SII-SWORD/CoKE huggingface dataset:
Pfam PF04734: Neutral/alkaline non-lysosomal ceramidase, N-terminal (domain)
This family represents N-terminal domain of a group of neutral/alkaline ceramidases found in both bacteria and eukaryotes. The EC classification is [ec:3.5.1.23].  The enzyme hydrolyses ceramide to generate sphingosine and fatty acid. The enzyme plays a regulatory role in a variety of physiological events in eukaryotes and also functions as an exotoxin in particular bacteria. This N-terminal domain carries two metal-binding sites, the first for Zn2+ residing within the domain, and the second, for Mg2+/Ca2+ lying at the interface between the two domains.
Pfam PF23462: NFP LysM3 domain (domain)
This entry represents the third LysM domain found in proteins from plants, including the NFP from Medicago truncatula. The LysM domain adopt a beta-alpha-alpha-beta fold, according to structure predictions and. NFP/NFR5 class of receptors are crucial for initial lipochitooligosaccharide (LCO) perception and essential for LCO-mediated root nodule symbiosis. LysM3 also plays a role in infection, although a less important role than that of LysM2.
Pfam PF23124: Antitoxin Xre/MbcA/ParS-like, N-terminal (domain)
This entry represents the N-terminal domain of a group of bacterial sequences related to the antitoxin components of a type II toxin-antitoxin (TA) system Xre/MbcA/ParS. This domain may adopt an alpha-helical fold.
Pfam PF01027: Inhibitor of apoptosis-promoting Bax1 (family)
Programmed cell-death involves a set of Bcl-2 family proteins, some of which inhibit apoptosis (Bcl-2 and Bcl-XL) and some of which promote it (Bax and Bak). Human Bax inhibitor, BI-1, is an evolutionarily conserved integral membrane protein containing multiple membrane-spanning segments predominantly localised to intracellular membranes. It has 6-7 membrane-spanning domains. The C termini of the mammalian BI-1 proteins are comprised of basic amino acids resembling some nuclear targeting sequences, but otherwise the predicted proteins lack motifs that suggest a function. As plant BI-1 appears to localise predominantly to the ER, we hypothesized that plant BI-1 could also regulate cell death triggered by ER stress.  BI-1 appears to exert its effect through an interaction with calmodulin. The budding yeast member of this family has been found unexpectedly to encode a BH3 domain-containing protein (Ybh3p) that regulates the mitochondrial pathway of apoptosis in a phylogenetically conserved manner. Examination of the crystal structure of a bacterial member of this family shows that these proteins mediate a calcium leak across the membrane that is pH-dependent. Calcium homoeostasis balances passive calcium leak with active calcium uptake. The structure exists in a pore-closed and pore-open conformation, at pHs of 8 and 6 respectively, and the pore can be opened by intracrystalline transition; together these findings suggest that pH controls the conformational transition.
Wikipedia: The testis-enhanced gene transcript (TEGT) family includes the testis-enhanced gene transcript proteins of mammals, which are expressed at high levels in the testis, the putative glutamate/aspartate binding proteins of plants and animals, the YccA protein of Escherichia coli and the YetJ protein of Bacillus subtilis. These proteins are about 200-250 residues in length and exhibit 7 TMSs.
Pfam PF22695: EST1-like DNA-binding domain (repeat)
This entry represents a DNA/RNA binding domain found in a group of worm sequences, such as [swissprot:G5ECF1] from C.elegans, which are related to Est1A from human (SMG6), defined as 14-3-3-like proteins involved in nonsense-mediated mRNA decay (NMD) pathway.
Pfam PF06236: Tyrosinase co-factor MelC1 (family)
This family consists of several tyrosinase co-factor MELC1 proteins from a number of Streptomyces species. The melanin operon (melC) of Streptomyces antibioticus contains two genes, melC1 and melC2 (apotyrosinase). It is thought that MelC1 forms a transient binary complex with the downstream apotyrosinase MelC2 to facilitate the incorporation of copper ion and the secretion of tyrosinase indicating that MelC1 is a chaperone for the apotyrosinase MelC2.
Pfam PF12379: Betacoronavirus replicase NSP3, N-terminal (family)
This domain family corresponds to the N-terminal domain of NSP3 (non-structural protein 3, also known as nsp3) found in Betacoronavirus, which is encoded on the replicase polyprotein. This family includes the NSP3a domain which has the ubiquitin-like 1 (UB1) and glutamic acid-rich acidic (AC) hypervariable domains. NSP3a interacts with numerous other proteins involved in replication and transcription and may serve as a scaffolding protein for these processes. The N-terminal NSP3a domain interacts with N (nucleocapsid) protein to colocalise genomic RNA with the nascent replicase-transcriptase complex at the earliest stages of infection, essential for the virus. The C-terminal Glu-rich subdomain is best described as a flexible tail attached to the globular UB1 subdomain. The family is found in association with [pfam:PF08716], [pfam:PF01661], [pfam:PF05409], [pfam:PF06471], [pfam:PF08717], [pfam:PF06478], [pfam:PF09401], [pfam:PF06460], [pfam:PF08715], [pfam:PF08710].
Pfam PF07305: Protein of unknown function (DUF1454) (family)
This family consists of several Enterobacterial sequences of around 200 residues in length which are often known as YiiQ proteins. The function of this family is unknown.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF19640: Family of unknown function (DUF6143) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are typically between 173 and 198 amino acids in length.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF11365: Protein SOGA (coiled_coil)
The SOGA (suppressor of glucose by autophagy) family  consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1  regulates autophagy by playing a role in the  reduction of glucose production in an adiponectin and insulin dependent manner.
Pfam PF18925: Family of unknown function (DUF5675) (domain)
This presumed domain is found in bacteria, archaea, alveolata and caudoviruses. Proteins in this family are typically between 133 and 179 amino acids in length.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF03462: PCRF domain (domain)
This domain is found in peptide chain release factors.
Wikipedia: A release factor is a protein that allows for the termination of translation by recognizing the termination codon or stop codon in an mRNA sequence. They are named so because they release new peptides from the ribosome.
Pfam PF04380: Membrane fusogenic activity (family)
BMFP consists of two structural domains, a coiled-coil C-terminal domain via which the protein self-associates as a trimer, and an N-terminal domain disordered at neutral pH but adopting an amphipathic alpha-helical structure in the presence of phospholipid vesicles, high ionic strength, acidic pH or SDS. BMFP interacts with phospholipid vesicles though the predicted amphipathic alpha-helix induced in the N-terminal half of the protein and promotes aggregation and fusion of vesicles in vitro.
Pfam PF11909: NADH-quinone oxidoreductase cyanobacterial subunit N (family)
The proton-pumping NADH:ubiquinone oxidoreductase catalyzes the electron transfer from NADH to ubiquinone linked with proton translocation across the membrane. It is the largest, most complex and least understood of the respiratory chain enzymes and is referred to as Complex I. The subunit composition of the enzyme varies between groups of organisms. Complex I originating from mammalian mitochondria contains 45 different proteins, whereas in bacteria, the corresponding complex NDH-1 consists of 14 different polypeptides. Homologues of these 14 proteins are found among subunits of the mitochondrial complex I, and therefore bacterial NDH-1 might be considered a model proton-pumping NADH dehydrogenase with a minimal set of subunits. Escherichia coli NDH-1 readily disintegrates into 3 subcomplexes: a water-soluble NADH dehydrogenase fragment (NuoE, -F, and -G),the connecting fragment (NuoB, -C, -D, and -I), and the membrane fragment (NuoA, -H, -J, -K, -L, -M, -N). In cyanobacteria and their descendants, the chloroplasts of green plants, the subunit composition of NDH-1 remains obscure. The genes for eleven subunits NdhA-NdhK, homologous to the NuoA-NuoD and NuoH-NuoN of the E. coli complex, have been found in the genome of Synechocystis sp. PCC 6803 which has a family of 6 ndhD genes and a family of 3 ndhF genes. Two reported multisubunit complexes, NDH-1L and NDH-1M, represent distinct NDH-1 complexes in the thylakoid membrane of Synechocystis 6803 -cyanobacterium. NDH-1L was shown to be essential for photoheterotrophic cell growth, whereas expression of NDH-1M was a prerequisite for CO2 uptake and played an important role in growth of cells at low CO2. Here we report the subunit composition of these two complexes. Fifteen proteins were discovered in NDH-1L including NdhL, a new component of the membrane fragment, and Ssl1690 (designated as NdhO), a novel peripheral subunit. The cyanobacterial NDH-1 complex contains additional subunits, NdhM and NdhN, compared with the minimal set of the bacterial enzyme and these seem to be specific for thylakoid-located NDH-1 of photosynthetic organisms.
Pfam PF16987: KIX domain (domain)
This KIX domain is an activator-binding domain.
Wikipedia: In biochemistry, the KIX domain (kinase-inducible domain (KID) interacting domain) or CREB binding domain is a protein domain of the eukaryotic transcriptional coactivators CBP and P300. It serves as a docking site for the formation of heterodimers between the coactivator and specific transcription factors. Structurally, the KIX domain is a globular domain consisting of three α-helices and two short 310-helices.
Pfam PF05410: Porcine arterivirus-type cysteine proteinase alpha (family)
Corresponds to Merops family C31. These peptidases are involved in viral polyprotein processing in replication.
Pfam PF00167: Fibroblast growth factor (domain)
Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organisms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerisation of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors.  These receptors can each bind several different members of this family.  Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organisms.
Wikipedia: 
Fibroblast growth factors (FGF) are a family of cell signalling proteins produced by macrophages; they are involved in a wide variety of processes, most notably as crucial elements for normal development in animal cells. Any irregularities in their function lead to a range of developmental defects. These growth factors typically act as systemic or locally circulating molecules of extracellular origin that activate cell surface receptors. A defining property of FGFs is that they bind to heparin and to heparan sulfate. Thus, some are sequestered in the extracellular matrix of tissues that contains heparan sulfate proteoglycans and are released locally upon injury or tissue remodeling.
Pfam PF08905: Domain of unknown function (DUF1850) (domain)
This family of proteins are functionally uncharacterised. Some members of this family appear to be misannotated as RocC an amino acid transporter from B. subtilis.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF20494: Lipoprotein YfjS/YafY domain (domain)
This entry is based on the E. coli YfjS and YafY lipoproteins.
Pfam PF13213: Protein of unknown function (DUF4021) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 60 amino acids in length. There is a conserved YGM sequence motif.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF06504: Replication protein C (RepC) (family)
This family consists of several bacterial replication protein C (RepC) sequences.
Pfam PF24603: Tetratricopeptide repeat (repeat)
This region of tetratricopeptide-like (TPR) repeats is found in a group of uncharacterised fungal proteins.
Pfam PF05533: Beet yellows virus-type papain-like endopeptidase C42 (domain)
Members of the Closteroviridae and Potyviridae families of plant positive-strand RNA viruses encode one or two papain-like leader proteinases, belonging to Merops peptidase family C42.
Pfam PF01992: ATP synthase (C/AC39) subunit (family)
This family includes the AC39 subunit from vacuolar ATP synthase [swissprot:P32366], and the C subunit from archaebacterial ATP synthase.  The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae [swissprot:P43456].
Wikipedia: Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pumps protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.
Pfam PF08506: Cse1 (repeat)
This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the nuclear export of importin alpha.  This domain contains HEAT repeats.
Wikipedia: In molecular biology, the CAS/CSE protein family is a family of proteins which includes mammalian cellular apoptosis susceptibility (CAS) proteins and yeast chromosome-segregation protein, CSE1. CAS is involved in both cellular apoptosis and proliferation. Apoptosis is inhibited in CAS-depleted cells, while the expression of CAS correlates to the degree of cellular proliferation. Like CSE1, it is essential for the mitotic checkpoint in the cell cycle, and has been shown to be associated with the microtubule network and the mitotic spindle, as is the protein MEK, which is thought to regulate the intracellular localization of CAS. In the nucleus, CAS acts as a nuclear transport factor in the importin pathway. The importin pathway mediates the nuclear transport of several proteins that are necessary for mitosis and further progression. CAS is therefore thought to affect the cell cycle through its effect on the nuclear transport of these proteins. Since apoptosis also requires the nuclear import of several proteins, it has been suggested that CAS also enables apoptosis by facilitating the nuclear import of at least a subset of these essential proteins.
Pfam PF21333: Follistatin, N-terminal (domain)
Follistatin (FST) is required for normal embryonic and ovarian follicle development. It regulates transforming growth factor-beta superfamily ligands, being described as a ligand antagonist. It consists of a N-terminal domain with a modified TB fold and three follistatin domains (FSD1-3) each of which is subdivided in EGF-like and Kazal-like subdomains. This domain is important for ligand specificity.
Pfam PF07709: Seven Residue Repeat (repeat)
Associated with [pfam:PF02969] in  This repeat is found in some Plasmodium and Theileria proteins.
Pfam PF05618: Putative ATP-dependant zinc protease (family)
Proteins in this family are annotated as being ATP-dependant zinc proteases.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF21920: Ski7 III domain (domain)
This entry represents the Ski7 III domain, which is a component of the C-terminal region of the Ski7 protein in budding yeast. Ski7 is a cofactor of the cytoplasmic exosome that functions in mRNA turnover and non-stop decay (NSD). The Ski7 II domain shares overall sequence similarity with the translational GTPase (trGTPase) Hbs1, but unlike other trGTPases, Ski7 might function as a GTP-binding protein rather than a GTP-hydrolyzing enzyme. The Ski7C is organized into three domains, with domain I adopting the alpha beta fold of GTP-binding domains, and domains II and III each adopting the structure of a closed beta barrel. Domains II and III appear to form a single unit and interact with the G domain, and the three domains interact intra-molecularly not only via their globular folds but also via extended segments.
Pfam PF17265: Family of unknown function (DUF5331) (family)
This bacterial family of unknown function can be found in Cyanobacteria.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF21933: MCM5, C-terminal domain (domain)
This entry represents the C-terminal domain of MCM5 from humans and its homologues, which is a HTH domain. MCM5 is part of the MCM2-7 complex.
Pfam PF01187: Macrophage migration inhibitory factor (MIF) (domain)
Macrophage migration inhibitory factor (MIF) is a key regulatory cytokine within innate and adaptive immune responses, capable of promoting and modulating the magnitude of the response . MIF is released from T-cells and macrophages, and acts within the neuroendocrine system. MIF is capable of tautomerase activity, although its biological function has not been fully characterised. It is induced by glucocorticoid and is capable of overriding the anti-inflammatory actions of glucocorticoid . MIF regulates cytokine secretion and the expression of receptors involved in the immune response. It can be taken up into target cells in order to interact with intracellular signalling molecules, inhibiting p53 function, and/or activating components of the mitogen-activated protein kinase and Jun-activation domain-binding protein-1 (Jab-1) . MIF has been linked to various inflammatory diseases, such as rheumatoid arthritis and atherosclerosis .

The MIF homologue D-dopachrome tautomerase (4.1.1.84) is involved in detoxification through the conversion of dopaminechrome (and possibly norepinephrinechrome), the toxic quinine product of the neurotransmitter dopamine (and norepinephrine), to an indole derivative that can serve as a precursor to neuromelanin .
Wikipedia: Macrophage migration inhibitory factor (MIF), also known as glycosylation-inhibiting factor (GIF), L-dopachrome isomerase, or phenylpyruvate tautomerase is a protein that in humans is encoded by the MIF gene. MIF is an important regulator of innate immunity. The MIF protein superfamily also includes a second member with functionally related properties, the D-dopachrome tautomerase (D-DT). CD74 is a surface receptor for MIF.
Pfam PF15391: Domain of unknown function (DUF4614) (family)
This domain family is found in eukaryotes, and is approximately 180 amino acids in length. There is a conserved EALT sequence motif.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF11714: Thrombin inhibitor Madanin (domain)
Members of this family are the peptidase inhibitor madanin proteins. These proteins were isolated from tick saliva.
Pfam PF18682: Pilin A4 (domain)
This domain is found in the major pilin protein PilA. PilA4 binds to PilMNO forming a complex with a well-defined platform linking the cytoplasmic PilM protein to pilus subunits in the periplasm. Structure analysis indicate that it is comprised of one alpha-helix and 4 beta-sheets.
Pfam PF12024: Domain of unknown function (DUF3512) (family)
This presumed domain is functionally uncharacterised. This domain is found in eukaryotes. This domain is typically between 231 to 249 amino acids in length. This domain is found associated with [pfam:PF00439].
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.