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Conserved domains on  [gi|321464062|gb|EFX75073|]
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hypothetical protein DAPPUDRAFT_226482 [Daphnia pulex]

Protein Classification

ubiquitin family protein( domain architecture ID 10110346)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_ElonginB cd01788
ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar ...
 6-107 1.23e-60

ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar proteins; Elongin B, also termed Elongin 18 kDa subunit, or EloB, or RNA polymerase II transcription factor SIII subunit B (SIII p18), is part of an E3 ubiquitin ligase complex called VEC that activates ubiquitination by the E2 ubiquitin-conjugating enzyme Ubc5. VEC is composed of von Hippel-Lindau tumor suppressor protein (pVHL), elongin C, cullin 2, NEDD8, and Rbx1. ElonginB binds elonginC to form the elonginBC complex which is a positive regulator of RNA polymerase II elongation factor Elongin A. The BC complex then binds VHL (von Hippel-Lindau) tumor suppressor protein to form a VCB ternary complex. Elongin B has a ubiquitin-like (Ubl) domain. Ub has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair.


:

Pssm-ID: 340486  Cd Length: 101  Bit Score: 180.95  E-value: 1.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321464062   6 CVYLMIRRKKTTIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGLISTTARAQSPASLSLAYRL 85
Cdd:cd01788    1 DVFLMIRRKKTTIFTDAKESTTVFELKKIIEGILKRPPEDQRLYKDDQLLDDTKTLGDCGFTSQTARAQAPATLGLAFRA 80

                         90       100
                 ....*....|....*....|..
gi 321464062  86 DnGEFETVDITPLSSPPELPDV 107
Cdd:cd01788   81 D-GEFEPLEITPLSSPPELPDV 101
 
Name Accession Description Interval E-value
Ubl_ElonginB cd01788
ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar ...
 6-107 1.23e-60

ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar proteins; Elongin B, also termed Elongin 18 kDa subunit, or EloB, or RNA polymerase II transcription factor SIII subunit B (SIII p18), is part of an E3 ubiquitin ligase complex called VEC that activates ubiquitination by the E2 ubiquitin-conjugating enzyme Ubc5. VEC is composed of von Hippel-Lindau tumor suppressor protein (pVHL), elongin C, cullin 2, NEDD8, and Rbx1. ElonginB binds elonginC to form the elonginBC complex which is a positive regulator of RNA polymerase II elongation factor Elongin A. The BC complex then binds VHL (von Hippel-Lindau) tumor suppressor protein to form a VCB ternary complex. Elongin B has a ubiquitin-like (Ubl) domain. Ub has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340486  Cd Length: 101  Bit Score: 180.95  E-value: 1.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321464062   6 CVYLMIRRKKTTIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGLISTTARAQSPASLSLAYRL 85
Cdd:cd01788    1 DVFLMIRRKKTTIFTDAKESTTVFELKKIIEGILKRPPEDQRLYKDDQLLDDTKTLGDCGFTSQTARAQAPATLGLAFRA 80

                         90       100
                 ....*....|....*....|..
gi 321464062  86 DnGEFETVDITPLSSPPELPDV 107
Cdd:cd01788   81 D-GEFEPLEITPLSSPPELPDV 101
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 14-66 4.60e-11

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: 54.19  E-value: 4.60e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 321464062    14 KKTTIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:smart00213   9 DGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGI 61
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 14-66 1.53e-10

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: 52.94  E-value: 1.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 321464062   14 KKTTIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:pfam00240   7 DGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGI 59
UBI4 COG5272
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
17-66 4.06e-05

Ubiquitin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444084 [Multi-domain]  Cd Length: 213  Bit Score: 40.93  E-value: 4.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 321464062  17 TIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:COG5272   12 TITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLEDDRTLADYNI 61
 
Name Accession Description Interval E-value
Ubl_ElonginB cd01788
ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar ...
 6-107 1.23e-60

ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar proteins; Elongin B, also termed Elongin 18 kDa subunit, or EloB, or RNA polymerase II transcription factor SIII subunit B (SIII p18), is part of an E3 ubiquitin ligase complex called VEC that activates ubiquitination by the E2 ubiquitin-conjugating enzyme Ubc5. VEC is composed of von Hippel-Lindau tumor suppressor protein (pVHL), elongin C, cullin 2, NEDD8, and Rbx1. ElonginB binds elonginC to form the elonginBC complex which is a positive regulator of RNA polymerase II elongation factor Elongin A. The BC complex then binds VHL (von Hippel-Lindau) tumor suppressor protein to form a VCB ternary complex. Elongin B has a ubiquitin-like (Ubl) domain. Ub has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340486  Cd Length: 101  Bit Score: 180.95  E-value: 1.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321464062   6 CVYLMIRRKKTTIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGLISTTARAQSPASLSLAYRL 85
Cdd:cd01788    1 DVFLMIRRKKTTIFTDAKESTTVFELKKIIEGILKRPPEDQRLYKDDQLLDDTKTLGDCGFTSQTARAQAPATLGLAFRA 80

                         90       100
                 ....*....|....*....|..
gi 321464062  86 DnGEFETVDITPLSSPPELPDV 107
Cdd:cd01788   81 D-GEFEPLEITPLSSPPELPDV 101
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 14-66 4.60e-11

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: 54.19  E-value: 4.60e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 321464062    14 KKTTIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:smart00213   9 DGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGI 61
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 14-66 1.53e-10

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: 52.94  E-value: 1.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 321464062   14 KKTTIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:pfam00240   7 DGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGI 59
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 9-66 7.37e-10

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: 51.06  E-value: 7.37e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 321464062   9 LMIRRKKTTIFT-DAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:cd17039    1 ITVKTLDGKTYTvEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGI 59
Ubl_UHRF1 cd17122
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing ...
 21-64 3.33e-05

ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing protein 1(UHRF1); UHRF1, also termed inverted CCAAT box-binding protein of 90 kDa, or nuclear protein 95, or nuclear zinc finger protein Np95 (Np95), or RING finger protein 106, or transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1, is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma, gastric cancer, esophageal squamous cell carcinoma, colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21.Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination ofTIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET and RING finger associated (SRA) domain, and a C-terminal RING-finger domain. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitination has an essential role in maintenance DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD finger targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-finger domain exhibits both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1.


Pssm-ID: 340642  Cd Length: 74  Bit Score: 39.08  E-value: 3.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 321464062  21 DAKET---------TNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADY 64
Cdd:cd17122    9 DGKEThridslsklTKVEELRQKIQELFGVEPERQRLFYRGKQMEDGHTLFDY 61
UBI4 COG5272
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
17-66 4.06e-05

Ubiquitin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444084 [Multi-domain]  Cd Length: 213  Bit Score: 40.93  E-value: 4.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 321464062  17 TIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:COG5272   12 TITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLEDDRTLADYNI 61
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
 14-66 2.15e-04

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 36.85  E-value: 2.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 321464062  14 KKTTIFTDAKETtnVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:cd16106   11 KKFTVEVEPDAT--VLELKELIAEKSDIPAEQQRLIYKGKILKDEETLSSYKI 61
Ubl_ubiquitin cd01803
ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes ...
 17-88 2.18e-04

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: 37.04  E-value: 2.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 321464062  17 TIFTDAKETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGListtaraQSPASLSLAYRLDNG 88
Cdd:cd01803   12 TITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNI-------QKESTLHLVLRLRGG 76
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 28-66 3.45e-03

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 34.04  E-value: 3.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 321464062   28 VSELKKIIQGITKIAPESQRL-FKDDR------IMEDNRCLADYGL 66
Cdd:pfam14560  25 IEELKEKLELITGTPPSSMRLqLYDDDdnlvakLDDDDALLGSYGV 70
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 25-67 5.08e-03

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 33.80  E-value: 5.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 321464062  25 TTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNR-CLADYGLI 67
Cdd:cd01795   15 TTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSaTLADLGIL 58
Ubl_BAG6 cd01809
ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; ...
 24-66 5.87e-03

ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; BAG6, also termed large proline-rich protein BAG6, or BAG family molecular chaperone regulator 6, or HLA-B-associated transcript 3 (Bat3), or protein Scythe, or protein G3, is a nucleo-cytoplasmic shuttling chaperone protein that is highly conserved in eukaryotes. It functions in two distinct biological pathways, ubiquitin-mediated protein degradation of defective polypeptides and tail-anchored transmembrane protein biogenesis in mammals. BAG6 is a component of the heterotrimeric BAG6 sortase complex composed of BAG6, transmembrane recognition complex 35 (TRC35) and ubiquitin-like protein 4A (UBL4A). The BAG6 complex together with the cochaperone small, glutamine-rich, tetratricopeptide repeat-containing, protein alpha (SGTA) plays a role in the biogenesis of tail-anchored membrane proteins and subsequently shown to regulate the ubiquitination and proteasomal degradation of mislocalized proteins. Moreover, BAG6 acts as an apoptotic regulator that binds reaper, a potent apoptotic inducer. BAG6/reaper is thought to signal apoptosis, in part through regulating the folding and activity of apoptotic signaling molecules. It is also likely a key regulator of the molecular chaperone Heat Shock Protein A2 (HSPA2) stability/function in human germ cells. Furthermore, aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and fungal resistance in plants. BAG6 contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which provides a platform for discriminating substrates with shorter hydrophobicity stretches as a signal for defective proteins.


Pssm-ID: 340507 [Multi-domain]  Cd Length: 71  Bit Score: 33.09  E-value: 5.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 321464062  24 ETTNVSELKKIIQGITKIAPESQRLFKDDRIMEDNRCLADYGL 66
Cdd:cd01809   19 EEITVKEFKEHIASSVNIPAEKQRLIFQGRVLQDDKKLKEYDV 61
 
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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