-22

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member pfam13019:

Pssm-ID: 475130  Cd Length: 165  Bit Score: 92.46  E-value: 3.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53749168    10 QFFVRLLDGKSL--TLSFSSP-LAYGEQIKQRIFEQTKIPTHLQ---RLISGGY-------QISDGSAISQPDATVNLVL 76
Cdd:pfam13019   2 NVLLSSFPGLSLppTLSLTLPsTATVSDLTDRLSSRLPESLLSSlilTTTSNKQlapssdtPLSSLLSSSADGTFLSLRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53749168    77 S--LRGGKGGFGSLLRGGGMKAGQKKTNN---FDACRDMSGRRLRHVNAENRLQEWKDGEEGRnlEKKALEYLKKQSNKV 151
Cdd:pfam13019  82 SvrLRGGKGGFGSQLRAAGGRMSSKKKSNgenNDSCRNLDGRRLRTVNEAKALAEYLASKPEM--DKKEKEARRKRWEAV 159


                  ....*
gi 53749168   152 KQGVG 156
Cdd:pfam13019 160 VEAAE 164
SDE2_2C pfam13297
Replication stress response SDE2 C-terminal; This domain represents the C-terminal region of ...
 351-402 3.61e-20

Replication stress response SDE2 C-terminal; This domain represents the C-terminal region of the Replication stress response SDE2, a genome surveillance factor. It contains the DNA-binding SAP domain, frequently found in proteins involved in DNA repair. SDE2 C-terminal domain must be cleaved from its N-terminal at a diglycine motif within the ubiquitin-like fold, after Proliferating cell nuclear antigen (PCNA) interaction. This generates a functional protein that negatively regulates damage-inducible PCNA monoubiquitination, which then is proteolytically degraded to allow S phase progression and replication fork recovery in response to DNA damage.


:

Pssm-ID: 463835  Cd Length: 80  Bit Score: 84.24  E-value: 3.61e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 53749168   351 PVEPLNFDDFNSPADMEVLGMERLKTELQSRGLKCGGTLRERAARLFLLKST 402
Cdd:pfam13297  17 KAAHIDLDAFSSAEELEALGLDRLKEALMALGLKCGGTLEERAARLFSVKGL 68
 
Name Accession Description Interval E-value
Sde2_N_Ubi pfam13019
Silencing defective 2 N-terminal ubiquitin domain; Sde2 (silencing defective 2) is a ...
 10-156 3.40e-22

Silencing defective 2 N-terminal ubiquitin domain; Sde2 (silencing defective 2) is a ubiquitin-fold-containing splicing regulator that supports splicing of selected pre-mRNAs in an intron-specific manner in Schizosaccharomyces pombe. Both fission yeast and human Sde2 are translated as inactive precursor proteins harbouring the ubiquitin-fold domain linked through an invariant GGKGG motif to a C-terminal domain. The Sde2 protein has a ubiquitin-fold at its N-terminus, which must be cleaved by the ubiquitin-specific proteases (USPs) Ubp5 and Ubp15. After cleavage, the C-terminal domain of Sde2, which starts with a lysine, gets incorporated into the spliceosome. This entry represents the ubiquitin fold N-terminal domain found in Sde2 proteins.


Pssm-ID: 372432  Cd Length: 165  Bit Score: 92.46  E-value: 3.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53749168    10 QFFVRLLDGKSL--TLSFSSP-LAYGEQIKQRIFEQTKIPTHLQ---RLISGGY-------QISDGSAISQPDATVNLVL 76
Cdd:pfam13019   2 NVLLSSFPGLSLppTLSLTLPsTATVSDLTDRLSSRLPESLLSSlilTTTSNKQlapssdtPLSSLLSSSADGTFLSLRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53749168    77 S--LRGGKGGFGSLLRGGGMKAGQKKTNN---FDACRDMSGRRLRHVNAENRLQEWKDGEEGRnlEKKALEYLKKQSNKV 151
Cdd:pfam13019  82 SvrLRGGKGGFGSQLRAAGGRMSSKKKSNgenNDSCRNLDGRRLRTVNEAKALAEYLASKPEM--DKKEKEARRKRWEAV 159


                  ....*
gi 53749168   152 KQGVG 156
Cdd:pfam13019 160 VEAAE 164
SDE2_2C pfam13297
Replication stress response SDE2 C-terminal; This domain represents the C-terminal region of ...
 351-402 3.61e-20

Replication stress response SDE2 C-terminal; This domain represents the C-terminal region of the Replication stress response SDE2, a genome surveillance factor. It contains the DNA-binding SAP domain, frequently found in proteins involved in DNA repair. SDE2 C-terminal domain must be cleaved from its N-terminal at a diglycine motif within the ubiquitin-like fold, after Proliferating cell nuclear antigen (PCNA) interaction. This generates a functional protein that negatively regulates damage-inducible PCNA monoubiquitination, which then is proteolytically degraded to allow S phase progression and replication fork recovery in response to DNA damage.


Pssm-ID: 463835  Cd Length: 80  Bit Score: 84.24  E-value: 3.61e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 53749168   351 PVEPLNFDDFNSPADMEVLGMERLKTELQSRGLKCGGTLRERAARLFLLKST 402
Cdd:pfam13297  17 KAAHIDLDAFSSAEELEALGLDRLKEALMALGLKCGGTLEERAARLFSVKGL 68
Ubl_ubiquitin cd01803
ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes ...
 9-81 2.59e-10

ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like (Ubl) proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ubiquitin (Ub)and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Ub includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric multiubiquitin protein chains.


Pssm-ID: 340501 [Multi-domain]  Cd Length: 76  Bit Score: 56.30  E-value: 2.59e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53749168   9 LQFFVRLLDGKSLTLSFSsPLAYGEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLVLSLRGG 81
Cdd:cd01803   1 MQIFVKTLTGKTITLEVE-PSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSdyniQKESTLHLVLRLRGG 76
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 9-77 7.65e-07

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 46.48  E-value: 7.65e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53749168      9 LQFFVRLLDGKS--LTLSFSSPLaygEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLVLS 77
Cdd:smart00213   1 IELTVKTLDGKTitLEVKPSDTV---SELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLAdygiQDGSTIHLVLR 72
PTZ00044 PTZ00044
ubiquitin; Provisional
 9-81 1.67e-05

ubiquitin; Provisional


Pssm-ID: 185411 [Multi-domain]  Cd Length: 76  Bit Score: 42.51  E-value: 1.67e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53749168    9 LQFFVRLLDGKSLTLSFSsPLAYGEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLVLSLRGG 81
Cdd:PTZ00044   1 MQILIKTLTGKKQSFNFE-PDNTVQQVKMALQEKEGIDVKQIRLIYSGKQMSDDLKLSdykvVPGSTIHMVLQLRGG 76
 
Name Accession Description Interval E-value
Sde2_N_Ubi pfam13019
Silencing defective 2 N-terminal ubiquitin domain; Sde2 (silencing defective 2) is a ...
 10-156 3.40e-22

Silencing defective 2 N-terminal ubiquitin domain; Sde2 (silencing defective 2) is a ubiquitin-fold-containing splicing regulator that supports splicing of selected pre-mRNAs in an intron-specific manner in Schizosaccharomyces pombe. Both fission yeast and human Sde2 are translated as inactive precursor proteins harbouring the ubiquitin-fold domain linked through an invariant GGKGG motif to a C-terminal domain. The Sde2 protein has a ubiquitin-fold at its N-terminus, which must be cleaved by the ubiquitin-specific proteases (USPs) Ubp5 and Ubp15. After cleavage, the C-terminal domain of Sde2, which starts with a lysine, gets incorporated into the spliceosome. This entry represents the ubiquitin fold N-terminal domain found in Sde2 proteins.


Pssm-ID: 372432  Cd Length: 165  Bit Score: 92.46  E-value: 3.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53749168    10 QFFVRLLDGKSL--TLSFSSP-LAYGEQIKQRIFEQTKIPTHLQ---RLISGGY-------QISDGSAISQPDATVNLVL 76
Cdd:pfam13019   2 NVLLSSFPGLSLppTLSLTLPsTATVSDLTDRLSSRLPESLLSSlilTTTSNKQlapssdtPLSSLLSSSADGTFLSLRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53749168    77 S--LRGGKGGFGSLLRGGGMKAGQKKTNN---FDACRDMSGRRLRHVNAENRLQEWKDGEEGRnlEKKALEYLKKQSNKV 151
Cdd:pfam13019  82 SvrLRGGKGGFGSQLRAAGGRMSSKKKSNgenNDSCRNLDGRRLRTVNEAKALAEYLASKPEM--DKKEKEARRKRWEAV 159


                  ....*
gi 53749168   152 KQGVG 156
Cdd:pfam13019 160 VEAAE 164
SDE2_2C pfam13297
Replication stress response SDE2 C-terminal; This domain represents the C-terminal region of ...
 351-402 3.61e-20

Replication stress response SDE2 C-terminal; This domain represents the C-terminal region of the Replication stress response SDE2, a genome surveillance factor. It contains the DNA-binding SAP domain, frequently found in proteins involved in DNA repair. SDE2 C-terminal domain must be cleaved from its N-terminal at a diglycine motif within the ubiquitin-like fold, after Proliferating cell nuclear antigen (PCNA) interaction. This generates a functional protein that negatively regulates damage-inducible PCNA monoubiquitination, which then is proteolytically degraded to allow S phase progression and replication fork recovery in response to DNA damage.


Pssm-ID: 463835  Cd Length: 80  Bit Score: 84.24  E-value: 3.61e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 53749168   351 PVEPLNFDDFNSPADMEVLGMERLKTELQSRGLKCGGTLRERAARLFLLKST 402
Cdd:pfam13297  17 KAAHIDLDAFSSAEELEALGLDRLKEALMALGLKCGGTLEERAARLFSVKGL 68
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 11-79 1.88e-11

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 59.49  E-value: 1.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53749168    11 FFVRLLDGKSLTLSFSsPLAYGEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLVLSLR 79
Cdd:pfam00240   1 ITVKTLDGKKITLEVD-PTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGeygiEDGSTIHLVLRQR 72
Ubl_ubiquitin cd01803
ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes ...
 9-81 2.59e-10

ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like (Ubl) proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ubiquitin (Ub)and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Ub includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric multiubiquitin protein chains.


Pssm-ID: 340501 [Multi-domain]  Cd Length: 76  Bit Score: 56.30  E-value: 2.59e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53749168   9 LQFFVRLLDGKSLTLSFSsPLAYGEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLVLSLRGG 81
Cdd:cd01803   1 MQIFVKTLTGKTITLEVE-PSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSdyniQKESTLHLVLRLRGG 76
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 11-75 4.14e-07

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 46.82  E-value: 4.14e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53749168  11 FFVRLLDGKSLTLSFSsPLAYGEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLV 75
Cdd:cd17039   1 ITVKTLDGKTYTVEVD-PDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSdygiKDGSTIHLV 68
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 9-77 7.65e-07

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 46.48  E-value: 7.65e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53749168      9 LQFFVRLLDGKS--LTLSFSSPLaygEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLVLS 77
Cdd:smart00213   1 IELTVKTLDGKTitLEVKPSDTV---SELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLAdygiQDGSTIHLVLR 72
Ubl_AtUPL5_like cd16107
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) ...
 10-75 8.85e-07

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) and similar proteins; Arabidopsis thaliana AtUPL5, also termed HECT-type E3 ubiquitin transferase UPL5, is an E3 ubiquitin-protein ligase that contains a ubiquitin-like domain (Ubl), a C-type lectin-binding domain, a leucine zipper and a HECT domain. HECT domain containing-ubiquitin-protein ligases have more than one member in different genomes, these proteins have been classified into four sub-families (UPL1/2, UPL3/4, UPL5 and UPL6/7). AtUPL5 fUPL5 regulates leaf senescence in Arabidopsis through degradation of the transcription factor WRKY53.


Pssm-ID: 340524  Cd Length: 70  Bit Score: 45.95  E-value: 8.85e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53749168  10 QFFVRLLDGKSLTLSfSSPLAYGEQIKQRIFEQTKIPTHLQRLISGGYQISDG----SAISQPDATVNLV 75
Cdd:cd16107   1 QIFVRTYCGKTIVLH-AKASDTVESLHQQIEARTGIPSLEQRLIFGGRQLQHSqsleSCKMENDATLFLV 69
Ubl_NEDD8 cd01806
ubiquitin-like (Ubl) domain found in neural precursor cell expressed developmentally ...
 13-81 5.64e-06

ubiquitin-like (Ubl) domain found in neural precursor cell expressed developmentally down-regulated protein 8 (NEDD8) and similar proteins; NEDD8, also termed Neddylin, or RELATED TO UBIQUITIN (RUB/Rub1p) in plant and yeast, is a ubiquitin-like protein that conjugates to nuclear proteins in a manner analogous to ubiquitination and sentrinization. It modifies a family of molecular scaffold proteins called cullins that are responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. NEDD8 deamidation and its inhibition of Cullin-RING ubiquitin ligases (CRLs) activity are responsible for Cycle-inhibiting factor (Cif)/Cif homolog in Burkholderia pseudomallei (CHBP)-induced cytopathic effect. NEDD8 contains a single conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Polyubiquitination, signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. Ubl NEDD8, contains many of the same lysines (K6, K11, K27, K33, K48) as Ub, where K27 has an role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340504 [Multi-domain]  Cd Length: 74  Bit Score: 43.92  E-value: 5.64e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53749168  13 VRLLDGKSLTLSFSsPLAYGEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLVLSLRGG 81
Cdd:cd01806   3 VKTLTGKEIEIDIE-PTDKVERIKERVEEKEGIPPQQQRLIFSGKQMNDEKTAAdykiEGGSVLHLVLALRGG 74
PTZ00044 PTZ00044
ubiquitin; Provisional
 9-81 1.67e-05

ubiquitin; Provisional


Pssm-ID: 185411 [Multi-domain]  Cd Length: 76  Bit Score: 42.51  E-value: 1.67e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53749168    9 LQFFVRLLDGKSLTLSFSsPLAYGEQIKQRIFEQTKIPTHLQRLISGGYQISDGSAIS----QPDATVNLVLSLRGG 81
Cdd:PTZ00044   1 MQILIKTLTGKKQSFNFE-PDNTVQQVKMALQEKEGIDVKQIRLIYSGKQMSDDLKLSdykvVPGSTIHMVLQLRGG 76
 
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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