LiteFold/InterPro · Datasets at Hugging Face

IPR020889

20,889

LPS-assembly protein LptD

LipoPS_assembly_LptD

Family

10,884

false

The cell envelope of Gram-negative bacteria consists of an inner (IM) and an outer membrane (OM) separated by an aqueous compartment, the periplasm, which contains the peptidoglycan layer. The OM is an asymmetric bilayer, with phospholipids in the inner leaflet and lipopolysaccharides (LPS) facing outward [ , ]. The OM...

[ "GO:0015920", "GO:0043165", "GO:0009279" ]

[ "lipopolysaccharide transport", "Gram-negative-bacterium-type cell outer membrane assembly", "cell outer membrane" ]

[ "biological_process", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_01411" ]

[ "LPS_assembly_LptD" ]

[ 10884 ]

1

[ "GP" ]

[ "GenProp1115" ]

[ "GP:GenProp1115" ]

1

[ "4n4r", "4q35", "4rhb", "5iv8", "5iv9", "5iva", "7omm", "8h1r", "8h1s", "9fz5", "9i92", "9i93", "9i94", "9i95", "9i96", "9i97", "9i98", "9kn3", "9q8n" ]

19

[ "PUB00028103", "PUB00053159", "PUB00053160", "PUB00053161", "PUB00053162", "PUB00053163", "PUB00053164", "PUB00053165", "PUB00053166", "PUB00053167" ]

[ "12045108", "16357861", "10574995", "8606190", "11278265", "8809774", "9575204", "18424520", "16861298", "15192148" ]

[ "Lipopolysaccharide endotoxins.", "Advances in understanding bacterial outer-membrane biogenesis.", "The activity of a putative polyisoprenol-linked sugar translocase (Wzx) involved in Escherichia coli O antigen assembly is independent of the chemical structure of the O repeat.", "An O-antigen processing func...

[ 2002, 2006, 1999, 1996, 2001, 1996, 1998, 2008, 2006, 2004 ]

10

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 10758, 6, 120 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

LPS-assembly protein LptD

LipoPS_assembly_LptD

7

IPR020890

20,890

Transcription regulator HTH, HdfR

Tscrpt_reg_HTH_HdfR

Family

1,244

false

The LysR-type transcriptional regulators (LTTRs) form one of the largest and most diverse families of bacterial regulators. These proteins are widely distributed and contribute to various aspects of bacterial metabolism and physiology. LTTRs are typically homotetramers, with each subunit consisting of an N-terminal DNA...

[ "GO:0003677", "GO:0003700", "GO:0045892" ]

[ "DNA binding", "DNA-binding transcription factor activity", "negative regulation of DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP" ]

[ "MF_01233" ]

[ "HTH_type_HdfR" ]

[ 1244 ]

1

[]

0

[]

0

[ "PUB00002150", "PUB00002180", "PUB00003277", "PUB00004664", "PUB00004739", "PUB00053169", "PUB00117984", "PUB00160345" ]

[ "1907267", "1592818", "1840615", "3413113", "2034653", "10913108", "12595552", "37285554" ]

[ "rbcR [correction of rcbR], a gene coding for a member of the LysR family of transcriptional regulators, is located upstream of the expressed set of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in the photosynthetic bacterium Chromatium vinosum.", "The Escherichia coli K-12 cyn operon is positively regul...

[ 1991, 1992, 1991, 1988, 1991, 2000, 2003, 2023 ]

8

[]

0

null

[ "Bacteria" ]

[ 1244 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Transcription regulator HTH, HdfR

Tscrpt_reg_HTH_HdfR

5

IPR020891

20,891

Uncharacterised protein family UPF0758, conserved site

UPF0758_CS

Conserved_site

24,670

false

UPF0758 was previously known as the radC family. The name was assigned according to the radC102 mutant of E. coli which was later demonstrated to be an allele of the transcription-repair-coupling factor recG [ , ]. It has been described as a putative JAMM-family deubiquitinating enzyme, but its function remains to be d...

[]

0

[ "PROSITE" ]

[ "PS01302" ]

[ "UPF0758" ]

[ 24670 ]

1

[]

0

[ "2qlc" ]

1

[ "PUB00037483", "PUB00044698", "PUB00044699" ]

[ "14737182", "11053371", "18556794" ]

[ "JAMM: a metalloprotease-like zinc site in the proteasome and signalosome.", "radC102 of Escherichia coli is an allele of recG.", "RadC, a misleading name?" ]

[ 2004, 2000, 2008 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]

[ 145, 24017, 28, 143, 337 ]

5

[ "Danio rerio", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]

[ 2, 4, 1 ]

3

true

Conserved_site

Uncharacterised protein family UPF0758, conserved site

UPF0758_CS

8

IPR020892

20,892

Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site

Cyclophilin-type_PPIase_CS

Conserved_site

85,061

false

Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity ( ), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [ , ]. They also have protein chaperone-like functions [ ] and are the major high-affinity binding proteins for the immu...

[ "GO:0003755", "GO:0006457" ]

[ "peptidyl-prolyl cis-trans isomerase activity", "protein folding" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE" ]

[ "PS00170" ]

[ "CSA_PPIASE_1" ]

[ 85061 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "5.2.1.8", "R-BTA-210991", "R-BTA-6798695", "R-BTA-72163", "R-CEL-210991", "R-CEL-72163", "R-DDI-72163", "R-DME-210991", "R-DME-6798695", "R-GGA-72163", "R-HSA-114608", "R-HSA-1169408", "R-HSA-141444", "R-HSA-159227", "R-HSA-159230", "R-HSA-159231", "R-HSA-159236", "R-HSA-162585", ...

[ "EC:5.2.1.8", "REACTOME:R-BTA-210991", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-72163", "REACTOME:R-CEL-210991", "REACTOME:R-CEL-72163", "REACTOME:R-DDI-72163", "REACTOME:R-DME-210991", "REACTOME:R-DME-6798695", "REACTOME:R-GGA-72163", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-1169408", "REA...

97

[ "1a33", "1a58", "1ak4", "1awq", "1awr", "1aws", "1awt", "1awu", "1awv", "1bck", "1c5f", "1clh", "1cwa", "1cwb", "1cwc", "1cwf", "1cwh", "1cwi", "1cwj", "1cwk", "1cwl", "1cwm", "1cwo", "1cyn", "1dyw", "1e3b", "1e8k", "1fgl", "1h0p", "1ihg", "1iip", "1ist"...

456

[ "PUB00000320", "PUB00017852", "PUB00021063", "PUB00056846", "PUB00056847" ]

[ "2186809", "14731520", "15998457", "21309470", "21295323" ]

[ "The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.", "Cyclophilins: a new family of proteins involved in intracellular folding.", "The cyclophilins.", "An overview of cyclophilins in human cancers.", "Emerging picture of ho...

[ 1990, 1992, 2005, 2010, 2011 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Imitervirales", "unclassified sequences" ]

[ 644, 33307, 50489, 5, 616 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 46, 16, 27, 16, 2, 99, 44, 9, 44, 73, 6, 8, 121 ]

13

true

Conserved_site

Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site

Cyclophilin-type_PPIase_CS

2

IPR020894

20,894

Cadherin conserved site

Cadherin_CS

Conserved_site

115,992

false

Cadherins are a group of transmembrane proteins that serve as the major adhesion molecules located within adherens junctions. They can regulate cell-cell adhesion through their extracellular domain and their cytosolic domains connect to the actin cytoskeleton by binding to catenins [ ]. These proteins preferentially in...

[ "GO:0007155", "GO:0005886" ]

[ "cell adhesion", "plasma membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PROSITE" ]

[ "PS00232" ]

[ "CADHERIN_1" ]

[ 115992 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-418990", "R-CEL-351906", "R-CEL-6798695", "R-CEL-6809371", "R-CEL-9013404", "R-CEL-9013408", "R-CEL-9013423", "R-CFA-1474228", "R-CFA-216083", "R-CFA-351906", "R-CFA-418990", "R-CFA-6805567", "R-CFA-6809371", "R-CFA-9764561", "R-CFA-9766229", "R-CFA-9768727", "R-DME-1474228", ...

[ "REACTOME:R-BTA-418990", "REACTOME:R-CEL-351906", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-6809371", "REACTOME:R-CEL-9013404", "REACTOME:R-CEL-9013408", "REACTOME:R-CEL-9013423", "REACTOME:R-CFA-1474228", "REACTOME:R-CFA-216083", "REACTOME:R-CFA-351906", "REACTOME:R-CFA-418990", "REACTOME:R-C...

135

[ "1edh", "1ff5", "1l3w", "1ncg", "1nch", "1nci", "1ncj", "1q1p", "1q55", "1q5a", "1q5b", "1q5c", "1suh", "1wyj", "2a4e", "2a62", "2o72", "2qvf", "2qvi", "2wcp", "2whv", "2yqg", "2yst", "3k5r", "3lnd", "3lne", "3lnf", "3lng", "3lnh", "3lni", "3mvs", "3ppe"...

169

[ "PUB00007174", "PUB00071518" ]

[ "11736639", "25014356" ]

[ "Structure and functions of classical cadherins.", "E-Cadherin Can Replace N-Cadherin during Secretory-Stage Enamel Development." ]

[ 2001, 2014 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "Halocatena pleomorpha", "metagenomes" ]

[ 113, 115873, 1, 5 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 24, 400, 38, 365, 334, 340 ]

6

true

Conserved_site

Cadherin conserved site

Cadherin_CS

8

IPR020895

20,895

Frataxin conserved site

Frataxin_CS

Conserved_site

8,373

false

This conserved site covers a conserved region in the central section of these proteins. The eukaryotic proteins in this entry include Frataxin, the protein that is mutated in Friedreich's ataxia [ ], and related sequences. Friedreich's ataxia is a progressive neurodegenerative disorder caused by loss of function mutati...

[]

0

[ "PROSITE" ]

[ "PS01344" ]

[ "FRATAXIN_1" ]

[ 8373 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-1268020", "R-BTA-1362409", "R-BTA-9854311", "R-BTA-9865881", "R-CEL-1362409", "R-CEL-9854311", "R-DDI-1362409", "R-DDI-9854311", "R-DDI-9865881", "R-DME-1362409", "R-DME-9854311", "R-DME-9865881", "R-HSA-1268020", "R-HSA-1362409", "R-HSA-9854311", "R-HSA-9865881", "R-MMU-12680...

[ "REACTOME:R-BTA-1268020", "REACTOME:R-BTA-1362409", "REACTOME:R-BTA-9854311", "REACTOME:R-BTA-9865881", "REACTOME:R-CEL-1362409", "REACTOME:R-CEL-9854311", "REACTOME:R-DDI-1362409", "REACTOME:R-DDI-9854311", "REACTOME:R-DDI-9865881", "REACTOME:R-DME-1362409", "REACTOME:R-DME-9854311", "REACTOM...

28

[ "1ekg", "1ew4", "1ly7", "1soy", "2eff", "2fql", "2ga5", "2p1x", "3oeq", "3oer", "3s4m", "3t3x", "4ec2", "4hs5", "4jpd", "4lk8", "4lp1", "5kz5", "5t0v", "5tre", "6fco", "6nzu", "6z1p", "7n9i", "8hz1", "8ivk", "8iwi", "8pk8", "8pk9", "8rme", "9jb5" ]

31

[ "PUB00003904", "PUB00004328", "PUB00005217", "PUB00005550", "PUB00034422", "PUB00042953", "PUB00042954" ]

[ "9241270", "8815938", "8596916", "8931268", "16930487", "16603772", "16428423" ]

[ "Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin.", "Clinical and genetic abnormalities in patients with Friedreich's ataxia.", "Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion.", "Friedreich's ataxia protein: phyl...

[ 1997, 1996, 1996, 1996, 2006, 2006, 2006 ]

7

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 4355, 3988, 30 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 3, 1, 2, 1, 1, 4, 4, 1, 3, 3, 1, 1, 9 ]

13

true

Conserved_site

Frataxin conserved site

Frataxin_CS

9

IPR020897

20,897

Synapsin, pre-ATP-grasp domain

Synapsin_pre-ATP-grasp_dom

Domain

3,868

false

This entry represents the pre-ATP-grasp structural domain found in synapsins, which precedes the ATP-grasp domain. The structure of the pre-ATP-grasp domain consists of α/β/α in three layers, and is possibly a rudiment form of the Rossmann-fold. This domain can have a substrate-binding function. The synapsins are a fam...

[]

0

[ "PFAM" ]

[ "PF02078" ]

[ "Synapsin" ]

[ 3868 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-DME-181429", "R-DME-212676", "R-HSA-181429", "R-HSA-212676", "R-HSA-9662360", "R-MMU-181429", "R-MMU-212676", "R-RNO-181429", "R-RNO-212676" ]

[ "REACTOME:R-DME-181429", "REACTOME:R-DME-212676", "REACTOME:R-HSA-181429", "REACTOME:R-HSA-212676", "REACTOME:R-HSA-9662360", "REACTOME:R-MMU-181429", "REACTOME:R-MMU-212676", "REACTOME:R-RNO-181429", "REACTOME:R-RNO-212676" ]

9

[ "1auv", "1aux", "1i7l", "1i7n", "1pk8", "1px2", "2p0a" ]

7

[ "PUB00018754", "PUB00018755", "PUB00053858", "PUB00053859" ]

[ "10940454", "7777057", "2859595", "10804215" ]

[ "Upregulation of synapsin IIa and IIb mRNAs in the paraventricular and supraoptic nuclei in chronic salt loaded and lactating rats.", "Essential functions of synapsins I and II in synaptic vesicle regulation.", "Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neuro...

[ 2000, 1995, 1985, 2000 ]

4

[]

0

null

[ "Eukaryota" ]

[ 3868 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 6, 4, 11, 7, 14 ]

6

true

Domain

Synapsin, pre-ATP-grasp domain

Synapsin_pre-ATP-grasp_dom

7

IPR020898

20,898

Synapsin, ATP-binding domain

Synapsin_ATP-bd_dom

Domain

4,776

false

This entry represent the ATP-grasp fold found in synapsins, which is responsible for Ca dependent ATP binding. The synapsins are a family of neuron-specific phosphoproteins that coat synaptic vesicles and are involved in the binding between these vesicles and the cytoskeleton (including actin filaments). The family com...

[]

0

[ "PFAM" ]

[ "PF02750" ]

[ "Synapsin_C" ]

[ 4776 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-DME-181429", "R-DME-212676", "R-HSA-181429", "R-HSA-212676", "R-HSA-9662360", "R-MMU-181429", "R-MMU-212676", "R-RNO-181429", "R-RNO-212676" ]

[ "REACTOME:R-DME-181429", "REACTOME:R-DME-212676", "REACTOME:R-HSA-181429", "REACTOME:R-HSA-212676", "REACTOME:R-HSA-9662360", "REACTOME:R-MMU-181429", "REACTOME:R-MMU-212676", "REACTOME:R-RNO-181429", "REACTOME:R-RNO-212676" ]

9

[ "1auv", "1aux", "1i7l", "1i7n", "1pk8", "1px2", "2p0a" ]

7

[ "PUB00018754", "PUB00018755", "PUB00053858", "PUB00053859" ]

[ "10940454", "7777057", "2859595", "10804215" ]

[ "Upregulation of synapsin IIa and IIb mRNAs in the paraventricular and supraoptic nuclei in chronic salt loaded and lactating rats.", "Essential functions of synapsins I and II in synaptic vesicle regulation.", "Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neuro...

[ 2000, 1995, 1985, 2000 ]

4

[]

0

null

[ "Bacteria", "Eukaryota", "uncultured phage cr108_1" ]

[ 48, 4727, 1 ]

3

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 6, 4, 13, 9, 14 ]

6

true

Domain

Synapsin, ATP-binding domain

Synapsin_ATP-bd_dom

7

IPR020899

20,899

Arginine repressor, C-terminal

Arg_repress_C

Domain

13,814

false

The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes, an example of the latter being Giardia lamblia (Giardia intestinalis) [ ]. The three-enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In simpler bacteria, the first enzyme, ...

[ "GO:0034618", "GO:0051259" ]

[ "arginine binding", "protein complex oligomerization" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF02863" ]

[ "Arg_repressor_C" ]

[ 13814 ]

1

[]

0

[ "1b4a", "1b4b", "1f9n", "1xxa", "1xxb", "1xxc", "2p5m", "2zfz", "3bue", "3cag", "3ere", "3fhz", "3laj", "3lap", "3v4g", "5cj9", "5jvo", "6wjo", "6wjp" ]

19

[ "PUB00003952", "PUB00008308", "PUB00008310", "PUB00009717", "PUB00009718", "PUB00024828" ]

[ "9334747", "9504342", "9851988", "1583685", "10331868", "11856827" ]

[ "Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA.", "Anaerobic bacterial metabolism in the ancient eukaryote Giardia duodenalis.", "The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its...

[ 1997, 1998, 1998, 1992, 1999, 2002 ]

6

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 13572, 7, 235 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Arginine repressor, C-terminal

Arg_repress_C

5

IPR020900

20,900

Arginine repressor, DNA-binding domain

Arg_repress_DNA-bd

Domain

13,796

false

The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes, an example of the latter being Giardia lamblia (Giardia intestinalis) [ ]. The three-enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In simpler bacteria, the first enzyme, ...

[ "GO:0003700", "GO:0006355", "GO:0006525" ]

[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription", "arginine metabolic process" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "PFAM" ]

[ "PF01316" ]

[ "Arg_repressor" ]

[ 13796 ]

1

[]

0

[ "1aoy", "1b4a", "1f9n", "2p5k", "2p5l", "3ere", "3fhz", "3laj", "3lap", "3v4g", "5cj9" ]

11

[ "PUB00008308", "PUB00008310", "PUB00009717", "PUB00009718" ]

[ "9504342", "9851988", "1583685", "10331868" ]

[ "Anaerobic bacterial metabolism in the ancient eukaryote Giardia duodenalis.", "The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its activation by the arginine repressor argR.", "Characterization of the arginine repressor from Salmonella typhimurium and its intera...

[ 1998, 1998, 1992, 1999 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 3, 13569, 12, 212 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Arginine repressor, DNA-binding domain

Arg_repress_DNA-bd

8

IPR020901

20,901

Proteinase inhibitor I2, Kunitz, conserved site

Prtase_inh_Kunz-CS

Conserved_site

29,480

false

This entry represents a conserved site spanning a region starting after the third cysteine and ending with the fifth one. The majority of the sequences having this domain belong to the MEROPS inhibitor family I2, clan IB; the Kunitz/bovine pancreatic trypsin inhibitor family, they inhibit proteases of the S1 family [ ]...

[]

0

[ "PROSITE" ]

[ "PS00280" ]

[ "BPTI_KUNITZ_1" ]

[ 29480 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-HSA-114608", "R-HSA-140834", "R-HSA-1442490", "R-HSA-1566977", "R-HSA-1650814", "R-HSA-186797", "R-HSA-2022090", "R-HSA-204005", "R-HSA-216083", "R-HSA-2168880", "R-HSA-2214320", "R-HSA-3000157", "R-HSA-3000178", "R-HSA-381426", "R-HSA-416476", "R-HSA-418594", "R-HSA-419037", "R...

[ "REACTOME:R-HSA-114608", "REACTOME:R-HSA-140834", "REACTOME:R-HSA-1442490", "REACTOME:R-HSA-1566977", "REACTOME:R-HSA-1650814", "REACTOME:R-HSA-186797", "REACTOME:R-HSA-2022090", "REACTOME:R-HSA-204005", "REACTOME:R-HSA-216083", "REACTOME:R-HSA-2168880", "REACTOME:R-HSA-2214320", "REACTOME:R-H...

88

[ "1aap", "1adz", "1b0c", "1bf0", "1bhc", "1bik", "1bpi", "1bpt", "1brb", "1brc", "1bth", "1bti", "1bun", "1bz5", "1bzx", "1ca0", "1cbw", "1co7", "1d0d", "1dem", "1den", "1dtk", "1dtx", "1eaw", "1ejm", "1f5r", "1f7z", "1fak", "1fy8", "1g6x", "1irh", "1jc6"...

175

[ "PUB00003271", "PUB00003421", "PUB00004837", "PUB00005002", "PUB00005362", "PUB00014133" ]

[ "1714504", "1593645", "8159751", "1304909", "1703675", "14705960" ]

[ "Crystal structure of a Y35G mutant of bovine pancreatic trypsin inhibitor.", "Evolutionary origin of a Kunitz-type trypsin inhibitor domain inserted in the amyloid beta precursor protein of Alzheimer's disease.", "Molecular cloning, expression, and partial characterization of a second human tissue-factor-pathw...

[ 1991, 1992, 1994, 1992, 1990, 2004 ]

6

[]

0

null

[ "Bacteria", "Betaentomopoxvirus", "Eukaryota", "bioreactor metagenome" ]

[ 34, 2, 29443, 1 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 56, 67, 31, 68, 54, 63 ]

6

true

Conserved_site

Proteinase inhibitor I2, Kunitz, conserved site

Prtase_inh_Kunz-CS

1

IPR020902

20,902

Actin/actin-like conserved site

Actin/actin-like_CS

Conserved_site

46,980

false

Actin [ , ] is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. These filaments interact with myosin to produce a sliding effect, which is the basis of muscular contraction and many aspects of cell motility, including cytokinesis. Each actin protomer binds one m...

[]

0

[ "PROSITE" ]

[ "PS01132" ]

[ "ACTINS_ACT_LIKE" ]

[ 46980 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...

[ "3.6.4.-", "PWY-7250", "R-BTA-114608", "R-BTA-190873", "R-BTA-196025", "R-BTA-2029482", "R-BTA-2132295", "R-BTA-390522", "R-BTA-3928662", "R-BTA-418990", "R-BTA-4420097", "R-BTA-445355", "R-BTA-446353", "R-BTA-5250924", "R-BTA-5626467", "R-BTA-5663213", "R-BTA-5663220", "R-BTA-5674...

[ "EC:3.6.4.-", "METACYC:PWY-7250", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-190873", "REACTOME:R-BTA-196025", "REACTOME:R-BTA-2029482", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-390522", "REACTOME:R-BTA-3928662", "REACTOME:R-BTA-418990", "REACTOME:R-BTA-4420097", "REACTOME:R-BTA-445355", "REA...

363

[ "1atn", "1c0f", "1c0g", "1d4x", "1dej", "1eqy", "1esv", "1h1v", "1hlu", "1ijj", "1j6z", "1k8k", "1kxp", "1lcu", "1lot", "1m8q", "1ma9", "1mdu", "1mvw", "1nlv", "1nm1", "1nmd", "1nwk", "1o18", "1o19", "1o1a", "1o1b", "1o1c", "1o1d", "1o1e", "1o1f", "1o1g"...

662

[ "PUB00000090", "PUB00001058", "PUB00004744", "PUB00004796" ]

[ "1388079", "8448030", "1828889", "1323828" ]

[ "Structure and function of actin.", "Actin isoforms.", "Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein.", "An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins." ]

[ 1992, 1993, 1991, 1992 ]

4

[]

0

null

[ "Bacteria", "Eukaryota", "Promethearchaeaceae", "Viruses", "unclassified sequences" ]

[ 24, 46920, 2, 5, 29 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 33, 8, 25, 19, 125, 66, 4, 22, 53, 5, 3, 52 ]

12

true

Conserved_site

Actin/actin-like conserved site

Actin/actin-like_CS

2

IPR020903

20,903

Epithelial sodium channel, conserved site

ENaC_CS

Conserved_site

8,890

false

The apical membrane of many tight epithelia contains sodium channels that are primarily characterised by their high affinity to the diuretic blocker amiloride [ , , , ]. These channels mediate the first step of active sodium reabsorption essential for the maintenance of body salt and water homeostasis [ ]. In vertebrat...

[ "GO:0005272", "GO:0006814", "GO:0016020" ]

[ "sodium channel activity", "sodium ion transport", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PROSITE" ]

[ "PS01206" ]

[ "ASC" ]

[ 8890 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-2672351", "R-BTA-9730628", "R-CEL-2672351", "R-CEL-9730628", "R-DME-2672351", "R-DRE-2672351", "R-GGA-2672351", "R-HSA-2672351", "R-HSA-9730628", "R-MMU-2672351", "R-MMU-9730628", "R-RNO-2672351", "R-RNO-9730628" ]

[ "REACTOME:R-BTA-2672351", "REACTOME:R-BTA-9730628", "REACTOME:R-CEL-2672351", "REACTOME:R-CEL-9730628", "REACTOME:R-DME-2672351", "REACTOME:R-DRE-2672351", "REACTOME:R-GGA-2672351", "REACTOME:R-HSA-2672351", "REACTOME:R-HSA-9730628", "REACTOME:R-MMU-2672351", "REACTOME:R-MMU-9730628", "REACTOM...

13

[ "2qts", "3ij4", "3s3w", "3s3x", "4fz0", "4fz1", "4ntw", "4ntx", "4nty", "4nyk", "5wku", "5wkv", "5wkx", "5wky", "6ave", "6bqn", "6cmc", "6l6i", "6l6n", "6l6p", "6vtk", "6vtl", "6wth", "6x9h", "7cfs", "7cft", "7lie", "7rnn", "8on7", "8on8", "8on9", "8ona"...

35

[ "PUB00001528", "PUB00002871", "PUB00002932", "PUB00003784" ]

[ "8181670", "7929098", "7499195", "8905643" ]

[ "Molecular properties of epithelial, amiloride-blockable Na+ channels.", "Membrane topology of the amiloride-sensitive epithelial sodium channel.", "Molecular cloning and functional expression of a novel amiloride-sensitive Na+ channel.", "Phylogenetic characterization of the epithelial Na+ channel (ENaC) fam...

[ 1994, 1994, 1995, 1996 ]

4

[]

0

null

[ "Eukaryota" ]

[ 8890 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 21, 30, 15, 30, 19, 32 ]

6

true

Conserved_site

Epithelial sodium channel, conserved site

ENaC_CS

4

IPR020904

20,904

Short-chain dehydrogenase/reductase, conserved site

Sc_DH/Rdtase_CS

Conserved_site

619,284

false

This entry represents one of the best conserved regions in this family of proteins It includes two perfectly conserved residues, a tyrosine and a lysine. The tyrosine residue participates in the catalytic mechanism. The short-chain dehydrogenases/reductases family (SDR) [ , ] is a very large family of enzymes, most of ...

[]

0

[ "PROSITE" ]

[ "PS00061" ]

[ "ADH_SHORT" ]

[ 619284 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "1.1.1", "R-BTA-1660661", "R-BTA-193144", "R-BTA-2162123", "R-BTA-2453902", "R-BTA-5365859", "R-BTA-5661270", "R-BTA-70895", "R-BTA-75105", "R-BTA-77108", "R-BTA-77111", "R-BTA-8964208", "R-BTA-9837999", "R-CEL-2187335", "R-CEL-5365859", "R-CEL-5661270", "R-CFA-75105", "R-DDI-89642...

[ "EC:1.1.1", "REACTOME:R-BTA-1660661", "REACTOME:R-BTA-193144", "REACTOME:R-BTA-2162123", "REACTOME:R-BTA-2453902", "REACTOME:R-BTA-5365859", "REACTOME:R-BTA-5661270", "REACTOME:R-BTA-70895", "REACTOME:R-BTA-75105", "REACTOME:R-BTA-77108", "REACTOME:R-BTA-77111", "REACTOME:R-BTA-8964208", "RE...

133

[ "1a27", "1a4u", "1ae1", "1ahh", "1ahi", "1b14", "1b15", "1b16", "1b2l", "1bdb", "1bhs", "1cyd", "1dhr", "1dht", "1dir", "1doh", "1e3s", "1e3w", "1e6w", "1e7w", "1e92", "1edo", "1equ", "1fds", "1fdt", "1fdu", "1fdv", "1fdw", "1fmc", "1g0n", "1g0o", "1g6k"...

818

[ "PUB00000419", "PUB00001371", "PUB00001399", "PUB00001408", "PUB00004592", "PUB00075490" ]

[ "7742302", "2707261", "1889416", "1740120", "6789320", "25526675" ]

[ "Short-chain dehydrogenases/reductases (SDR).", "The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc.", "Characteristics of short-chain alcohol dehydrogenases and related enzymes.", "cis-diol dehydrogen...

[ 1995, 1989, 1991, 1992, 1981, 2015 ]

6

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Viruses", "unclassified sequences" ]

[ 3995, 456563, 152609, 1, 70, 6046 ]

6

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 169, 44, 85, 40, 16, 123, 83, 40, 124, 113, 9, 10, 151 ]

13

true

Conserved_site

Short-chain dehydrogenase/reductase, conserved site

Sc_DH/Rdtase_CS

9

IPR020905

20,905

NAD(P)H-quinone oxidoreductase subunit O

NdhO

Family

908

false

NAD(P)H-quinone oxidoreductase (NDH-1) shuttles electrons from an unknown electron donor, via FMN and iron-sulphur (Fe-S) centres, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. It couples the redox reaction...

[ "GO:0016655", "GO:0005886" ]

[ "oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor", "plasma membrane" ]

[ "molecular_function", "cellular_component" ]

2

[ "HAMAP", "PFAM" ]

[ "MF_01354", "PF11910" ]

[ "NDH1_NDH1O", "NdhO" ]

[ 362, 908 ]

2

[ "EC" ]

[ "7.1.1.-" ]

[ "EC:7.1.1.-" ]

1

[ "6hum", "6khi", "6khj", "6l7o", "6l7p", "6nbq", "6nbx", "6nby", "6tjv", "7wfg", "7wg5", "9grx" ]

12

[]

0

[]

0

null

[ "Cyanobacteriota", "Eukaryota" ]

[ 375, 533 ]

2

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 4, 4 ]

3

true

Family

NAD(P)H-quinone oxidoreductase subunit O

NdhO

2

IPR020906

20,906

Double-stranded DNA-binding Cren7

dsDNA-bd_Cren7

Family

149

false

Cren7 is a chromatin protein found in Crenarchaeota and has a higher affinity for double-stranded DNA than for single-stranded DNA. The protein contains negative DNA supercoils and is associated with genomic DNA in vivo. Cren7 interacts with duplex DNA through a β-sheet and a long flexible loop. It is binding to double...

[ "GO:0003690", "GO:0005737" ]

[ "double-stranded DNA binding", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "HAMAP", "PFAM" ]

[ "MF_01387", "PF11520" ]

[ "Chromatin_Cren7", "Cren7" ]

[ 119, 149 ]

2

[]

0

[ "2jtm", "3kxt", "3lwh", "3lwi", "4r55", "4r56", "5k07", "5k17", "5wvw", "5wvy", "5wvz", "5wwc", "6a2h", "6a2i" ]

14

[ "PUB00048078", "PUB00097468" ]

[ "18096617", "20512977" ]

[ "Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea.", "Crystal structure of the crenarchaeal conserved chromatin protein Cren7 and double-stranded DNA complex." ]

[ 2008, 2010 ]

2

[]

0

null

[ "Thermoproteota" ]

[ 149 ]

1

[]

0

true

Family

Double-stranded DNA-binding Cren7

dsDNA-bd_Cren7

1

IPR020907

20,907

PhoP/PhoQ regulator MgrB

MgrB

Family

769

false

This entry represents MgrB, a short lipoprotein that is induced by low extracellular levels of magnesium via the PhoQ/PhoP two-component regulatory system [ ]. Deletion of MgrB results in a potent increase in PhoP-regulated transcription [ ].

[]

0

[ "HAMAP", "PFAM" ]

[ "MF_01596", "PF13998" ]

[ "MgrB", "MgrB" ]

[ 571, 769 ]

2

[]

0

[]

0

[ "PUB00053170", "PUB00057924" ]

[ "10464230", "20041203" ]

[ "Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12: identification of extracellular Mg2+-responsive promoters.", "Feedback inhibition in the PhoQ/PhoP signaling system by a membrane peptide." ]

[ 1999, 2009 ]

2

[]

0

null

[ "Bacteria" ]

[ 769 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

PhoP/PhoQ regulator MgrB

MgrB

1

IPR020908

20,908

Uncharacterised protein family UPF0738

UPF0738

Family

869

false

This is a protein of unknown function.

[]

0

[ "HAMAP", "PFAM" ]

[ "MF_01861", "PF19785" ]

[ "UPF0738", "UPF0738" ]

[ 477, 869 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Rhizophagus irregularis", "human gut metagenome" ]

[ 867, 1, 1 ]

3

[]

0

true

Family

Uncharacterised protein family UPF0738

UPF0738

1

IPR020909

20,909

UPF0736

Family

840

false

This is a protein of unknown function.

[]

0

[ "HAMAP", "PFAM" ]

[ "MF_01860", "PF12227" ]

[ "UPF0736", "DUF3603" ]

[ 468, 840 ]

2

[]

0

[ "8b3s" ]

1

[]

0

[]

0

null

[ "Bacteria", "Bastillevirinae" ]

[ 821, 19 ]

2

[]

0

true

Family

UPF0736

1

IPR020910

20,910

Uncharacterised protein family UPF0370

UPF0370

Family

1,106

false

This entry describes proteins of unknown function that are thought to be membrane proteins.

[]

0

[ "HAMAP", "NCBIFAM", "PFAM" ]

[ "MF_01566", "NF010185", "PF13980" ]

[ "UPF0370", "PRK13664.1", "UPF0370" ]

[ 824, 1059, 1106 ]

3

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria" ]

[ 1106 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family UPF0370

UPF0370

5

IPR020911

20,911

Uncharacterised protein family UPF0325

UPF0325

Family

1,524

false

This is a protein of unknown function.

[]

0

[ "HAMAP", "NCBIFAM", "PFAM" ]

[ "MF_01519", "NF010213", "PF11944" ]

[ "UPF0325", "PRK13677.1", "DUF3461" ]

[ 1252, 1366, 1524 ]

3

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Hirondellea gigas", "metagenomes" ]

[ 1520, 1, 3 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family UPF0325

UPF0325

6

IPR020912

20,912

Uncharacterised protein family UPF0295

UPF0295

Family

1,439

false

This entry describes proteins of unknown function, which are thought to be membrane proteins.

[]

0

[ "HAMAP", "NCBIFAM", "PFAM" ]

[ "MF_01502", "NF002796", "PF11023" ]

[ "UPF0295", "PRK02935.1", "DUF2614" ]

[ 796, 1387, 1439 ]

3

[]

0

[]

0

[]

0

[]

0

null

[ "Bacillus phage Mgbh1", "Bacteria", "Eukaryota", "Ferroplasma", "bioreactor metagenome" ]

[ 1, 1429, 6, 2, 1 ]

5

[]

0

true

Family

Uncharacterised protein family UPF0295

UPF0295

6

IPR020913

20,913

Uncharacterised protein family UPF0323

UPF0323

Family

95

false

This entry describes proteins of unknown function that are confined to epsilonproteobacteria.

[]

0

[ "HAMAP" ]

[ "MF_01421" ]

[ "UPF0323" ]

[ 95 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Campylobacterales" ]

[ 95 ]

1

[]

0

true

Family

Uncharacterised protein family UPF0323

UPF0323

5

IPR020914

20,914

Probable succinate transporter subunit YjjB

YjjB

Family

967

false

This entry includes probable succinate transporter subunit YjjB from gammaproteobacteria. YjjB is thought to play a role in the production of succinate [ ].

[]

0

[ "HAMAP", "NCBIFAM" ]

[ "MF_01191", "NF007391" ]

[ "YjjB", "PRK09917.1" ]

[ 943, 967 ]

2

[]

0

[]

0

[ "PUB00099774" ]

[ "28673128" ]

[ "Escherichia coli yjjPB genes encode a succinate transporter important for succinate production." ]

[ 2017 ]

1

[]

0

null

[ "Bacteria" ]

[ 967 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Probable succinate transporter subunit YjjB

YjjB

3

IPR020915

20,915

Uncharacterised protein family UPF0311

UPF0311

Family

5,331

false

This is a protein of unknown function.

[]

0

[ "HAMAP", "PANTHER" ]

[ "MF_00775", "PTHR37315" ]

[ "UPF0311", "" ]

[ 2572, 5324 ]

2

[]

0

[ "3c5o", "3g7g", "4pux" ]

3

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "Halobacteriales", "unclassified sequences" ]

[ 2954, 2321, 17, 39 ]

4

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family UPF0311

UPF0311

9

IPR020916

20,916

Protein-glutamine gamma-glutamyltransferase, bacteria

Gln_gamma-glutamylTfrase_bac

Family

1,211

false

This entry represents a protein-glutamine gamma-glutamyltransferase which may play a role in the assembly of the spore coat proteins by catalysing epsilon-(gamma-glutamyl)lysine cross-links.

[ "GO:0003810" ]

[ "protein-glutamine gamma-glutamyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM", "PFAM" ]

[ "MF_00727", "NF002869", "PF20085" ]

[ "Tgl", "PRK03187.1", "TGL" ]

[ 870, 794, 1211 ]

3

[ "EC" ]

[ "2.3.2.13" ]

[ "EC:2.3.2.13" ]

1

[ "4p8i", "4pa5", "7c9j" ]

3

[ "PUB00034533", "PUB00104126" ]

[ "15317760", "12501297" ]

[ "Transglutaminase-mediated cross-linking of GerQ in the coats of Bacillus subtilis spores.", "Transglutaminase in sporulating cells of Bacillus subtilis." ]

[ 2004, 1998 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "Methanocella", "Terrestrivirus sp.", "metagenomes" ]

[ 1193, 2, 2, 1, 13 ]

5

[]

0

true

Family

Protein-glutamine gamma-glutamyltransferase, bacteria

Gln_gamma-glutamylTfrase_bac

6

IPR020917

20,917

Primosomal protein 1

DnaT

Family

898

false

This entry represents Primosomal protein 1 (DnaT) and similar proteins from Proteobacteria. DnaT, a DnaB/C complex loader protein, is required for primosome-dependent normal DNA replication [ ]. It is part of the "PriA-PriB" pathway for primosome assembly [ ] and is involved in inducing stable DNA replication during SO...

[ "GO:0006260", "GO:1990077" ]

[ "DNA replication", "primosome complex" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01061", "NF002770" ]

[ "DnaT", "PRK02854.1" ]

[ 866, 887 ]

2

[ "GP", "GP" ]

[ "GenProp1130", "GenProp1187" ]

[ "GP:GenProp1130", "GP:GenProp1187" ]

2

[ "6aep", "6aeq" ]

2

[ "PUB00099779", "PUB00099781", "PUB00099782" ]

[ "30593500", "27387236", "24280305" ]

[ "Function of a strand-separation pin element in the PriA DNA replication restart helicase.", "DnaT is a PriC-binding protein.", "The N-terminal domain of DnaT, a primosomal DNA replication protein, is crucial for PriB binding and self-trimerization." ]

[ 2019, 2016, 2013 ]

3

[]

0

null

[ "Gammaproteobacteria" ]

[ 898 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Primosomal protein 1

DnaT

9

IPR020918

20,918

Peptide chain release factor subunit 1

Prf1

Family

915

false

This entry represents Peptide chain release factor subunit 1, which seems to have functional resemblance to eukaryotic RF1 [ ]. Terminating protein synthesis on the ribosome requires the presence of a class I polypeptide chain release factor (RF) to induce peptidyl-tRNA hydrolysis. Bacteria possess two class I RFs; RF1...

[ "GO:0003747", "GO:0006415", "GO:0005737" ]

[ "translation release factor activity", "translational termination", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_00424" ]

[ "Rel_fact_arch_1" ]

[ 915 ]

1

[]

0

[ "3agk", "3vmf", "4af1" ]

3

[ "PUB00053182", "PUB00053183", "PUB00053184" ]

[ "9179839", "10788613", "10471834" ]

[ "Polypeptide chain release factors.", "Translation termination factor aRF1 from the archaeon Methanococcus jannaschii is active with eukaryotic ribosomes.", "Polypeptide release factor eRF1 from Tetrahymena thermophila: cDNA cloning, purification and complex formation with yeast eRF3." ]

[ 1997, 2000, 1999 ]

3

[ "IPR004403" ]

[]

1

0

1

[ "Archaea", "candidate division WOR-3 bacterium", "ecological metagenomes" ]

[ 899, 1, 15 ]

3

[]

0

true

Family

Peptide chain release factor subunit 1

Prf1

6

IPR020919

20,919

Small ribosomal subunit protein eS8, archaea

Ribosomal_protein_eS8_arc

Family

871

false

This entry represents the archaeal eS8 proteins, which are about 125 amino acids in length. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growin...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_00029" ]

[ "Ribosomal_eS8" ]

[ 871 ]

1

[]

0

[ "2kco", "4v4n", "4v6u", "5jb3", "5jbh", "6skf", "6skg", "6sw9", "6swc", "6swd", "6th6", "6tmf", "7zag", "7zah", "7zai", "7zhg", "8hkx", "8hky", "8hkz", "8hl1", "8hl2", "8hl3", "8hl4", "8hl5", "8wkp", "8wq2", "8wq4", "9e71", "9e7f", "9fhl", "9fny", "9fnz"...

44

[ "PUB00003471", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00110894" ]

[ "7662106", "11297922", "11290319", "11114498", "23636399" ]

[ "Amino acid sequence of the ribosomal protein HS23 from the halophilic Haloarcula marismortui and homology studies to other ribosomal proteins.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Structures o...

[ 1995, 2001, 2001, 2000, 2013 ]

5

[ "IPR001047" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 849, 22 ]

2

[]

0

true

Family

Small ribosomal subunit protein eS8, archaea

Ribosomal_protein_eS8_arc

7

IPR020920

20,920

L-lactate dehydrogenase, bacterial

LldD

Family

3,110

false

This entry represents the bacterial L-lactate dehydrogenase, a member of the FMN-dependent alpha-hydroxy acid dehydrogenase family. It catalyses the oxidation of L-lactate to pyruvate [ , , , ]. The lld operon was previously named lct [ ].

[ "GO:0004457", "GO:0010181", "GO:0006089" ]

[ "lactate dehydrogenase activity", "FMN binding", "lactate metabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01559", "NF033901" ]

[ "L_lact_dehydr", "L_lactate_LldD" ]

[ 2515, 3110 ]

2

[]

0

[]

0

[ "PUB00019771", "PUB00053244", "PUB00070340", "PUB00105413", "PUB00105414" ]

[ "8407843", "8759842", "18473", "22574176", "30066495" ]

[ "Three overlapping lct genes involved in L-lactate utilization by Escherichia coli.", "Cloning of a Neisseria meningitidis gene for L-lactate dehydrogenase (L-LDH): evidence for a second meningococcal L-LDH with different regulation.", "Inducible membrane-bound L-lactate dehydrogenase from Escherichia coli. Pur...

[ 1993, 1996, 1977, 2012, 2018 ]

5

[ "IPR012133" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta", "metagenomes" ]

[ 3096, 8, 6 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

L-lactate dehydrogenase, bacterial

LldD

2

IPR020921

20,921

Erythronate-4-phosphate dehydrogenase

Erythronate-4-P_DHase

Family

4,886

false

Pyridoxal-5'-phosphate is the active form of vitamin B6 and is an essential cofactor for many enzymes, particularly those involved in amino acid metabolism [ ]. There are three known pathways for pyridoxal-5'-phosphate biosynthesis: the de novo pathway, the salvage pathway, and the fungal type pathway. Bacteria, fungi,...

[ "GO:0033711", "GO:0008615", "GO:0005737" ]

[ "4-phosphoerythronate dehydrogenase activity", "pyridoxine biosynthetic process", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "CDD" ]

[ "MF_01825", "cd12158" ]

[ "PdxB", "ErythrP_dh" ]

[ 4688, 4886 ]

2

[ "EC" ]

[ "1.1.1.290" ]

[ "EC:1.1.1.290" ]

1

[ "2o4c", "3oet", "5dt9" ]

3

[ "PUB00053235", "PUB00053236" ]

[ "15483325", "9696782" ]

[ "Evolution of vitamin B6 (pyridoxine) metabolism by gain and loss of genes.", "Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12." ]

[ 2005, 1998 ]

2

[]

0

null

[ "Bacteria", "Opisthokonta", "metagenomes" ]

[ 4831, 3, 52 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Erythronate-4-phosphate dehydrogenase

Erythronate-4-P_DHase

6

IPR020922

20,922

dITP/XTP pyrophosphatase

dITP/XTP_pyrophosphatase

Family

25,078

false

This entry represents a family of nucleoside-triphosphatases that hydrolyse non-standard nucleotides such as deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP). It has been suggested that they may function as part of a preemptive DNA repair system by excluding non-standard purines from DNA precursor poo...

[ "GO:0017111", "GO:0009143" ]

[ "ribonucleoside triphosphate phosphatase activity", "nucleoside triphosphate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01405" ]

[ "Non_canon_purine_NTPase" ]

[ 25078 ]

1

[ "EC" ]

[ "3.6.1.66" ]

[ "EC:3.6.1.66" ]

1

[ "1b78", "1k7k", "1v7r", "1vp2", "2dvn", "2dvo", "2dvp", "2e5x", "2mjp", "2pyu", "2q16", "2zti", "3s86", "3tqu", "4bnq", "6wwd" ]

16

[ "PUB00053239" ]

[ "17090528" ]

[ "Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase." ]

[ 2007 ]

1

[ "IPR002637" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified Caudoviricetes", "unclassified sequences" ]

[ 477, 24069, 34, 3, 495 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

dITP/XTP pyrophosphatase

dITP/XTP_pyrophosphatase

4

IPR020923

20,923

DNA ligase B

DNA_ligase_B

Family

2,659

false

DNA ligase B, a protein that is is highly conserved throughout the Enterobacteriaceae family, is an NAD(+)-dependent enzyme that catalyses the sealing of 5' phosphate and 3' hydroxyl termini at nicks in duplex DNA by means of three sequential nucleotidyl transfer reactions. Unlike DNA ligase A, it is not essential unde...

[ "GO:0003911", "GO:0006259", "GO:0006260" ]

[ "DNA ligase (NAD+) activity", "DNA metabolic process", "DNA replication" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01587", "NF005987" ]

[ "DNA_ligase_B", "PRK08097.1" ]

[ 2636, 2657 ]

2

[ "EC" ]

[ "6.5.1.2" ]

[ "EC:6.5.1.2" ]

1

[]

0

[ "PUB00053240", "PUB00099765" ]

[ "11812821", "28700629" ]

[ "A second NAD(+)-dependent DNA ligase (LigB) in Escherichia coli.", "Escherichia coli DNA ligase B may mitigate damage from oxidative stress." ]

[ 2001, 2017 ]

2

[]

0

null

[ "Gammaproteobacteria", "Trichuris trichiura", "marine sediment metagenome" ]

[ 2656, 1, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

DNA ligase B

DNA_ligase_B

6

IPR020924

20,924

Small ribosomal subunit protein eS6, archaea

Ribosomal_eS6_arc

Family

1,045

false

This entry represents the archaeal eS6 proteins. A number of eukaryotic and archaeal ribosomal proteins have been grouped on the basis of sequence similarities. Small ribosomal subunit protein eS6, previously known as Ribosomal protein S6 is the major substrate of protein kinases in eukaryotic ribosomes [ ] and may pla...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_00512" ]

[ "Ribosomal_eS6" ]

[ 1045 ]

1

[]

0

[ "4v4n", "4v6u", "5jb3", "5jbh", "6skf", "6skg", "6sw9", "6swc", "6swd", "6th6", "6tmf", "7zag", "7zah", "7zai", "7zhg", "8hkx", "8hky", "8hkz", "8hl1", "8hl2", "8hl3", "8hl4", "8hl5", "8wkp", "8wq2", "8wq4", "9e71", "9e7f", "9fhl", "9fny", "9fnz", "9fo0"...

43

[ "PUB00002823", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "8440735", "11297922", "11290319", "11114498" ]

[ "Identification of 40 S ribosomal protein S6 phosphorylation sites in Swiss mouse 3T3 fibroblasts stimulated with serum.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 1993, 2001, 2001, 2000 ]

4

[ "IPR001377" ]

[]

1

0

1

[ "Archaea", "Candidatus Uhrbacteria bacterium GW2011_GWC2_53_7", "Eukaryota", "unclassified sequences" ]

[ 872, 1, 145, 27 ]

4

[ "Zea mays" ]

[ 1 ]

1

true

Family

Small ribosomal subunit protein eS6, archaea

Ribosomal_eS6_arc

3

IPR020925

20,925

Large ribosomal subunit protein eL15, conserved site

Ribosomal_eL15_CS

Conserved_site

5,091

false

This entry represents a short conserved sequence region located in the central section of the members of the large ribosomal subunit protein eL15 family. A number of eukaryotic and archaebacterial ribosomal proteins can be grouped on the basis of sequence similarities [ ]. One of these families consists of: Mammalian e...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PROSITE" ]

[ "PS01194" ]

[ "RIBOSOMAL_L15E" ]

[ 5091 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706", "R-DDI-97595...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-9759...

64

[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...

647

[ "PUB00000245", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "7733938", "11297922", "11290319", "11114498" ]

[ "The Thermoplasma acidophilum rpl15 gene encodes a homologue of eukaryotic ribosomal proteins L15/YL10.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 1995, 2001, 2001, 2000 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 584, 3, 4490, 14 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 5, 1, 1, 2, 9, 3, 1, 6, 4, 2, 2, 13 ]

12

true

Conserved_site

Large ribosomal subunit protein eL15, conserved site

Ribosomal_eL15_CS

6

IPR020926

20,926

Large ribosomal subunit protein eL15, archaeal

Ribosomal_eL15_arc

Family

688

false

This entry represents the archaeal eL15 proteins found in archaea. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in ac...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_00256" ]

[ "Ribosomal_eL15" ]

[ 688 ]

1

[]

0

[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...

80

[ "PUB00000245", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "7733938", "11297922", "11290319", "11114498" ]

[ "The Thermoplasma acidophilum rpl15 gene encodes a homologue of eukaryotic ribosomal proteins L15/YL10.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 1995, 2001, 2001, 2000 ]

4

[ "IPR000439" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 684, 4 ]

2

[]

0

true

Family

Large ribosomal subunit protein eL15, archaeal

Ribosomal_eL15_arc

4

IPR020929

20,929

Large ribosomal subunit protein uL5, conserved site

Ribosomal_uL5_CS

Conserved_site

23,547

false

This entry represents a short conserved sequence found in the N-terminal region of the members of the large ribosomal subunit protein uL5 family. Large ribosomal subunit protein uL5, previously known as Ribosomal protein L5, is ~180 amino acids in length. In Escherichia coli, uL5 is known to be involved in binding 5S R...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PROSITE" ]

[ "PS00358" ]

[ "RIBOSOMAL_L5" ]

[ 23547 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706", "R-DDI-975956", "R-DDI-975957", "R-DME-156827", "R-DME-1799339", "R-DME-72689", "R-DME-72706", "R-DME-975956", "R-DME-975957...

[ "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-975956", "REACTOME:R-CEL-975957", "REACTOME:R-DDI-156827", "REACTOME:R-DDI-1799339", "REACTOME:R-DDI-72689", "REACTOME:R-DDI-72706", "REACTOME:R-DDI-975956", "REACTOME:R-DDI-97595...

57

[ "1ffk", "1iq4", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1mji", "1ml5", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn"...

1,612

[ "PUB00000599", "PUB00000693", "PUB00001802", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00104042" ]

[ "2198942", "1840500", "2016059", "11297922", "11290319", "11114498", "11866091" ]

[ "Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui.", "The structure of the gene for ribosomal protein L5 in the archaebacterium Sulfolobus acidocaldarius.", "Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21...

[ 1990, 1991, 1991, 2001, 2001, 2000, 2002 ]

7

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 372, 16496, 6438, 241 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 11, 2, 1, 2, 1, 4, 3, 1, 9, 5, 2, 2, 23 ]

13

true

Conserved_site

Large ribosomal subunit protein uL5, conserved site

Ribosomal_uL5_CS

2

IPR020930

20,930

Large ribosomal subunit protein uL5, bacteria

Ribosomal_uL5_bact

Family

49,555

false

This entry represents uL5 proteins mainly found in bacteria and chloroplasts. Large ribosomal subunit protein uL5, previously known as Ribosomal protein L5, is ~180 amino acids in length. In Escherichia coli, uL5 is known to be involved in binding 5S RNA to the large ribosomal subunit [ ]. Ribosomes are the particles t...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM", "PANTHER" ]

[ "MF_01333_B", "NF000585", "PTHR33284" ]

[ "Ribosomal_uL5_B", "PRK00010.1", "" ]

[ 25050, 25313, 24217 ]

3

[]

0

[ "1b75", "1d6k", "1dfu", "1feu", "1iq4", "1mji", "1ml5", "1njm", "1njp", "1nkw", "1nwx", "1nwy", "1sm1", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xbp", "2j28", "2rdo", "2zjp", "2zjq", "2zjr", "3bbx", "3cf5", "3dll", "3iyx", "3iyy", "3j3v", "3j5l", "3j5s"...

1,142

[ "PUB00000599", "PUB00000693", "PUB00001802", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00104042" ]

[ "2198942", "1840500", "2016059", "11297922", "11290319", "11114498", "11866091" ]

[ "Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui.", "The structure of the gene for ribosomal protein L5 in the archaebacterium Sulfolobus acidocaldarius.", "Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21...

[ 1990, 1991, 1991, 2001, 2001, 2000, 2002 ]

7

[ "IPR002132" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "candidate division MSBL1 archaeon SCGC-AAA382N08", "unclassified sequences" ]

[ 45674, 2958, 1, 1, 921 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 10, 2, 11, 13 ]

4

true

Family

Large ribosomal subunit protein uL5, bacteria

Ribosomal_uL5_bact

7

IPR020931

20,931

Decarboxylase MfnA, archaea

MfnA

Family

669

false

Members of this protein family are the archaeal form of decarboxylases. This entry includes TK1814 from Thermococcus kodakarensis. TK1814 functions as an aspartate 1-decarboxylase (ADC) and may be responsible for beta-alanine biosynthesis [ ].

[ "GO:0016831" ]

[ "carboxy-lyase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01610", "TIGR03812" ]

[ "MfnA_decarbox", "tyr_de_CO2_Arch" ]

[ 589, 668 ]

2

[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "4.1.1.11", "4.1.1.25", "PWY-3581", "PWY-5155", "PWY-5254", "PWY-5474", "PWY-6133", "PWY-6802", "PWY-7297", "PWY-7826" ]

[ "EC:4.1.1.11", "EC:4.1.1.25", "METACYC:PWY-3581", "METACYC:PWY-5155", "METACYC:PWY-5254", "METACYC:PWY-5474", "METACYC:PWY-6133", "METACYC:PWY-6802", "METACYC:PWY-7297", "METACYC:PWY-7826" ]

10

[ "3f9t", "6jy1", "6ldr", "6lds", "6ldt", "6m4y" ]

6

[ "PUB00076906" ]

[ "24415726" ]

[ "An archaeal glutamate decarboxylase homolog functions as an aspartate decarboxylase and is involved in β-alanine and coenzyme A biosynthesis." ]

[ 2014 ]

1

[]

0

null

[ "Archaea", "Bacteria", "ecological metagenomes" ]

[ 617, 41, 11 ]

3

[]

0

true

Family

Decarboxylase MfnA, archaea

MfnA

2

IPR020934

20,934

Small ribosomal subunit protein uS19, conserved site

Ribosomal_uS19_CS

Conserved_site

47,396

false

This entry represents a conserved site in the C-terminal section of the small ribosomal subunit protein uS19 family (in eukaryotes known as Ribosomal S15). The small subunit ribosomal proteins can be categorised as: primary binding proteins, which bind directly and independently to 16S rRNA; secondary binding proteins,...

[ "GO:0003723" ]

[ "RNA binding" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00323" ]

[ "RIBOSOMAL_S19" ]

[ 47396 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72649", "R-CEL-72689", "R-CEL-72695", "R-CEL-72702", "R-CEL-72706", "R-CEL-975956", ...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72702", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-179933...

92

[ "1fjg", "1fka", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1qkf", "1qkh", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo", "1xmq", "1xnq"...

1,739

[ "PUB00001612", "PUB00004907", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "2044758", "9371771", "11297922", "11290319", "11114498" ]

[ "rig encodes ribosomal protein S15. The primary structure of mammalian ribosomal protein S15.", "Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: str...

[ 1991, 1997, 2001, 2001, 2000 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 787, 22901, 23303, 405 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 30, 1, 1, 2, 1, 5, 3, 2, 10, 4, 2, 3, 34 ]

13

true

Conserved_site

Small ribosomal subunit protein uS19, conserved site

Ribosomal_uS19_CS

7

IPR020935

20,935

Phosphodiesterase YfcE, conserved site

PdiEstase_YfcE_CS

Conserved_site

2,886

false

This entry represents a short conserved sequence region found in a family of short, hydrophilic proteins that are all known or suspected phosphodiestreases. The best characterised of these is YfcE from Escherichia coli [ ]. The physiological substrate for this protein is not known, though it is capable of hydrolysing p...

[]

0

[ "PROSITE" ]

[ "PS01269" ]

[ "UPF0025" ]

[ 2886 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME" ]

[ "3.1.4.-", "PWY-5978", "PWY-6129", "PWY-6689", "PWY-7119", "PWY-7366", "R-DDI-3238698" ]

[ "EC:3.1.4.-", "METACYC:PWY-5978", "METACYC:PWY-6129", "METACYC:PWY-6689", "METACYC:PWY-7119", "METACYC:PWY-7366", "REACTOME:R-DDI-3238698" ]

7

[ "1s3l", "1s3m", "1s3n", "1su1", "2ahd" ]

5

[ "PUB00015606", "PUB00044047" ]

[ "15128743", "17586769" ]

[ "Structural and functional characterization of a novel phosphodiesterase from Methanococcus jannaschii.", "Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene." ]

[ 2004, 2007 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 483, 2035, 346, 22 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Conserved_site

Phosphodiesterase YfcE, conserved site

PdiEstase_YfcE_CS

7

IPR020936

20,936

tRNA uridine(34) hydroxylase

TrhO

Family

17,987

false

TrhO (also known as YceA in E. coli) catalyses oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-carboxymethoxyuridine (cmo5U) biosynthesis [ ]. This entry also includes uncharacterised proteins from archaea and plants.

[]

0

[ "HAMAP", "PANTHER" ]

[ "MF_00469", "PTHR43268" ]

[ "TrhO", "" ]

[ 14116, 15130 ]

2

[]

0

[ "4f67" ]

1

[ "PUB00094522" ]

[ "31253794" ]

[ "Dual pathways of tRNA hydroxylation ensure efficient translation by expanding decoding capability." ]

[ 2019 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobacteriati", "unclassified sequences" ]

[ 13843, 3879, 12, 253 ]

4

[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 15, 2, 1, 4, 1, 11, 4, 17 ]

8

true

Family

tRNA uridine(34) hydroxylase

TrhO

6

IPR020939

20,939

Large ribosomal subunit protein bL34, conserved site

Ribosomal_bL34_CS

Conserved_site

19,310

false

This entry represents a conserved site from ribosomal protein L34 (also known as Large ribosomal subunit protein bL34), one of the proteins from the large subunit of the ribosome from bacteria. It is a small basic protein of 44 to 51 amino-acid residues [ ]. L34 belongs to a family of ribosomal proteins which, on the b...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PROSITE" ]

[ "PS00784" ]

[ "RIBOSOMAL_L34" ]

[ 19310 ]

1

[]

0

[ "1nkw", "1nwx", "1nwy", "1sm1", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xbp", "2j28", "2rdo", "2zjp", "2zjq", "2zjr", "3bbx", "3cf5", "3dll", "3j3v", "3j3w", "3j5l", "3j7z", "3j8g", "3j9w", "3j9y", "3j9z", "3ja1", "3jbu", "3jbv", "3jcd", "3jce", "3jcj"...

1,157

[ "PUB00004412", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "1461740", "11297922", "11290319", "11114498" ]

[ "Nucleotide sequence of the Borrelia burgdorferi rpmH gene encoding ribosomal protein L34.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 1992, 2001, 2001, 2000 ]

4

[]

0

null

[ "Bacteria", "Eukaryota", "candidate division MSBL1 archaeon SCGC-AAA382N08", "unclassified sequences" ]

[ 18381, 712, 1, 216 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 5, 1, 2, 5 ]

4

true

Conserved_site

Large ribosomal subunit protein bL34, conserved site

Ribosomal_bL34_CS

9

IPR020940

20,940

Thymidylate synthase, active site

Thymidylate_synthase_AS

Active_site

20,519

false

Thymidylate synthase ( ) [ , ] catalyzes the reductive methylation of dUMP to dTMP with concomitant conversion of 5,10-methylenetetrahydrofolate to dihydrofolate: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP This provides the sole de novo pathway for production of dTMP and is the only enzyme in folate m...

[ "GO:0004799", "GO:0006231" ]

[ "thymidylate synthase activity", "dTMP biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE" ]

[ "PS00091" ]

[ "THYMIDYLATE_SYNTHASE" ]

[ 20519 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.1.1.45", "PWY-3841", "PWY-7184", "PWY-7187", "PWY-7198", "PWY-7199", "PWY-7210", "R-DME-499943", "R-HSA-499943", "R-HSA-69205", "R-MMU-499943", "R-RNO-499943", "R-SCE-499943", "R-SPO-499943" ]

[ "EC:2.1.1.45", "METACYC:PWY-3841", "METACYC:PWY-7184", "METACYC:PWY-7187", "METACYC:PWY-7198", "METACYC:PWY-7199", "METACYC:PWY-7210", "REACTOME:R-DME-499943", "REACTOME:R-HSA-499943", "REACTOME:R-HSA-69205", "REACTOME:R-MMU-499943", "REACTOME:R-RNO-499943", "REACTOME:R-SCE-499943", "REACT...

14

[ "1aiq", "1ajm", "1an5", "1aob", "1axw", "1b02", "1bdu", "1bid", "1bjg", "1bko", "1bkp", "1bo7", "1bo8", "1bp0", "1bp6", "1bq1", "1bq2", "1bsf", "1bsp", "1ci7", "1ddu", "1dna", "1ev5", "1ev8", "1evf", "1evg", "1f28", "1f4b", "1f4c", "1f4e", "1f4f", "1f4g"...

327

[ "PUB00000031", "PUB00000137", "PUB00002591", "PUB00005100", "PUB00030463", "PUB00036705", "PUB00037605", "PUB00081476", "PUB00081477", "PUB00081481" ]

[ "6996564", "2117882", "2243092", "3099389", "14555647", "16615077", "16511011", "16162288", "16178783", "7574499" ]

[ "On the mechanism of action of folate- and biopterin-requiring enzymes.", "Cloning and characterization of the thymidylate synthase gene from Lactococcus lactis subsp. lactis.", "Structural and functional analysis of the human thymidylate synthase gene.", "Atomic structure of thymidylate synthase: target for ...

[ 1980, 1990, 1990, 1987, 2003, 2006, 2005, 2005, 2005, 1995 ]

10

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobacteriati", "Viruses", "unclassified sequences" ]

[ 14680, 4988, 36, 566, 249 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 9, 2, 1, 2, 1, 4, 7, 1, 6, 3, 1, 1, 14 ]

13

true

Active_site

Thymidylate synthase, active site

Thymidylate_synthase_AS

5

IPR020941

20,941

Suppressor of fused-like domain

SUFU-like_domain

Domain

7,989

false

Sufu, encoding the human ortholog of Drosophila suppressor of fused, appears to have a conserved role in the repression of Hedgehog signalling [ ]. It is a repressor of the Gli and Ci transcription factors of the Hedgehog signalling cascade [ ], and functions by binding these proteins and preventing their translocation...

[]

0

[ "PFAM" ]

[ "PF05076" ]

[ "SUFU" ]

[ 7989 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-5610780", "R-HSA-5610783", "R-HSA-5610785", "R-HSA-5610787", "R-HSA-5632684", "R-MMU-5610780", "R-MMU-5610785", "R-MMU-5610787", "R-MMU-5632684" ]

[ "REACTOME:R-HSA-5610780", "REACTOME:R-HSA-5610783", "REACTOME:R-HSA-5610785", "REACTOME:R-HSA-5610787", "REACTOME:R-HSA-5632684", "REACTOME:R-MMU-5610780", "REACTOME:R-MMU-5610785", "REACTOME:R-MMU-5610787", "REACTOME:R-MMU-5632684" ]

9

[ "1m1l", "3k5j", "4bl8", "4bl9", "4bla", "4blb", "4bld", "4km8", "4km9", "4kma", "4kmd", "4kmh", "6lph" ]

13

[ "PUB00010225", "PUB00010226", "PUB00028921", "PUB00070721", "PUB00101092", "PUB00101143" ]

[ "12150819", "12068298", "15367681", "22200572", "34280190", "28965847" ]

[ "Medulloblastoma: a problem of developmental biology.", "Mutations in SUFU predispose to medulloblastoma.", "Suppressor of fused regulates Gli activity through a dual binding mechanism.", "A novel family of toxin/antitoxin proteins in Bacillus species.", "Diverse LXG toxin and antitoxin systems specifically...

[ 2002, 2002, 2004, 2012, 2021, 2017 ]

6

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobacteriati", "metagenomes" ]

[ 6055, 1903, 12, 19 ]

4

[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 4, 2, 4, 4, 4 ]

5

true

Domain

Suppressor of fused-like domain

SUFU-like_domain

5

IPR020944

20,944

Nodulation protein S

NodS

Family

209

false

This entry consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involve...

[ "GO:0008757", "GO:0009312" ]

[ "S-adenosylmethionine-dependent methyltransferase activity", "oligosaccharide biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM", "PIRSF" ]

[ "NF041650", "PIRSF009310" ]

[ "nod_mtase_NodS", "NodS" ]

[ 200, 209 ]

2

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...

[ "2.1.1.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601", "PWY-6045"...

[ "EC:2.1.1.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", "METACYC:PWY-5...

146

[ "3ofj", "3ofk" ]

2

[ "PUB00011401" ]

[ "11344149" ]

[ "Rhizobial NodL O-acetyl transferase and NodS N-methyl transferase functionally interfere in production of modified Nod factors." ]

[ 2001 ]

1

[ "IPR008715" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 209 ]

1

[]

0

true

Family

Nodulation protein S

NodS

7

IPR020945

20,945

DMSO/Nitrate reductase chaperone

DMSO/NO3_reduct_chaperone

Family

18,822

false

This entry represents a family of proteins which are involved in enzymes assembly and/or maturation: The TorD protein is involved in the maturation of the the trimethylamine N-oxide reductase TorA (a DMSO reductase family member) in Escherichia coli [ ]. TorA is a molybdenum-containing enzyme which requires the the ins...

[]

0

[ "PFAM" ]

[ "PF02613" ]

[ "Nitrate_red_del" ]

[ 18822 ]

1

[ "GP" ]

[ "GenProp0127" ]

[ "GP:GenProp0127" ]

1

[ "1n1c", "1s9u", "2idg", "2o9x", "2xol", "2y6y", "2yjm", "3cw0", "3efp", "3u41", "8jzc", "8jzd", "9m26" ]

13

[ "PUB00012283", "PUB00017539", "PUB00042993", "PUB00053977", "PUB00053978", "PUB00058076", "PUB00058081", "PUB00058082", "PUB00058083", "PUB00058084" ]

[ "12766163", "9632249", "12067345", "1732220", "9305880", "22289056", "12527378", "12813051", "20169075", "16540088" ]

[ "Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA.", "NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli.", "Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the ...

[ 2003, 1998, 2002, 1992, 1997, 2012, 2003, 2003, 2010, 2006 ]

10

[]

[ "IPR003765", "IPR017843", "IPR023069", "IPR026269" ]

0

4

0

[ "Archaea", "Bacteria", "Escherichia phage RCS47", "Eukaryota", "unclassified sequences" ]

[ 562, 18056, 1, 12, 191 ]

5

[ "Escherichia coli (strain K12)" ]

[ 5 ]

1

true

Family

DMSO/Nitrate reductase chaperone

DMSO/NO3_reduct_chaperone

6

IPR020946

20,946

Flavin monooxygenase-like

Flavin_mOase-like

Family

68,128

false

Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes [ ]. Using an NADPH cofactor and FAD prosthetic group, these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorus and selenium atoms in a range of structurally diverse compounds. FMOs hav...

[ "GO:0004499", "GO:0050660", "GO:0050661" ]

[ "N,N-dimethylaniline monooxygenase activity", "flavin adenine dinucleotide binding", "NADP binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "PFAM" ]

[ "PF00743" ]

[ "FMO-like" ]

[ 68128 ]

1

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "1.14.13", "GenProp1464", "R-BTA-217271", "R-CFA-1614558", "R-CFA-217271", "R-HSA-1614558", "R-HSA-217271", "R-HSA-5579019", "R-MMU-1614558", "R-MMU-217271", "R-RNO-1614558", "R-RNO-217271", "R-SSC-1614558", "R-SSC-217271" ]

[ "EC:1.14.13", "GP:GenProp1464", "REACTOME:R-BTA-217271", "REACTOME:R-CFA-1614558", "REACTOME:R-CFA-217271", "REACTOME:R-HSA-1614558", "REACTOME:R-HSA-217271", "REACTOME:R-HSA-5579019", "REACTOME:R-MMU-1614558", "REACTOME:R-MMU-217271", "REACTOME:R-RNO-1614558", "REACTOME:R-RNO-217271", "REAC...

14

[ "1vqw", "1w4x", "2gv8", "2gvc", "2vq7", "2vqb", "2xlp", "2xlr", "2xls", "2xlt", "2xlu", "2xve", "2xvf", "2xvh", "2xvi", "2xvj", "2ylr", "2yls", "2ylt", "2ylw", "2ylz", "2ym1", "2ym2", "3gwd", "3gwf", "3ucl", "4aos", "4aox", "4ap1", "4ap3", "4c74", "4c77"...

81

[ "PUB00000158", "PUB00000516", "PUB00002611", "PUB00002642", "PUB00002834", "PUB00004772", "PUB00005185", "PUB00082329", "PUB00101886" ]

[ "8311461", "1417778", "2318837", "1712018", "8486656", "1542660", "8091229", "27166860", "32156684" ]

[ "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities.", "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family.", "The flavin-containing monooxygenase enzymes expressed in...

[ 1994, 1992, 1990, 1991, 1993, 1992, 1994, 2016, 2020 ]

9

[]

[ "IPR000960" ]

0

1

0

[ "Bacteria", "Eukaryota", "Halobacteriales", "Sym plasmid", "metagenomes" ]

[ 18784, 49001, 16, 1, 326 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 111, 9, 8, 4, 25, 25, 12, 76, 31, 1, 1, 113 ]

12

true

Family

Flavin monooxygenase-like

Flavin_mOase-like

5

IPR020951

20,951

Mitochondrial import receptor subunit Tom22, fungi

Tom22_fungi

Family

30

false

Tom22 is a central component of the TOM (Translocase of Outer Membrane) complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with tom20, it functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates t...

[ "GO:0030150", "GO:0005741", "GO:0005742" ]

[ "protein import into mitochondrial matrix", "mitochondrial outer membrane", "mitochondrial outer membrane translocase complex" ]

[ "biological_process", "cellular_component", "cellular_component" ]

3

[ "NCBIFAM" ]

[ "TIGR00986" ]

[ "3a0801s05tom22" ]

[ 30 ]

1

[]

0

[ "6jnf", "6ucu", "6ucv", "8b4i", "8hco", "8w5j", "8w5k", "8xkw", "8xkx", "8xky", "9j99" ]

11

[ "PUB00054239", "PUB00074948" ]

[ "10519552", "15523480" ]

[ "Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase.", "Assembling the mitochondrial outer membrane." ]

[ 1999, 2004 ]

2

[ "IPR005683" ]

[]

1

0

1

[ "Ascomycota" ]

[ 30 ]

1

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 1, 1, 1 ]

3

true

Family

Mitochondrial import receptor subunit Tom22, fungi

Tom22_fungi

5

IPR020952

20,952

Antitermination protein N, arginine-rich motif

Antiterm_prot_N_Arg-rich

Family

117

false

Antitermination proteins positively regulate expression of bacteriophage early and late gene operons [ ]. Bacterial host RNA polymerase is modified by these antitermination proteins to a terminator-resistant form that transcribes through termination sites that would otherwise prevent expression of the regulated genes. ...

[]

0

[ "PFAM" ]

[ "PF11438" ]

[ "N36" ]

[ 117 ]

1

[]

0

[ "1qfq", "5lm7", "5ms0", "6gov", "7a4f", "7a4g", "7a4h", "7a4i", "7a4j" ]

9

[ "PUB00034623", "PUB00053256" ]

[ "10759866", "9882646" ]

[ "Antitermination in bacteriophage lambda. The structure of the N36 peptide-boxB RNA complex.", "Processive antitermination." ]

[ 2000, 1999 ]

2

[]

0

null

[ "Bacteria", "Timema douglasi", "Viruses" ]

[ 99, 1, 17 ]

3

[]

0

true

Family

Antitermination protein N, arginine-rich motif

Antiterm_prot_N_Arg-rich

4

IPR020954

20,954

Antigenic heat-stable 120 kDa protein, N-terminal domain

Sca4_N

Domain

237

false

This domain is found in Antigenic heat-stable 120 kDa protein. Sca4 (surface cell antigen 4 or Antigenic heat-stable 120 kDa protein) is a surface protein of Rickettsia (intracellular pathogens) that mediates protrusion from an infected cell and engulfment by the adjacent cell in order to mediate spreading [ , ].

[]

0

[ "PFAM" ]

[ "PF12574" ]

[ "120_Rick_ant" ]

[ 237 ]

1

[]

0

[ "4lq8" ]

1

[ "PUB00053371", "PUB00105746", "PUB00105747" ]

[ "8112862", "21841197", "27768890" ]

[ "Cloning, sequencing, and expression of the gene coding for an antigenic 120-kilodalton protein of Rickettsia conorii.", "The rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin.", "Rickettsia Sca4 Reduces Vinculin-Mediated Intercellular Tension to Promote Spread." ]

[ 1994, 2011, 2016 ]

3

[]

0

null

[ "Rickettsiaceae", "Spiralia" ]

[ 234, 3 ]

2

[]

0

true

Domain

Antigenic heat-stable 120 kDa protein, N-terminal domain

Sca4_N

5

IPR020955

20,955

Uncharacterised protein family Atu4866

Uncharacterised_Atu4866

Family

1,702

false

The function of the proteins in this entry is not known, though Atu4866 from Agrobacterium tumefaciens has been structurally characterised. Atu4866 adopts a streptavidin-like fold and has a β-barrel/sandwich which is formed by eight antiparallel β-strands [ ]. Atu4866 has a potential ligand-binding site where it has a ...

[]

0

[ "PFAM" ]

[ "PF11512" ]

[ "Atu4866" ]

[ 1702 ]

1

[]

0

[ "2jmb" ]

1

[ "PUB00053257" ]

[ "18042676" ]

[ "The hypothetical protein Atu4866 from Agrobacterium tumefaciens adopts a streptavidin-like fold." ]

[ 2008 ]

1

[]

0

null

[ "Bacteria", "Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211)", "metagenomes" ]

[ 1696, 1, 5 ]

3

[]

0

true

Family

Uncharacterised protein family Atu4866

Uncharacterised_Atu4866

4

IPR020956

20,956

Transcription factor Aft1, osmotic stress domain

TF_Aft1_OSM

Domain

1,418

false

This region is found in the transcription factor Aft1 which is required for a wide range of stress responses. The OSM domain has been shown to be involved in the osmotic stress response [ ]. Atf1 is a bZIP family transcription factor found in the postharvest pathogen Penicillium expansum (blue mould rot fungus). It pos...

[]

0

[ "PFAM" ]

[ "PF11785" ]

[ "Aft1_OSA" ]

[ 1418 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-SCE-3214847", "R-SCE-450341", "R-SPO-3214847", "R-SPO-450341" ]

[ "REACTOME:R-SCE-3214847", "REACTOME:R-SCE-450341", "REACTOME:R-SPO-3214847", "REACTOME:R-SPO-450341" ]

4

[]

0

[ "PUB00053258", "PUB00163232" ]

[ "18375981", "39802737" ]

[ "Distinct regions of ATF/CREB proteins Atf1 and Pcr1 control recombination hotspot ade6-M26 and the osmotic stress response.", "Chromatin accessibility profile and the role of PeAtf1 transcription factor in the postharvest pathogen <i>Penicillium expansum</i>." ]

[ 2008, 2025 ]

2

[]

0

null

[ "Eukaryota", "marine metagenome" ]

[ 1417, 1 ]

2

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 2, 1, 1 ]

3

true

Domain

Transcription factor Aft1, osmotic stress domain

TF_Aft1_OSM

8

IPR020957

20,957

Tachystatin B

Tachystatin_B

Family

2

false

Tachystatin B is an antimicrobial chitin binding peptide and consists of two isotopes B1 and B2. Both structures contain a short antiparallel β sheet with an inhibitory cysteine knot motif. Tyr(14) and Arg(17) are thought to be the essential residues for chitin binding [ ].

[]

0

[ "PFAM" ]

[ "PF11478" ]

[ "Tachystatin_B" ]

[ 2 ]

1

[]

0

[ "2dcv", "2dcw" ]

2

[ "PUB00040215" ]

[ "17394123" ]

[ "The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif." ]

[ 2007 ]

1

[]

0

null

[ "Tachypleus tridentatus" ]

[ 2 ]

1

[]

0

true

Family

Tachystatin B

Tachystatin_B

2

IPR020958

20,958

Domain of unknown function DUF3686

DUF3686

Domain

2,004

false

This entry represents an N-terminal domain associated with ATPases and some uncharacterised proteins; it is approximately 450 amino acids in length and contains two conserved sequence motifs: DVF and SPNGED.

[]

0

[ "PFAM" ]

[ "PF12458" ]

[ "DUF3686" ]

[ 2004 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 1991, 4, 9 ]

3

[]

0

true

Domain

Domain of unknown function DUF3686

DUF3686

9

IPR020959

20,959

Arabinofuranosyltransferase AftA, C-terminal

ArabinofuranosylTrfase_AftA_C

Domain

1,099

false

The arabinofuranosyltransferase enzyme AftA is involved in cell wall arabinan biosynthesis in bacteria [ ]. It catalyses the addition of the first key arabinofuranosyl residue from the sugar donor beta-D-arabinofuranosyl-1-monophosphoryldecaprenol to the galactan domain of the cell wall, thus priming the galactan for f...

[ "GO:0016757", "GO:0044038", "GO:0005886", "GO:0016020" ]

[ "glycosyltransferase activity", "cell wall macromolecule biosynthetic process", "plasma membrane", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

4

[ "PFAM" ]

[ "PF12249" ]

[ "AftA_C" ]

[ 1099 ]

1

[ "EC", "METACYC" ]

[ "2.4.2.46", "PWY-6397" ]

[ "EC:2.4.2.46", "METACYC:PWY-6397" ]

2

[ "8if8" ]

1

[ "PUB00053259" ]

[ "16595677" ]

[ "Identification of a novel arabinofuranosyltransferase (AftA) involved in cell wall arabinan biosynthesis in Mycobacterium tuberculosis." ]

[ 2006 ]

1

[]

0

null

[ "Bacteria", "freshwater metagenome" ]

[ 1098, 1 ]

2

[]

0

true

Domain

Arabinofuranosyltransferase AftA, C-terminal

ArabinofuranosylTrfase_AftA_C

4

IPR020960

20,960

Aleutian mink disease parvovirus non-structural protein 1-3

ADV_NS1-3

Domain

1,013

false

This entry represents a domain found in Aleutian mink disease parvovirus (ADV) non-structural protein 1-3 (NS1-3). It is approximately 50 amino acids in length. ADV utilizes caspase activity to cleave its major non-structural protein (NS1), enable the localization of this protein to the nucleus and facilitate virus rep...

[]

0

[ "PFAM" ]

[ "PF12475" ]

[ "Amdo_NSP_1-3" ]

[ 1013 ]

1

[]

0

[]

0

[ "PUB00053398", "PUB00099776", "PUB00099778" ]

[ "7998830", "12692232", "24606679" ]

[ "Sequence comparison of the non-structural genes of four different types of Aleutian mink disease parvovirus indicates an unusual degree of variability.", "Caspase cleavage of the nonstructural protein NS1 mediates replication of Aleutian mink disease parvovirus.", "Molecular characterization of the small nonst...

[ 1994, 2003, 2014 ]

3

[]

0

null

[ "Amdoparvovirus" ]

[ 1013 ]

1

[]

0

true

Domain

Aleutian mink disease parvovirus non-structural protein 1-3

ADV_NS1-3

9

IPR020961

20,961

Domain of unknown function DUF3642, lipoprotein

DUF3642_lipo

Domain

484

false

This domain is found in proteins which are major virulence factors from Gram-negative bacteria and is approximately 60 amino acids in length. There is a single completely conserved Y residue that may be functionally important.

[]

0

[ "PFAM" ]

[ "PF12182" ]

[ "DUF3642" ]

[ 484 ]

1

[]

0

[ "3ge2", "5cyb" ]

2

[]

0

[]

0

null

[ "Bacteria", "human gut metagenome" ]

[ 483, 1 ]

2

[]

0

true

Domain

Domain of unknown function DUF3642, lipoprotein

DUF3642_lipo

3

IPR020962

20,962

Bacteriophage phiX174, GpK

Phage_phiX174_GpK

Family

82

false

This family of proteins is found in the microviridae (isometric ssDNA phages) and are approximately 60 amino acids in length. The function of these proteins are unknown. In phi X174 site-directed mutagenesis of gene K produces small plaques on su- hosts. The mutant phage has an identical latent period, but a more reduc...

[]

0

[ "PFAM" ]

[ "PF12283" ]

[ "Protein_K" ]

[ 82 ]

1

[]

0

[]

0

[ "PUB00053261" ]

[ "3155803" ]

[ "Gene K of bacteriophage phi X174 codes for a protein which affects the burst size of phage production." ]

[ 1985 ]

1

[]

0

null

[ "Bacteria", "Bullavirinae", "Opisthokonta" ]

[ 15, 65, 2 ]

3

[]

0

true

Family

Bacteriophage phiX174, GpK

Phage_phiX174_GpK

7

IPR020963

20,963

Arabinofuranosyltransferase AftA, N-terminal

ArabinofuranosylTrfase_AftA_N

Domain

1,146

false

The arabinofuranosyltransferase enzyme AftA is involved in cell wall arabinan biosynthesis in bacteria [ ]. It catalyses the addition of the first key arabinofuranosyl residue from the sugar donor beta-D-arabinofuranosyl-1-monophosphoryldecaprenol to the galactan domain of the cell wall, thus priming the galactan for f...

[ "GO:0016757", "GO:0044038", "GO:0005886", "GO:0016020" ]

[ "glycosyltransferase activity", "cell wall macromolecule biosynthetic process", "plasma membrane", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

4

[ "PFAM" ]

[ "PF12250" ]

[ "AftA_N" ]

[ 1146 ]

1

[ "EC", "METACYC" ]

[ "2.4.2.46", "PWY-6397" ]

[ "EC:2.4.2.46", "METACYC:PWY-6397" ]

2

[ "8if8" ]

1

[ "PUB00053259" ]

[ "16595677" ]

[ "Identification of a novel arabinofuranosyltransferase (AftA) involved in cell wall arabinan biosynthesis in Mycobacterium tuberculosis." ]

[ 2006 ]

1

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 1143, 3 ]

2

[]

0

true

Domain

Arabinofuranosyltransferase AftA, N-terminal

ArabinofuranosylTrfase_AftA_N

9

IPR020964

20,964

Acyl-CoA dehydrogenase, C-terminal

Acyl-CoA_dehydrogenase_C

Domain

637

false

This entry represents the C-terminal α helical domain of some bacterial Acyl-CoA dehydrogenases. It is found in association with , , . There is a conserved ARRL sequence motif.

[]

0

[ "PFAM" ]

[ "PF12186" ]

[ "AcylCoA_dehyd_C" ]

[ 637 ]

1

[]

0

[ "2oku" ]

1

[]

0

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 596, 41 ]

2

[]

0

true

Domain

Acyl-CoA dehydrogenase, C-terminal

Acyl-CoA_dehydrogenase_C

5

IPR020965

20,965

Aromatic prenyltransferase, CloQ-type

Prenyltransferase_CloQ

Family

384

false

This entry includes prenyltransferase-like proteins, including: Aromatic prenyltransferases NovQ from Streptomyces niveus and CloQ from Streptomyces roseochromogenes. They catalyse the transfer of a dimethylallyl group to 4-hydroxyphenylpyruvate to produce the ring A structure in the novobiocin and clorobiocin biosynth...

[ "GO:0016740" ]

[ "transferase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "SFLD", "CDD" ]

[ "PF11468", "SFLDG01163", "cd13931" ]

[ "PTase_Orf2", "II", "PT-CloQ_NphB" ]

[ 384, 329, 203 ]

3

[]

0

[ "1zb6", "1zcw", "1zdw", "1zdy", "2xlq", "2xly", "2xm5", "2xm7", "4ee6", "4ee7", "4ee8", "5y4g", "5y72", "5y7c", "5y84", "5yk9", "5ynt", "5ynu", "5ynv", "5ynw", "5z43", "5z44", "5z45", "5z46", "7fhb", "7fhc", "7fhd", "7fhe", "7fhf" ]

29

[ "PUB00072698", "PUB00072699", "PUB00072911", "PUB00072912", "PUB00072913" ]

[ "19557032", "12618544", "17543953", "17103476", "19339241" ]

[ "NovQ is a prenyltransferase capable of catalyzing the addition of a dimethylallyl group to both phenylpropanoids and flavonoids.", "CloQ, a prenyltransferase involved in clorobiocin biosynthesis.", "A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylatio...

[ 2009, 2003, 2007, 2006, 2009 ]

5

[ "IPR033964" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "marine sediment metagenome" ]

[ 276, 106, 2 ]

3

[]

0

true

Family

Aromatic prenyltransferase, CloQ-type

Prenyltransferase_CloQ

8

IPR020966

20,966

Aluminum-activated malate transporter

ALMT

Family

8,065

false

This entry represents a malate transporter which has been is identified as being critical for aluminium tolerance in Arabidopsis thaliana [ , , , ]. Some family members have been reported to be permeable to chloride, nitrate, sulphate and malate [ , , , ].

[]

0

[ "PFAM" ]

[ "PF11744" ]

[ "ALMT" ]

[ 8065 ]

1

[]

0

[ "7voj", "7vq3", "7vq4", "7vq5", "7vq7", "7w6k", "8hiw", "8hiy", "8zte", "8ztg", "8zth", "8zti", "8ztj", "8ztk", "8ztl", "8ztm", "8ztn", "8zvf", "9jtw" ]

19

[ "PUB00053262", "PUB00059247", "PUB00059248", "PUB00059249", "PUB00059250", "PUB00059251", "PUB00059252", "PUB00059253" ]

[ "16740662", "17885092", "18826429", "19321711", "14871306", "16391684", "15769806", "18550686" ]

[ "AtALMT1, which encodes a malate transporter, is identified as one of several genes critical for aluminum tolerance in Arabidopsis.", "Characterization of AtALMT1 expression in aluminum-inducible malate release and its role for rhizotoxic stress tolerance in Arabidopsis.", "Aluminum-activated citrate and malate...

[ 2006, 2007, 2009, 2009, 2004, 2005, 2005, 2008 ]

8

[]

0

null

[ "Bacteria", "Eukaryota", "viral metagenome" ]

[ 38, 8026, 1 ]

3

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 65, 33, 1, 34 ]

4

true

Family

Aluminum-activated malate transporter

ALMT

8

IPR020967

20,967

Borrelia attachment ligand, p66

Borrelia_attachment_p66

Family

239

false

Borrelia burgdorferi, the agent of Lyme disease, expresses several adhesion molecules that are probably required for initial establishment of infection in mammalian hosts, and for colonization of various tissues within the host.

[]

0

[ "PFAM" ]

[ "PF11263" ]

[ "Attachment_P66" ]

[ 239 ]

1

[]

0

[]

0

[ "PUB00053263" ]

[ "12748384" ]

[ "Targeted mutation of the outer membrane protein P66 disrupts attachment of the Lyme disease agent, Borrelia burgdorferi, to integrin alphavbeta3." ]

[ 2003 ]

1

[]

0

null

[ "Borreliaceae", "Menopon gallinae" ]

[ 238, 1 ]

2

[]

0

true

Family

Borrelia attachment ligand, p66

Borrelia_attachment_p66

6

IPR020968

20,968

Bacteriocin class II, aureocin-like

Bacteriocin_II_aureocin-like

Family

57

false

This is a small family of type II bacteriocins usually encoded on a plasmid. Characteristically the members are small, cationic, rich in Lys and Try, and bring about a generalised membrane permeabilisation leading to leakage of ions. The family includes aureocin A, lacticins Q and Z, and BhtB [ , ].

[]

0

[ "PFAM" ]

[ "PF11758" ]

[ "Bacteriocin_IIi" ]

[ 57 ]

1

[]

0

[ "2n8o", "2n8p", "6sif", "6sig", "7p5r", "8avr", "8avs", "8avt", "8avu" ]

9

[ "PUB00053395", "PUB00053396" ]

[ "12054867", "12406714" ]

[ "Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus.", "Mode of action of the antimicrobial peptide aureocin A53 from Staphylococcus aureus." ]

[ 2002, 2002 ]

2

[]

0

null

[ "Bacillati" ]

[ 57 ]

1

[]

0

true

Family

Bacteriocin class II, aureocin-like

Bacteriocin_II_aureocin-like

5

IPR020969

20,969

Ankyrin-G binding site

Ankyrin-G_BS

Binding_site

2,833

false

Interactions with ankyrin-G are crucial to the localisation of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localise sodium channels to a varie...

[ "GO:0005267", "GO:0016020" ]

[ "potassium channel activity", "membrane" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM" ]

[ "PF11956" ]

[ "KCNQC3-Ank-G_bd" ]

[ 2833 ]

1

[ "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-1296072", "R-HSA-1296072", "R-HSA-445095" ]

[ "REACTOME:R-BTA-1296072", "REACTOME:R-HSA-1296072", "REACTOME:R-HSA-445095" ]

3

[ "8xo1" ]

1

[ "PUB00053264", "PUB00053265", "PUB00053266", "PUB00053267", "PUB00053268" ]

[ "12716895", "16525039", "16735477", "17311847", "19112491" ]

[ "Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits.", "A common ankyrin-G-based mechanism retains KCNQ and NaV channels at electrically active domains of the axon.", "Polarized axonal surface expression of neuronal KCNQ channels is mediated by multiple signals in...

[ 2003, 2006, 2006, 2007, 2008 ]

5

[]

0

null

[ "Gnathostomata" ]

[ 2833 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 15, 9, 9, 9 ]

4

true

Binding_site

Ankyrin-G binding site

Ankyrin-G_BS

1

IPR020970

20,970

Bacteriocin class IIc

Bacteriocin_IIc

Family

19

false

This class of bacteriocins was previously described as class V. The members include gassericin A, acidocin B and butyrovibriocin AR10, all of which are hydrophobic cyclical structures [ ]. The N- and C-termini are covalently linked, and the circular molecule is resistant to several proteases and peptidases [ ]. The imm...

[]

0

[ "PFAM" ]

[ "PF12173" ]

[ "BacteriocIIc_cy" ]

[ 19 ]

1

[]

0

[ "2mwr", "6wi6" ]

2

[ "PUB00053269", "PUB00053270", "PUB00053271" ]

[ "7551031", "15544534", "19114506" ]

[ "Genetic analysis of acidocin B, a novel bacteriocin produced by Lactobacillus acidophilus.", "The circular bacteriocins gassericin A and circularin A.", "DNA sequencing and homologous expression of a small peptide conferring immunity to gassericin A, a circular bacteriocin produced by Lactobacillus gasseri LA3...

[ 1995, 2004, 2009 ]

3

[]

0

null

[ "Bacillota" ]

[ 19 ]

1

[]

0

true

Family

Bacteriocin class IIc

Bacteriocin_IIc

2

IPR020971

20,971

ATP synthase, F1 beta subunit

ATP_synth_F1_beta_su

Domain

1,074

false

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. This entry represents the beta subunit of the F1 component. The NMR solution structure of the protein in SDS micell...

[ "GO:0005524", "GO:0016887", "GO:0006754", "GO:0045259" ]

[ "ATP binding", "ATP hydrolysis activity", "ATP biosynthetic process", "proton-transporting ATP synthase complex" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "PFAM" ]

[ "PF11421" ]

[ "Synthase_beta" ]

[ 1074 ]

1

[ "EC", "METACYC" ]

[ "7.1.2.2", "PWY-7980" ]

[ "EC:7.1.2.2", "METACYC:PWY-7980" ]

2

[ "1pyv" ]

1

[ "PUB00030047" ]

[ "15037074" ]

[ "NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia." ]

[ 2004 ]

1

[]

0

null

[ "Magnoliopsida" ]

[ 1074 ]

1

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 10, 5, 15 ]

3

true

Domain

ATP synthase, F1 beta subunit

ATP_synth_F1_beta_su

8

IPR020972

20,972

Dermonecrotic/RTX toxin, membrane localization domain

Dermonecrotic/RTX_toxin_MLD

Domain

266

false

This is a membrane localisation domain found in multiple families of bacterial toxins including some clostridial glucosyltransferase toxins and various MARTX toxins (multifunctional-autoprocessing RTX toxins) [ ]. In the Pasteurella multocida toxin (PMT, also known as dermonecrotic toxin) C-terminal fragment, structura...

[]

0

[ "PFAM" ]

[ "PF11647" ]

[ "MLD" ]

[ 266 ]

1

[]

0

[ "2ebf", "2ebh", "2ec5", "2n9v", "2n9w", "4err", "5w6l", "5xn7", "6a7h", "6a8j" ]

10

[ "PUB00040389", "PUB00053274", "PUB00085052" ]

[ "17360394", "17464284", "20212166" ]

[ "Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin.", "Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain.", "Identification of a conserved membrane localization domain within numerous large bacterial protein toxi...

[ 2007, 2007, 2010 ]

3

[]

0

null

[ "Pseudomonadati" ]

[ 266 ]

1

[]

0

true

Domain

Dermonecrotic/RTX toxin, membrane localization domain

Dermonecrotic/RTX_toxin_MLD

3

IPR020973

20,973

Packaging enzyme P4

Packaging_enz_P4

Family

13

false

This entry represents P4, a packaging motor which is involved in the packaging of Pseudomonas bacteriophage genomes into preformed capsids using ATP. The P4 protein is located at the vertices of the icosahedral capsid. ATP drives RNA translocation through cooperative conformational changes [ ].

[ "GO:0019072" ]

[ "viral genome packaging" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF11602" ]

[ "NTPase_P4" ]

[ 13 ]

1

[]

0

[ "1w44", "1w46", "1w47", "1w48", "1w49", "1w4a", "1w4b", "1w4c", "2vhc", "2vhj", "2vhq", "2vht", "2vhu", "4blo", "4blp", "4blq", "4blr", "4bls", "4blt", "4bwy", "5muu", "5muv", "5muw", "6hy0", "7eso", "7esp", "7esq", "7esv" ]

28

[ "PUB00032176" ]

[ "15369673" ]

[ "Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation." ]

[ 2004 ]

1

[]

0

null

[ "Cystoviridae" ]

[ 13 ]

1

[]

0

true

Family

Packaging enzyme P4

Packaging_enz_P4

5

IPR020974

20,974

CGT/MARTX, cysteine protease (CPD) domain

CPD_dom

Domain

943

false

Large bacterial protein toxins autotranslocate functional effector domains to the eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Gram-positive bacteria and the multifuncti...

[]

0

[ "PFAM", "PROFILE" ]

[ "PF11713", "PS51771" ]

[ "Peptidase_C80", "CGT_MARTX_CPD" ]

[ 927, 900 ]

2

[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "...

[ "2.4.1.-", "3.4.22.-", "PWY-1901", "PWY-1961", "PWY-1981", "PWY-2021", "PWY-2881", "PWY-2901", "PWY-2902", "PWY-4421", "PWY-4801", "PWY-5094", "PWY-5105", "PWY-5129", "PWY-5139", "PWY-5160", "PWY-5161", "PWY-5268", "PWY-5284", "PWY-5286", "PWY-5310", "PWY-5312", "PWY-5313...

[ "EC:2.4.1.-", "EC:3.4.22.-", "METACYC:PWY-1901", "METACYC:PWY-1961", "METACYC:PWY-1981", "METACYC:PWY-2021", "METACYC:PWY-2881", "METACYC:PWY-2901", "METACYC:PWY-2902", "METACYC:PWY-4421", "METACYC:PWY-4801", "METACYC:PWY-5094", "METACYC:PWY-5105", "METACYC:PWY-5129", "METACYC:PWY-5139",...

201

[ "3eeb", "3fzy", "3gcd", "3ho6", "3pa8", "3pee", "4r04", "6ar6", "6en3", "6oq5", "7d5y", "7ml7", "7n8x", "7n95", "7n97", "7n9q", "7n9r", "7n9s", "7n9y", "7pog", "7v1n", "8jb5", "8jhz", "8qen", "8qeo", "8x2h", "8x2i", "8y9b", "8y9c", "8yja", "8yjc", "9bja"...

36

[ "PUB00051676", "PUB00052954", "PUB00053274", "PUB00077741" ]

[ "18845756", "19465933", "17464284", "20628577" ]

[ "Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain.", "Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin.", "Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain.", "Inositol hexakisphosp...

[ 2008, 2009, 2007, 2010 ]

4

[]

[ "IPR049824" ]

0

1

0

[ "Bacteria", "Bilateria", "hydrothermal vent metagenome" ]

[ 831, 111, 1 ]

3

[]

0

true

Domain

CGT/MARTX, cysteine protease (CPD) domain

CPD_dom

5

IPR020976

20,976

LCI fold

Antimicrobial_lci

Domain

230

false

This entry represents the LCI fold found in bacteria, functionally related to antimicrobial activity. It is approximately 40 amino acids in length and consists of three antiparallel β-strands in a β1-β3-β2 topology. This domain has been reported linked to CHAP, PGBD and SH3 domains in a putative cysteine protease [ ].

[]

0

[ "PFAM" ]

[ "PF12197" ]

[ "lci" ]

[ 230 ]

1

[]

0

[ "2b9k" ]

1

[ "PUB00099867" ]

[ "27934875" ]

[ "Functional and structural characterization of a novel putative cysteine protease cell wall-modifying multi-domain enzyme selected from a microbial metagenome." ]

[ 2016 ]

1

[]

0

null

[ "Bacteria", "Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)" ]

[ 229, 1 ]

2

[]

0

true

Domain

LCI fold

Antimicrobial_lci

4

IPR020977

20,977

Beta-casein-like

Family

2,206

false

This entry represents eukaryotic proteins that are typically between 216 to 240 amino acids in length which have two conserved sequence motifs: VLR and TRIY. Beta-casein-like protein is associated with cell morphology and a regulation of growth pattern of tumours. It is found in adenocarcinomas of uterine cervical tiss...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF12304", "PTHR31258" ]

[ "BCLP", "" ]

[ 2204, 2180 ]

2

[]

0

[]

0

[ "PUB00053273" ]

[ "11394883" ]

[ "Cloning and characterization of a tumor-associated antigen, beta-casein-like protein." ]

[ 2001 ]

1

[]

0

null

[ "Vertebrata" ]

[ 2206 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 7, 3, 7, 10 ]

4

true

Family

Beta-casein-like

7

IPR020978

20,978

Cryptochrome C-terminal

Cryptochrome_C

Domain

1,083

false

Cryptochromes are blue/ultraviolet-A light sensing photoreceptors involved in regulating various growth and developmental responses in plants [ ]. Cryptochromes are inactive monomers in the dark but change its conformation to homooligomers upon photon absoption [ ]. This entry represents the C-terminal end of Cryptochr...

[]

0

[ "PFAM" ]

[ "PF12546" ]

[ "Cryptochrome_C" ]

[ 1083 ]

1

[]

0

[ "6lz3", "9lpg" ]

2

[ "PUB00053367", "PUB00099815", "PUB00099816", "PUB00099817" ]

[ "16531484", "32169020", "17002522", "15751956" ]

[ "Cryptochrome 1 from Brassica napus is up-regulated by blue light and controls hypocotyl/stem growth and anthocyanin accumulation.", "Mechanisms of Cryptochrome-Mediated Photoresponses in Plants.", "Cryptochrome signaling in plants.", "Role of structural plasticity in signal transduction by the cryptochrome b...

[ 2006, 2020, 2007, 2005 ]

4

[]

0

null

[ "Spermatophyta" ]

[ 1083 ]

1

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 5, 10, 24 ]

3

true

Domain

Cryptochrome C-terminal

Cryptochrome_C

3

IPR020979

20,979

Uncharacterised protein family A0KLC6

Uncharacterised_A0KLC6

Family

570

false

This family of proteins is found in bacteria and are typically between 114 and 143 amino acids in length. There is a conserved KNLFD sequence motif. The annotation with this family suggests that it may be the B subunit of bacterial type IIA DNA topoisomerase but there is no evidence to support this annotation.

[]

0

[ "PFAM" ]

[ "PF12290" ]

[ "DUF3802" ]

[ 570 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "marine sediment metagenome" ]

[ 569, 1 ]

2

[]

0

true

Family

Uncharacterised protein family A0KLC6

Uncharacterised_A0KLC6

1

IPR020980

20,980

Menbrane protein HflK, N-terminal

Membrane_HflK_N

Domain

6,477

false

HflK is a bacterial membrane protein which is thought, together with the HflC protein, to form a membrane protease complex whose activity is modulated by the GTPase HflX [ ]. This entry represents the N-terminal, membrane-spanning, region of of HflK responsible for anchoring the protein in the bacterial membrane. It is...

[]

0

[ "PFAM" ]

[ "PF12221" ]

[ "HflK_N" ]

[ 6477 ]

1

[]

0

[ "7vhp", "7wi3", "9cz1", "9cz2" ]

4

[ "PUB00043068" ]

[ "8248183" ]

[ "The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain." ]

[ 1993 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 6356, 7, 114 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Menbrane protein HflK, N-terminal

Membrane_HflK_N

7

IPR020981

20,981

Monopolin complex subunit Csm1/Pcs1, C-terminal

-Csm1/Pcs1_C

Domain

1,430

false

Saccharomyces cerevisiae Csm1 is part of the monopolin complex. Csm1 forms a complex with Mde4 and promotes monoorientation during meiosis [ ]. It plays a mitotic role in DNA replication [ ] and is required for condensin recruitment to the replication fork barrier site and rDNA repeat segregation [ ]. This entry also c...

[ "GO:0005515" ]

[ "protein binding" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF12539" ]

[ "Csm1" ]

[ 1430 ]

1

[]

0

[ "3n4r", "3n4s", "3n4x", "3n7n", "5ktb", "5v1a", "5v3n", "6dei", "6mj8", "6mjb", "6mjc", "6mje" ]

12

[ "PUB00044339", "PUB00044753", "PUB00053368" ]

[ "17627824", "15023545", "19362534" ]

[ "The kinetochore proteins Pcs1 and Mde4 and heterochromatin are required to prevent merotelic orientation.", "Saccharomyces cerevisiae CSM1 gene encoding a protein influencing chromosome segregation in meiosis I interacts with elements of the DNA replication complex.", "The cis element and factors required for ...

[ 2007, 2004, 2009 ]

3

[]

0

null

[ "Eukaryota" ]

[ 1430 ]

1

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 1, 1, 1 ]

3

true

Domain

Monopolin complex subunit Csm1/Pcs1, C-terminal

-Csm1/Pcs1_C

9

IPR020982

20,982

Bacteriophage T4, GpT, holin

Phage_T4_GpT_holin

Family

537

false

One mechanism by which bacteriophages effect host lysis begins with the accumulation of a holin in the host membrane and an endolysin in the host cytoplasm during late gene expression. At an allele-specific time, the holin disrupts the membrane, thus allowing the endolysin to enter the periplasm and degrade the cell wa...

[ "GO:0044659" ]

[ "viral release from host cell by cytolysis" ]

[ "biological_process" ]

1

[ "HAMAP", "PFAM" ]

[ "MF_04104", "PF11031" ]

[ "HOLIN_T4", "Phage_holin_T" ]

[ 499, 537 ]

2

[]

0

[ "6psk", "6px4", "6pxe" ]

3

[ "PUB00053276" ]

[ "16166524" ]

[ "Periplasmic domains define holin-antiholin interactions in t4 lysis inhibition." ]

[ 2005 ]

1

[]

0

null

[ "Bacteria", "Viruses" ]

[ 3, 534 ]

2

[]

0

true

Family

Bacteriophage T4, GpT, holin

Phage_T4_GpT_holin

4

IPR020984

20,984

Speedy

Family

2,049

false

This entry represents Speedy proteins found in animals. Speedy (Spy1, also known as RINGO A) is a cell cycle regulatory protein which binds and activates CDK1 and CDK2 [ ], protein kinases that allows progression through G1/S phase and further replication events. Spy1 activates CDK2 inducing a conformational change of ...

[ "GO:0019901", "GO:0045737" ]

[ "protein kinase binding", "positive regulation of cyclin-dependent protein serine/threonine kinase activity" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF11357" ]

[ "Spy1" ]

[ 2049 ]

1

[]

0

[ "5uq1", "5uq2", "5uq3", "7e34" ]

4

[ "PUB00054157", "PUB00099648", "PUB00099649" ]

[ "17671428", "28666995", "12972555" ]

[ "Spy1 enhances phosphorylation and degradation of the cell cycle inhibitor p27.", "Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins.", "Spy1 interacts with p27Kip1 to allow G1/S progression." ]

[ 2007, 2017, 2003 ]

3

[]

[ "IPR057742" ]

0

1

0

[ "Eukaryota" ]

[ 2049 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 36, 9, 10 ]

4

true

Family

Speedy

6

IPR020987

20,987

Centromere protein Cenp-M

Centromere_Cenp-M

Family

1,295

false

The prime candidate for specifying centromere identity is the array of nucleosomes assembles associated with CENP-A [ ]. CENP-A recruits a nucleosome associated complex (CENP-A-NAC complex) comprised of CENP-M which this entry represents, along with two other proteins [ ]. Assembly of the CENP-A NAC at centromeres is p...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF11111", "PTHR34436" ]

[ "CENP-M", "" ]

[ 1295, 1199 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-141444", "R-BTA-2467813", "R-BTA-2500257", "R-BTA-5663220", "R-BTA-606279", "R-BTA-68877", "R-BTA-9648025", "R-GGA-141444", "R-GGA-2467813", "R-GGA-2500257", "R-GGA-5663220", "R-GGA-606279", "R-GGA-9648025", "R-HSA-141444", "R-HSA-2467813", "R-HSA-2500257", "R-HSA-5663220", ...

[ "REACTOME:R-BTA-141444", "REACTOME:R-BTA-2467813", "REACTOME:R-BTA-2500257", "REACTOME:R-BTA-5663220", "REACTOME:R-BTA-606279", "REACTOME:R-BTA-68877", "REACTOME:R-BTA-9648025", "REACTOME:R-GGA-141444", "REACTOME:R-GGA-2467813", "REACTOME:R-GGA-2500257", "REACTOME:R-GGA-5663220", "REACTOME:R-G...

27

[ "4p0t", "4wau", "7pkn", "7qoo", "7r5s", "7r5v", "7xhn", "7xho", "7ywx", "7yyh" ]

10

[ "PUB00044194" ]

[ "16622419" ]

[ "The human CENP-A centromeric nucleosome-associated complex." ]

[ 2006 ]

1

[]

0

null

[ "Eukaryota" ]

[ 1295 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 5, 3, 5 ]

4

true

Family

Centromere protein Cenp-M

Centromere_Cenp-M

5

IPR020988

20,988

Peptidase U32, collagenase

Pept_U32_collagenase

Domain

7,310

false

The peptidases families associated with clan U-have an unknown catalytic mechanism as the protein fold of the active site domain and the active site residues have not been reported. This domain is found in a number of proteins belonging to the MEROPS peptidase family U32. Peptidase family U32 contains endopeptidases, i...

[]

0

[ "PFAM" ]

[ "PF12392" ]

[ "DUF3656" ]

[ 7310 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ctrMq22", "metagenomes" ]

[ 251, 6906, 85, 1, 67 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Peptidase U32, collagenase

Pept_U32_collagenase

6

IPR020990

20,990

Carboxysome assembly protein CsoS2/2B

CSOS2/2B

Family

241

false

This family represents carboxysome assembly proteins, including CsoS2 and S2B (also known as carboxysome shell proteins), which are alpha-carboxysome scaffold proteins required for alpha-carboxysome (Cb) assembly. They mediate interaction between RuBisCO and shell proteins to organize and assemble Cb [ , , ]. The N-ter...

[ "GO:0043886" ]

[ "structural constituent of carboxysome shell" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF12288" ]

[ "CsoS2_M" ]

[ 241 ]

1

[]

0

[ "8b12", "8wxb", "8yvc", "8yvd", "8yve", "8yvf", "8yvi", "9f0h" ]

8

[ "PUB00096685", "PUB00096686", "PUB00096687" ]

[ "25826651", "32123388", "26608811" ]

[ "Advances in Understanding Carboxysome Assembly in Prochlorococcus and Synechococcus Implicate CsoS2 as a Critical Component.", "Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation.", "Programmed Ribosomal Frameshifting Mediates Expression of the α-Carboxysome." ]

[ 2015, 2020, 2016 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 217, 13, 11 ]

3

[]

0

true

Family

Carboxysome assembly protein CsoS2/2B

CSOS2/2B

3

IPR020991

20,991

Head-to-tail connector protein, podovirus-type

Connector_podovirus

Family

2,592

false

The tail of bacteriophage T7, a member of the Podoviridae family, is composed of at least four proteins; one of them is gene product 8 (gp8), known as the connector [ ]. DNA enters the viral head during DNA packaging through a channel formed by the connector. The connector sits at a unique 5-fold vertex of the icosahed...

[]

0

[ "PFAM" ]

[ "PF12236" ]

[ "Head-tail_con" ]

[ 2592 ]

1

[]

0

[ "3j4a", "6qwp", "6qx5", "6qxm", "6r21", "6tjp", "7bou", "7bp0", "7ey6", "7ey8", "7y1c", "7y22", "8ck0", "8dgf", "8e4g", "8es4", "8i4m", "8vb4", "9efk", "9jyz", "9jz0", "9v30" ]

22

[ "PUB00081256", "PUB00082265", "PUB00082266" ]

[ "23884409", "22186221", "15784250" ]

[ "Structural characterization of the bacteriophage T7 tail machinery.", "Viral connectors for DNA encapsulation.", "Structure of the connector of bacteriophage T7 at 8A resolution: structural homologies of a basic component of a DNA translocating machinery." ]

[ 2013, 2012, 2005 ]

3

[]

[ "IPR038995" ]

0

1

0

[ "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 1172, 13, 1219, 188 ]

4

[]

0

true

Family

Head-to-tail connector protein, podovirus-type

Connector_podovirus

9

IPR020992

20,992

Tail specific protease, C-terminal

Tail_Prtase_C

Domain

7,670

false

This entry represents the C-terminal domain of tail-specific protease Prc, involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3) [ ]. This protease belongs to MEROPS serine peptidase family S41A (C-terminal processing peptidase-1, clan SK). This d...

[]

0

[ "PFAM" ]

[ "PF11818" ]

[ "DUF3340" ]

[ 7670 ]

1

[ "EC" ]

[ "3.4.21.102" ]

[ "EC:3.4.21.102" ]

1

[ "5wql", "6iqq", "6iqr", "6iqs", "6iqu", "8xud" ]

6

[ "PUB00057845" ]

[ "1856173" ]

[ "Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3." ]

[ 1991 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 7575, 18, 77 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Tail specific protease, C-terminal

Tail_Prtase_C

4

IPR020993

20,993

Centromere protein Cenp-K

Centromere_CenpK

Family

2,087

false

Cenp-K is one of seven new Cenp-A-nucleosome distal (CAD) centromere components (the others being Cenp-L, Cenp-O, Cenp-P, Cenp-Q, Cenp-R and Cenp-S) that are identified as assembling on the Cenp-A nucleosome associated complex, NAC [ ]. The Cenp-A NAC is essential, as disruption of the complex causes errors of chromoso...

[ "GO:0051382", "GO:0005634" ]

[ "kinetochore assembly", "nucleus" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "PANTHER" ]

[ "PF11802", "PTHR14401" ]

[ "CENP-K", "" ]

[ 1254, 2057 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-141444", "R-HSA-2467813", "R-HSA-2500257", "R-HSA-5663220", "R-HSA-606279", "R-HSA-68877", "R-HSA-9648025", "R-MMU-141444", "R-MMU-2467813", "R-MMU-2500257", "R-MMU-5663220", "R-MMU-606279", "R-MMU-68877", "R-MMU-9648025" ]

[ "REACTOME:R-HSA-141444", "REACTOME:R-HSA-2467813", "REACTOME:R-HSA-2500257", "REACTOME:R-HSA-5663220", "REACTOME:R-HSA-606279", "REACTOME:R-HSA-68877", "REACTOME:R-HSA-9648025", "REACTOME:R-MMU-141444", "REACTOME:R-MMU-2467813", "REACTOME:R-MMU-2500257", "REACTOME:R-MMU-5663220", "REACTOME:R-M...

14

[ "5z08", "7pb4", "7pkn", "7qoo", "7r5s", "7r5v", "7xhn", "7xho", "7ywx", "7yyh" ]

10

[ "PUB00044194", "PUB00044862", "PUB00086852", "PUB00088168" ]

[ "16622419", "18007590", "18045986", "12719471" ]

[ "The human CENP-A centromeric nucleosome-associated complex.", "The CENP-A NAC/CAD kinetochore complex controls chromosome congression and spindle bipolarity.", "KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly in vertebrates.", "Sim4: a novel fission yeast kinetochore protein required...

[ 2006, 2007, 2008, 2003 ]

4

[]

0

null

[ "Eukaryota", "Streptomyces" ]

[ 2085, 2 ]

2

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 5, 7, 4, 1, 6, 1 ]

6

true

Family

Centromere protein Cenp-K

Centromere_CenpK

5

IPR020994

20,994

Uncharacterised protein family, calcium binding protein, CcbP

Uncharacterised_Ca-bd_CcbP

Family

461

false

CcbP is a Ca(2+) binding protein found in bacteria which is thought to bind Ca(2+) by protein surface charge. When bound to Ca(2+), the protein becomes more compact and the level of free calcium decreases. Within the bacteria, Ca(2+) has a role in the early stages of heterocyst differentiation. The free Ca(2+) concentr...

[]

0

[ "PFAM" ]

[ "PF11535" ]

[ "Calci_bind_CcbP" ]

[ 461 ]

1

[]

0

[ "2k2v", "2p0p", "2p0q", "3urg" ]

4

[ "PUB00053280", "PUB00055576" ]

[ "15811937", "15469503" ]

[ "CcbP, a calcium-binding protein from Anabaena sp. PCC 7120, provides evidence that calcium ions regulate heterocyst differentiation.", "Calcium signalling in bacteria." ]

[ 2005, 2004 ]

2

[]

0

null

[ "Bacteria", "Methanobacteriota", "ecological metagenomes" ]

[ 380, 75, 6 ]

3

[]

0

true

Family

Uncharacterised protein family, calcium binding protein, CcbP

Uncharacterised_Ca-bd_CcbP

2

IPR020995

20,995

Chlorosome envelope protein C

Chlorosome_envelope_CsmC

Family

31

false

Chlorosomes are light-harvesting antennae found in green bacteria. This entry represents Chlorosome envelope protein C (CsmC) which is one of the proteins that exists in the chlorosome envelope and has been shown to exist as a homomultimer with CsmD in the chlorosome envelope [ ]. CsmC is thought to be important in chl...

[]

0

[ "PFAM" ]

[ "PF11098" ]

[ "Chlorosome_CsmC" ]

[ 31 ]

1

[]

0

[]

0

[ "PUB00053279" ]

[ "16866355" ]

[ "Molecular contacts for chlorosome envelope proteins revealed by cross-linking studies with chlorosomes from Chlorobium tepidum." ]

[ 2006 ]

1

[]

0

null

[ "Bacteria" ]

[ 31 ]

1

[]

0

true

Family

Chlorosome envelope protein C

Chlorosome_envelope_CsmC

3

IPR020996

20,996

Type III secretion system, AvrPto

T3SS_AvrPto

Family

45

false

This entry represents the bacterial effector protein AvrPto, from Pseudomonas syringae and in particular the central core region of the protein that consists of a three-helix bundle motif. AvrPto is part of a type III secretion system from P.syringae which is involved in the bacterial speck disease of tomato. In resist...

[]

0

[ "PFAM" ]

[ "PF11592" ]

[ "AvrPto" ]

[ 45 ]

1

[]

0

[ "1r5e", "2qkw" ]

2

[ "PUB00030532" ]

[ "15242602" ]

[ "The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis." ]

[ 2004 ]

1

[]

0

null

[ "Pseudomonadota" ]

[ 45 ]

1

[]

0

true

Family

Type III secretion system, AvrPto

T3SS_AvrPto

3

IPR020997

20,997

Ataxin-1, N-terminal

Ataxin-1_N

Domain

1,772

false

This entry represents the N-terminal domain of Ataxin-1, which directly binds Capicua and modulates Capicua repressor activity in Drosophila and mammalian cells. It is also thought to be involved in RNA metabolism and the expansion of the polyglutamine tract may alter this function. Ataxin-1 is typically between 49 and...

[]

0

[ "PFAM" ]

[ "PF12547" ]

[ "ATXN-1_C" ]

[ 1772 ]

1

[]

0

[]

0

[ "PUB00053281" ]

[ "17190598" ]

[ "ATAXIN-1 interacts with the repressor Capicua in its native complex to cause SCA1 neuropathology." ]

[ 2006 ]

1

[]

0

null

[ "Eukaryota" ]

[ 1772 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 10, 3, 4, 7 ]

4

true

Domain

Ataxin-1, N-terminal

Ataxin-1_N

8

IPR020998

20,998

Mediator of RNA polymerase II transcription subunit 3

Med3

Family

66

false

Med3 is a subunit of the RNA polymerase II mediator complex. It is a direct target of Cyc8-Tup1 transcriptional corepressor [ ]. The Mediator complex is a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-s...

[ "GO:0003712", "GO:0006357", "GO:0016592" ]

[ "transcription coregulator activity", "regulation of transcription by RNA polymerase II", "mediator complex" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PFAM" ]

[ "PF11593" ]

[ "Med3" ]

[ 66 ]

1

[]

0

[ "7uic", "7uik", "7uil", "7uio" ]

4

[ "PUB00053372" ]

[ "10722672" ]

[ "Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II holoenzyme." ]

[ 2000 ]

1

[]

0

null

[ "saccharomyceta" ]

[ 66 ]

1

[ "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 1 ]

1

true

Family

Mediator of RNA polymerase II transcription subunit 3

Med3

2

IPR020999

20,999

RCR1/2

Family

2,005

false

RCR proteins are ER membrane proteins that regulate chitin deposition in fungal cell walls. Although chitin, a linear polymer of beta-1,4-linked N-acetylglucosamine, constitutes only 2% of the cell wall it plays a vital role in the overall protection of the cell wall against stress, noxious chemicals and osmotic pressu...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF12273", "PTHR28187" ]

[ "RCR", "" ]

[ 1974, 1282 ]

2

[]

0

[]

0

[ "PUB00043144", "PUB00053282", "PUB00163383" ]

[ "17213653", "15590673", "32421152" ]

[ "Peculiar protein-protein interactions of the novel endoplasmic reticulum membrane protein Rcr1 and ubiquitin ligase Rsp5.", "A novel endoplasmic reticulum membrane protein Rcr1 regulates chitin deposition in the cell wall of Saccharomyces cerevisiae.", "Calcineurin-dependent regulation of endocytosis by a plas...

[ 2007, 2005, 2020 ]

3

[]

0

null

[ "Eukaryota" ]

[ 2005 ]

1

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 2, 2, 1 ]

3

true

Family

RCR1/2

4

IPR021001

21,001

Spidroin, C-terminal

Spidroin_C

Domain

544

false

Spidroin is spider dragline silk. It is composed of two proteins, major ampullate spidroin 1 (MaSp1) and major ampullate spidroin 2 (MaSp2) [ ]. MaSp1 contains five α-helices [ ]. Spidroins contain repetitive units capped between non-repetitive N-terminal and C-terminal domains, whose composition varies among species a...

[]

0

[ "PFAM" ]

[ "PF11260" ]

[ "Spidroin_MaSp" ]

[ 544 ]

1

[]

0

[ "2k3p", "2khm", "2m0m", "2mab", "2mfz" ]

5

[ "PUB00053364", "PUB00053365", "PUB00097404" ]

[ "16283740", "17096540", "23418525" ]

[ "Analysis of the conserved N-terminal domains in major ampullate spider silk proteins.", "N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins.", "Structural characterization of minor ampullate spidroin domains and their distinct roles in fibroin solubility and...

[ 2005, 2006, 2013 ]

3

[]

0

null

[ "Araneae" ]

[ 544 ]

1

[]

0

true

Domain

Spidroin, C-terminal

Spidroin_C

4

IPR021002

21,002

Replication protein 1a, necrotic phentoype-determining domain

1a_necrotic_phenotyp-det_dom

Domain

372

false

Replication protein 1a is a core component of the viral replicase complex in Cucumber mosaic virus and related plant viruses. 1a protein is the major virulence factor of the cucumber mosaic virus (CMV). The Ns strain of CMV causes necrotic lesions to Nicotiana spp. while other strains cause systemic mosaic [ ].

[ "GO:0008168", "GO:0016817" ]

[ "methyltransferase activity", "hydrolase activity, acting on acid anhydrides" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF12467" ]

[ "CMV_1a" ]

[ 372 ]

1

[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "...

[ "2.1.1.-", "3.6.4.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601",...

[ "EC:2.1.1.-", "EC:3.6.4.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", ...

148

[]

0

[ "PUB00053357" ]

[ "15305604" ]

[ "The necrotic pathotype of the cucumber mosaic virus (CMV) ns strain is solely determined by amino acid 461 of the 1a protein." ]

[ 2004 ]

1

[]

0

null

[ "Glycine max", "Riboviria" ]

[ 1, 371 ]

2

[]

0

true

Domain

Replication protein 1a, necrotic phentoype-determining domain

1a_necrotic_phenotyp-det_dom

7

IPR021003

21,003

Cytomegalovirus glycoprotein N, N-terminal

Cytomegalovirus_glycopN_N

Domain

238

false

This domain family is found in viruses, and is approximately 30 amino acids in length. The signature is found in association with . This family is an envelope glycoprotein of (Human herpesvirus 5) [ ].

[]

0

[ "PFAM" ]

[ "PF12522" ]

[ "UL73_N" ]

[ 238 ]

1

[ "REACTOME", "REACTOME" ]

[ "R-HSA-9609690", "R-HSA-9610379" ]

[ "REACTOME:R-HSA-9609690", "REACTOME:R-HSA-9610379" ]

2

[]

0

[ "PUB00053393" ]

[ "11090188" ]

[ "Complex formation by human cytomegalovirus glycoproteins M (gpUL100) and N (gpUL73)." ]

[ 2000 ]

1

[]

0

null

[ "Cytomegalovirus", "Micromonospora fiedleri" ]

[ 237, 1 ]

2

[]

0

true

Domain

Cytomegalovirus glycoprotein N, N-terminal

Cytomegalovirus_glycopN_N

4

IPR021004

21,004

Dispersed gene family protein 1, domain 4

Dispersed_gene_fam_prot1_dom4

Domain

774

false

Dispersed gene family protein 1 of Trypanosoma cruzi is likely to be highly expressed, and is expressed from the sub-telomeric region [ ]. However, its function is not known. This entry represents domain 4 on this protein which is likely disordered.

[]

0

[ "PFAM" ]

[ "PF11024" ]

[ "DGF-1_4" ]

[ 774 ]

1

[]

0

[]

0

[ "PUB00054242" ]

[ "18037385" ]

[ "Comparative codon and amino acid composition analysis of Tritryps-conspicuous features of Leishmania major." ]

[ 2007 ]

1

[]

0

null

[ "Trypanosoma" ]

[ 774 ]

1

[]

0

true

Domain

Dispersed gene family protein 1, domain 4

Dispersed_gene_fam_prot1_dom4

9

IPR021006

21,006

HDA1 complex subunit 2/3

Hda2/3

Family

990

false

This entry contains the class II histone deacetylase complex subunits Hda2 and Hda3 from fungi.

[ "GO:0070823" ]

[ "HDA1 complex" ]

[ "cellular_component" ]

1

[ "PFAM" ]

[ "PF11496" ]

[ "HDA2-3" ]

[ 990 ]

1

[]

0

[ "3hgq", "3hgt", "6z6f", "6z6h", "6z6o", "6z6p" ]

6

[ "PUB00053285" ]

[ "11287668" ]

[ "HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1." ]

[ 2001 ]

1

[]

[ "IPR026216" ]

0

1

0

[ "Eukaryota" ]

[ 990 ]

1

[ "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 2 ]

1

true

Family

HDA1 complex subunit 2/3

Hda2/3

5

IPR021007

21,007

Complementary sex determiner, C-terminal

Sex_determ_C

Domain

976

false

This entry represents the C-terminal end of the sex determination protein. Sex determination proteins are found in eukaryotes. Proteins in this family are typically between 168 and 410 amino acids in length. It plays a role in the gender determination of around 20% of all animals. In the honeybee, the mechanism of sex ...

[]

0

[ "PFAM" ]

[ "PF11671" ]

[ "Apis_Csd" ]

[ 976 ]

1

[]

0

[]

0

[ "PUB00053286", "PUB00160302" ]

[ "15382141", "21110346" ]

[ "The dice of fate: the csd gene and how its allelic composition regulates sexual development in the honey bee, Apis mellifera.", "Function and evolution of sex determination mechanisms, genes and pathways in insects." ]

[ 2004, 2011 ]

2

[]

0

null

[ "Apocrita" ]

[ 976 ]

1

[]

0

true

Domain

Complementary sex determiner, C-terminal

Sex_determ_C

5

IPR021008

21,008

D-Ala-teichoic acid biosynthesis protein DltX

DltX

Family

1,151

false

This entry represents a family of DltX proteins of approximately 50 amino acids in length predominantly found in bacillota, including from Bacillus thuringiensis. Members of this group are small, single-pass transmembrane proteins required for the D-alanylation of teichoic acids. DltX binds to the MBOAT protein DltB ( ...

[]

0

[ "PFAM" ]

[ "PF12459" ]

[ "DltX" ]

[ 1151 ]

1

[]

0

[]

0

[ "PUB00153778", "PUB00153779" ]

[ "28824570", "37308592" ]

[ "DltX of <i>Bacillus thuringiensis</i> Is Essential for D-Alanylation of Teichoic Acids and Resistance to Antimicrobial Response in Insects.", "Mechanism of D-alanine transfer to teichoic acids shows how bacteria acylate cell envelope polymers." ]

[ 2017, 2023 ]

2

[]

0

null

[ "Bacteria", "bioreactor metagenome" ]

[ 1150, 1 ]

2

[]

0

true

Family

D-Ala-teichoic acid biosynthesis protein DltX

DltX

2

IPR021009

21,009

Motility repressor MogR, DNA-binding domain

MogR_DNA-bd

Domain

256

false

This domain family is found in bacteria, and is approximately 150 amino acids in length. MogR is involved in the transcriptional repressor of flagellar motility genes, such as flaA, during extracellular growth at 37 degrees Celsius and during intracellular infection. It binds directly to gene promoter region and probab...

[]

0

[ "PFAM" ]

[ "PF12181" ]

[ "MogR_DNAbind" ]

[ 256 ]

1

[]

0

[ "3fdq", "7x9s" ]

2

[ "PUB00051944", "PUB00053287" ]

[ "19446532", "16617375" ]

[ "Recognition of AT-rich DNA binding sites by the MogR repressor.", "The MogR transcriptional repressor regulates nonhierarchal expression of flagellar motility genes and virulence in Listeria monocytogenes." ]

[ 2009, 2006 ]

2

[]

0

null

[ "Bacteria" ]

[ 256 ]

1

[]

0

true

Domain

Motility repressor MogR, DNA-binding domain

MogR_DNA-bd

7

IPR021010

21,010

Cytosolic motility protein

Cytosolic_motility_protein

Family

799

false

This entry represents proteins found in nematodes. They complex with MSP (major sperm protein) to allow motility [ ]. Their action is quite similar to the action of bacterial actin molecules.

[]

0

[ "PFAM", "PANTHER" ]

[ "PF12150", "PTHR31578" ]

[ "MFP2b", "" ]

[ 795, 699 ]

2

[]

0

[ "2bjq", "2bjr" ]

2

[ "PUB00032774" ]

[ "15755452" ]

[ "Structure of MFP2 and its function in enhancing MSP polymerization in Ascaris sperm amoeboid motility." ]

[ 2005 ]

1

[]

0

null

[ "Chromadorea" ]

[ 799 ]

1

[ "Caenorhabditis elegans" ]

[ 12 ]

1

true

Family

Cytosolic motility protein

Cytosolic_motility_protein

4