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UniProtKB - Q00578 (RAD25_YEAST)

Entry version 195 (07 Apr 2021)
Sequence version 1 (01 Apr 1993)
Previous versions | rss
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Protein

General transcription and DNA repair factor IIH helicase subunit XPB

Gene

SSL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/SSL2, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/SSL2 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription (PubMed:8269516, PubMed:7693549, PubMed:7961739, PubMed:8202161, PubMed:7813015, PubMed:8631896). XPB/SSL2 acts as a double-stranded DNA translocase promoting DNA opening by tracking along the nontemplate promoter strand, rotating and inserting DNA into the Pol II active site cleft, leading to DNA unwinding. May also use this translocase mechanism during DNA repair rather than physically wedging open damaged DNA (PubMed:25775526).7 Publications

Miscellaneous

A C-terminal deletion renders yeast hypersensitive to UV light.
Present with 825 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi386 – 393ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA repair, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-113418, Formation of the Early Elongation Complex
R-SCE-674695, RNA Polymerase II Pre-transcription Events
R-SCE-6781823, Formation of TC-NER Pre-Incision Complex
R-SCE-6782135, Dual incision in TC-NER
R-SCE-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-6796648, TP53 Regulates Transcription of DNA Repair Genes
R-SCE-72086, mRNA Capping
R-SCE-73772, RNA Polymerase I Promoter Escape
R-SCE-73776, RNA Polymerase II Promoter Escape
R-SCE-73779, RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-SCE-75953, RNA Polymerase II Transcription Initiation
R-SCE-75955, RNA Polymerase II Transcription Elongation
R-SCE-76042, RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-77075, RNA Pol II CTD phosphorylation and interaction with CE

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
General transcription and DNA repair factor IIH helicase subunit XPB (EC:3.6.4.12)
Short name:
TFIIH subunit XPB
Alternative name(s):
DNA repair helicase RAD25
RNA polymerase II transcription factor B subunit SSL2
Short name:
TFB subunit SSL2
Suppressor of stem-loop mutation 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SSL2
Synonyms:LOM3, RAD25, UVS112
Ordered Locus Names:YIL143C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IX

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000001405, SSL2

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YIL143C

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001019941 – 843General transcription and DNA repair factor IIH helicase subunit XPBAdd BLAST843

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei752PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q00578

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q00578

PRoteomics IDEntifications database

More...PRIDEi		Q00578

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q00578

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q00578

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription.

3 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34849, 128 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1659, General transcription factor complex TFIIH

Database of interacting proteins

More...DIPi		DIP-731N

Protein interaction database and analysis system

More...IntActi		Q00578, 23 interactors

Molecular INTeraction database

More...MINTi		Q00578

STRING: functional protein association networks

More...STRINGi		4932.YIL143C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q00578, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q00578

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini373 – 535Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST163
Domaini589 – 743Helicase C-terminalPROSITE-ProRule annotationAdd BLAST155

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi64 – 75Nuclear localization signalSequence analysisAdd BLAST12
Motifi487 – 491DEVH box5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi302 – 309Asp/Glu-rich (acidic)8

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the helicase family. RAD25/XPB subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1123, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000002204

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_008213_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q00578

Identification of Orthologs from Complete Genome Data

More...OMAi		SQEWGLM

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR032438, ERCC3_RAD25_C
IPR006935, Helicase/UvrB_N
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR001161, XPB/Ssl2
IPR032830, XPB/Ssl2_N

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16203, ERCC3_RAD25_C, 1 hit
PF13625, Helicase_C_3, 1 hit
PF04851, ResIII, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00603, rad25, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q00578-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTDVEGYQPK SKGKIFPDMG ESFFSSDEDS PATDAEIDEN YDDNRETSEG 
        60         70         80         90        100
RGERDTGAMV TGLKKPRKKT KSSRHTAADS SMNQMDAKDK ALLQDTNSDI 
       110        120        130        140        150
PADFVPDSVS GMFRSHDFSY LRLRPDHASR PLWISPSDGR IILESFSPLA 
       160        170        180        190        200
EQAQDFLVTI AEPISRPSHI HEYKITAYSL YAAVSVGLET DDIISVLDRL 
       210        220        230        240        250
SKVPVAESII NFIKGATISY GKVKLVIKHN RYFVETTQAD ILQMLLNDSV 
       260        270        280        290        300
IGPLRIDSDH QVQPPEDVLQ QQLQQTAGKP ATNVNPNDVE AVFSAVIGGD 
       310        320        330        340        350
NEREEEDDDI DAVHSFEIAN ESVEVVKKRC QEIDYPVLEE YDFRNDHRNP 
       360        370        380        390        400
DLDIDLKPST QIRPYQEKSL SKMFGNGRAR SGIIVLPCGA GKTLVGITAA 
       410        420        430        440        450
CTIKKSVIVL CTSSVSVMQW RQQFLQWCTL QPENCAVFTS DNKEMFQTES 
       460        470        480        490        500
GLVVSTYSMV ANTRNRSHDS QKVMDFLTGR EWGFIILDEV HVVPAAMFRR 
       510        520        530        540        550
VVSTIAAHAK LGLTATLVRE DDKIGDLNFL IGPKLYEANW MELSQKGHIA 
       560        570        580        590        600
NVQCAEVWCP MTAEFYQEYL RETARKRMLL YIMNPTKFQA CQFLIQYHER 
       610        620        630        640        650
RGDKIIVFSD NVYALQEYAL KMGKPFIYGS TPQQERMNIL QNFQYNDQIN 
       660        670        680        690        700
TIFLSKVGDT SIDLPEATCL IQISSHYGSR RQEAQRLGRI LRAKRRNDEG 
       710        720        730        740        750
FNAFFYSLVS KDTQEMYYST KRQAFLVDQG YAFKVITHLH GMENIPNLAY 
       760        770        780        790        800
ASPRERRELL QEVLLKNEEA AGIEVGDDAD NSVGRGSNGH KRFKSKAVRG 
       810        820        830        840 
EGSLSGLAGG EDMAYMEYST NKNKELKEHH PLIRKMYYKN LKK
Length:843
Mass (Da):95,341
Last modified:April 1, 1993 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFA4013E8156FE1C5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti9P → S in AAA34942 (PubMed:1333609).Curated1
Sequence conflicti48S → L in AAA34942 (PubMed:1333609).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti427W → L in suppressor mutant. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Z38059 Genomic DNA Translation: CAA86135.1
M94176 Genomic DNA Translation: AAA35102.1
L01414 Genomic DNA Translation: AAA34942.1
AY692883 Genomic DNA Translation: AAT92902.1
BK006942 Genomic DNA Translation: DAA08410.1

Protein sequence database of the Protein Information Resource

More...PIRi		S31272

NCBI Reference Sequences

More...RefSeqi		NP_012123.1, NM_001179491.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YIL143C_mRNA; YIL143C; YIL143C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854663

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YIL143C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38059 Genomic DNA Translation: CAA86135.1
M94176 Genomic DNA Translation: AAA35102.1
L01414 Genomic DNA Translation: AAA34942.1
AY692883 Genomic DNA Translation: AAT92902.1
BK006942 Genomic DNA Translation: DAA08410.1
PIRiS31272
RefSeqiNP_012123.1, NM_001179491.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FMFelectron microscopy6.001294-785[»]
5OQJelectron microscopy4.7071-843[»]
5OQMelectron microscopy5.8071-843[»]
5SVAelectron microscopy15.30Z1-843[»]
6GYMelectron microscopy6.7071-843[»]
SMRiQ00578
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34849, 128 interactors
ComplexPortaliCPX-1659, General transcription factor complex TFIIH
DIPiDIP-731N
IntActiQ00578, 23 interactors
MINTiQ00578
STRINGi4932.YIL143C

PTM databases

iPTMnetiQ00578

Proteomic databases

MaxQBiQ00578
PaxDbiQ00578
PRIDEiQ00578
TopDownProteomicsiQ00578

Genome annotation databases

EnsemblFungiiYIL143C_mRNA; YIL143C; YIL143C
GeneIDi854663
KEGGisce:YIL143C

Organism-specific databases

SGDiS000001405, SSL2
VEuPathDBiFungiDB:YIL143C

Phylogenomic databases

eggNOGiKOG1123, Eukaryota
GeneTreeiENSGT00390000002204
HOGENOMiCLU_008213_0_0_1
InParanoidiQ00578
OMAiSQEWGLM

Enzyme and pathway databases

ReactomeiR-SCE-113418, Formation of the Early Elongation Complex
R-SCE-674695, RNA Polymerase II Pre-transcription Events
R-SCE-6781823, Formation of TC-NER Pre-Incision Complex
R-SCE-6782135, Dual incision in TC-NER
R-SCE-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-6796648, TP53 Regulates Transcription of DNA Repair Genes
R-SCE-72086, mRNA Capping
R-SCE-73772, RNA Polymerase I Promoter Escape
R-SCE-73776, RNA Polymerase II Promoter Escape
R-SCE-73779, RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-SCE-75953, RNA Polymerase II Transcription Initiation
R-SCE-75955, RNA Polymerase II Transcription Elongation
R-SCE-76042, RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-77075, RNA Pol II CTD phosphorylation and interaction with CE

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q00578
RNActiQ00578, protein

Family and domain databases

InterProiView protein in InterPro
IPR032438, ERCC3_RAD25_C
IPR006935, Helicase/UvrB_N
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR001161, XPB/Ssl2
IPR032830, XPB/Ssl2_N
PfamiView protein in Pfam
PF16203, ERCC3_RAD25_C, 1 hit
PF13625, Helicase_C_3, 1 hit
PF04851, ResIII, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 2 hits
TIGRFAMsiTIGR00603, rad25, 1 hit
PROSITEiView protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRAD25_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q00578
Secondary accession number(s): D6VVE4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 7, 2021
This is version 195 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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