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Entry version 188 (13 Feb 2019)
Sequence version 2 (01 Oct 1994)
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Protein

Urea amidolyase

Gene

DUR1,2

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

Hydrolysis of urea to ammonia and CO2.

Miscellaneous

Present with 952 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

biotin

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: urea degradation

This protein is involved in step 1 and 2 of the subpathway that synthesizes CO(2) and NH(3) from urea (allophanate route).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Urea amidolyase (DUR1,2)
  2. Urea amidolyase (DUR1,2)
This subpathway is part of the pathway urea degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from urea (allophanate route), the pathway urea degradation and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei747ATPBy similarity1
Binding sitei830ATPBy similarity1
Binding sitei865ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi122 – 129ATPPROSITE-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

  • allophanate hydrolase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: InterPro
  • urea carboxylase activity Source: SGD

GO - Biological processi

  • allantoin catabolic process Source: SGD
  • arginine metabolic process Source: UniProtKB-KW
  • urea catabolic process Source: SGD

<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 functionHydrolase, Ligase, Multifunctional enzyme
Biological processArginine metabolism
LigandATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YBR208C-MONOMER
YEAST:YBR208C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.4.6 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-8951664 Neddylation

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00258;UER00371

UPA00258;UER00372

<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_and_taxonomy_section">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:
Urea amidolyase
Including the following 2 domains:
Urea carboxylase (EC:6.3.4.6)
Allophanate hydrolase (EC:3.5.1.54)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:DUR1,2
Ordered Locus Names:YBR208C
ORF Names:YBR1448
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 II

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YBR208C

Saccharomyces Genome Database

More...
SGDi
S000000412 DUR1,2

<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

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001468321 – 1835Urea amidolyaseAdd BLAST1835

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 residuei803PhosphoserineCombined sources1
Modified residuei1798N6-biotinyllysinePROSITE-ProRule annotationBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32528

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

More...
PaxDbi
P32528

PRoteomics IDEntifications database

More...
PRIDEi
P32528

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32528

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By allophanate or its non-metabolized analog oxalurate. Repressed in the presence of readily used nitrogen sources.

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
32904, 39 interactors

Database of interacting proteins

More...
DIPi
DIP-6296N

Protein interaction database and analysis system

More...
IntActi
P32528, 9 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YBR208C

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P32528

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

More...
SMRi
P32528

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_and_domains_section">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>Domaini632 – 1075Biotin carboxylationAdd BLAST444
Domaini751 – 948ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini1754 – 1832Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST79

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000251581

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32528

KEGG Orthology (KO)

More...
KOi
K14541

Identification of Orthologs from Complete Genome Data

More...
OMAi
HYNSNRL

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.100.10, 2 hits
3.90.1300.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014085 Allophanate_hydrolase
IPR023631 Amidase_dom
IPR036928 AS_sf
IPR011761 ATP-grasp
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR003778 CT_A_B
IPR003833 CT_C_D
IPR029000 Cyclophilin-like_dom_sf
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
IPR014084 Urea_COase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01425 Amidase, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02786 CPSase_L_D2, 1 hit
PF02626 CT_A_B, 1 hit
PF02682 CT_C_D, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00796 AHS1, 1 hit
SM00797 AHS2, 1 hit
SM00878 Biotin_carb_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50891 SSF50891, 2 hits
SSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52440 SSF52440, 1 hit
SSF75304 SSF75304, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02713 allophanate_hyd, 1 hit
TIGR00724 urea_amlyse_rel, 1 hit
TIGR02712 urea_carbox, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P32528-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTVSSDTTAE ISLGWSIQDW IDFHKSSSSQ ASLRLLESLL DSQNVAPVDN
60 70 80 90 100
AWISLISKEN LLHQFQILKS RENKETLPLY GVPIAVKDNI DVRGLPTTAA
110 120 130 140 150
CPSFAYEPSK DSKVVELLRN AGAIIVGKTN LDQFATGLVG TRSPYGKTPC
160 170 180 190 200
AFSKEHVSGG SSAGSASVVA RGIVPIALGT DTAGSGRVPA ALNNLIGLKP
210 220 230 240 250
TKGVFSCQGV VPACKSLDCV SIFALNLSDA ERCFRIMCQP DPDNDEYSRP
260 270 280 290 300
YVSNPLKKFS SNVTIAIPKN IPWYGETKNP VLFSNAVENL SRTGANVIEI
310 320 330 340 350
DFEPLLELAR CLYEGTWVAE RYQAIQSFLD SKPPKESLDP TVISIIEGAK
360 370 380 390 400
KYSAVDCFSF EYKRQGILQK VRRLLESVDV LCVPTCPLNP TMQQVADEPV
410 420 430 440 450
LVNSRQGTWT NFVNLADLAA LAVPAGFRDD GLPNGITLIG KKFTDYALLE
460 470 480 490 500
LANRYFQNIF PNGSRTYGTF TSSSVKPAND QLVGPDYDPS TSIKLAVVGA
510 520 530 540 550
HLKGLPLHWQ LEKVNATYLC TTKTSKAYQL FALPKNGPVL KPGLRRVQDS
560 570 580 590 600
NGSQIELEVY SVPKELFGAF ISMVPEPLGI GSVELESGEW IKSFICEESG
610 620 630 640 650
YKAKGTVDIT KYGGFRAYFE MLKKKESQKK KLFDTVLIAN RGEIAVRIIK
660 670 680 690 700
TLKKLGIRSV AVYSDPDKYS QHVTDADVSV PLHGTTAAQT YLDMNKIIDA
710 720 730 740 750
AKQTNAQAII PGYGFLSENA DFSDACTSAG ITFVGPSGDI IRGLGLKHSA
760 770 780 790 800
RQIAQKAGVP LVPGSLLITS VEEAKKVAAE LEYPVMVKST AGGGGIGLQK
810 820 830 840 850
VDSEEDIEHI FETVKHQGET FFGDAGVFLE RFIENARHVE VQLMGDGFGK
860 870 880 890 900
AIALGERDCS LQRRNQKVIE ETPAPNLPEK TRLALRKAAE SLGSLLNYKC
910 920 930 940 950
AGTVEFIYDE KKDEFYFLEV NTRLQVEHPI TEMVTGLDLV EWMIRIAAND
960 970 980 990 1000
APDFDSTKVE VNGVSMEARL YAENPLKNFR PSPGLLVDVK FPDWARVDTW
1010 1020 1030 1040 1050
VKKGTNISPE YDPTLAKIIV HGKDRDDAIS KLNQALEETK VYGCITNIDY
1060 1070 1080 1090 1100
LKSIITSDFF AKAKVSTNIL NSYQYEPTAI EITLPGAHTS IQDYPGRVGY
1110 1120 1130 1140 1150
WRIGVPPSGP MDAYSFRLAN RIVGNDYRTP AIEVTLTGPS IVFHCETVIA
1160 1170 1180 1190 1200
ITGGTALCTL DGQEIPQHKP VEVKRGSTLS IGKLTSGCRA YLGIRGGIDV
1210 1220 1230 1240 1250
PKYLGSYSTF TLGNVGGYNG RVLKLGDVLF LPSNEENKSV ECLPQNIPQS
1260 1270 1280 1290 1300
LIPQISETKE WRIGVTCGPH GSPDFFKPES IEEFFSEKWK VHYNSNRFGV
1310 1320 1330 1340 1350
RLIGPKPKWA RSNGGEGGMH PSNTHDYVYS LGAINFTGDE PVIITCDGPS
1360 1370 1380 1390 1400
LGGFVCQAVV PEAELWKVGQ VKPGDSIQFV PLSYESSRSL KESQDVAIKS
1410 1420 1430 1440 1450
LDGTKLRRLD SVSILPSFET PILAQMEKVN ELSPKVVYRQ AGDRYVLVEY
1460 1470 1480 1490 1500
GDNEMNFNIS YRIECLISLV KKNKTIGIVE MSQGVRSVLI EFDGYKVTQK
1510 1520 1530 1540 1550
ELLKVLVAYE TEIQFDENWK ITSNIIRLPM AFEDSKTLAC VQRYQETIRS
1560 1570 1580 1590 1600
SAPWLPNNVD FIANVNGISR NEVYDMLYSA RFMVLGLGDV FLGSPCAVPL
1610 1620 1630 1640 1650
DPRHRFLGSK YNPSRTYTER GAVGIGGMYM CIYAANSPGG YQLVGRTIPI
1660 1670 1680 1690 1700
WDKLCLAASS EVPWLMNPFD QVEFYPVSEE DLDKMTEDCD NGVYKVNIEK
1710 1720 1730 1740 1750
SVFDHQEYLR WINANKDSIT AFQEGQLGER AEEFAKLIQN ANSELKESVT
1760 1770 1780 1790 1800
VKPDEEEDFP EGAEIVYSEY SGRFWKSIAS VGDVIEAGQG LLIIEAMKAE
1810 1820 1830
MIISAPKSGK IIKICHGNGD MVDSGDIVAV IETLA
Length:1,835
Mass (Da):201,832
Last modified:October 1, 1994 - v2
<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:iF52B0DD0FE42CD65
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 conflicti96P → R in AAC41643 (PubMed:1802034).Curated1
Sequence conflicti256 – 258LKK → KKN in AAC41643 (PubMed:1802034).Curated3
Sequence conflicti459I → M in AAC41643 (PubMed:1802034).Curated1
Sequence conflicti830E → K in AAC41643 (PubMed:1802034).Curated1
Sequence conflicti1395D → E in AAC41643 (PubMed:1802034).Curated1

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
M64926 Genomic DNA Translation: AAC41643.1
Z36077 Genomic DNA Translation: CAA85172.1
Z21487 Genomic DNA Translation: CAA79695.1
BK006936 Genomic DNA Translation: DAA07325.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S46082

NCBI Reference Sequences

More...
RefSeqi
NP_009767.1, NM_001178556.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YBR208C_mRNA; YBR208C_mRNA; YBR208C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852507

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YBR208C

<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
M64926 Genomic DNA Translation: AAC41643.1
Z36077 Genomic DNA Translation: CAA85172.1
Z21487 Genomic DNA Translation: CAA79695.1
BK006936 Genomic DNA Translation: DAA07325.1
PIRiS46082
RefSeqiNP_009767.1, NM_001178556.1

3D structure databases

ProteinModelPortaliP32528
SMRiP32528
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32904, 39 interactors
DIPiDIP-6296N
IntActiP32528, 9 interactors
STRINGi4932.YBR208C

PTM databases

iPTMnetiP32528

Proteomic databases

MaxQBiP32528
PaxDbiP32528
PRIDEiP32528

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR208C_mRNA; YBR208C_mRNA; YBR208C
GeneIDi852507
KEGGisce:YBR208C

Organism-specific databases

EuPathDBiFungiDB:YBR208C
SGDiS000000412 DUR1,2

Phylogenomic databases

HOGENOMiHOG000251581
InParanoidiP32528
KOiK14541
OMAiHYNSNRL

Enzyme and pathway databases

UniPathwayi
UPA00258;UER00371

UPA00258;UER00372

BioCyciMetaCyc:YBR208C-MONOMER
YEAST:YBR208C-MONOMER
BRENDAi6.3.4.6 984
ReactomeiR-SCE-8951664 Neddylation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P32528

Family and domain databases

Gene3Di2.40.100.10, 2 hits
3.90.1300.10, 1 hit
InterProiView protein in InterPro
IPR014085 Allophanate_hydrolase
IPR023631 Amidase_dom
IPR036928 AS_sf
IPR011761 ATP-grasp
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR003778 CT_A_B
IPR003833 CT_C_D
IPR029000 Cyclophilin-like_dom_sf
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
IPR014084 Urea_COase
PfamiView protein in Pfam
PF01425 Amidase, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02786 CPSase_L_D2, 1 hit
PF02626 CT_A_B, 1 hit
PF02682 CT_C_D, 1 hit
SMARTiView protein in SMART
SM00796 AHS1, 1 hit
SM00797 AHS2, 1 hit
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF50891 SSF50891, 2 hits
SSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52440 SSF52440, 1 hit
SSF75304 SSF75304, 1 hit
TIGRFAMsiTIGR02713 allophanate_hyd, 1 hit
TIGR00724 urea_amlyse_rel, 1 hit
TIGR02712 urea_carbox, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<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 nameiDUR1_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: P32528
Secondary accession number(s): D6VQK5
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1994
Last modified: February 13, 2019
This is version 188 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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