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UniProtKB - Q91437 (PYR1_SQUAC)

Entry version 139 (02 Dec 2020)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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Protein

CAD protein

Gene

CAD

Organism
Squalus acanthias (Spiny dogfish)
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 transcript 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

This protein is a 'fusion' protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).

<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

<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

Zn2+By similarityNote: Binds 3 Zn2+ ions per subunit (for dihydroorotase activity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate is an activator while UMP is an inhibitor of the CPSase reaction (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1, 2 and 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. CAD protein (CAD)
  2. CAD protein (CAD)
  3. CAD protein (CAD)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei252For GATase activityBy similarity1
Active sitei336For GATase activityBy similarity1
Active sitei338For GATase activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1478Zinc 1; via tele nitrogenBy similarity1
Metal bindingi1478Zinc 2; via pros nitrogenBy similarity1
Metal bindingi1480Zinc 1; via tele nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei1482N-carbamoyl-L-aspartateBy similarity1
Binding sitei1512N-carbamoyl-L-aspartateBy similarity1
Metal bindingi1563Zinc 1; via carbamate groupBy similarity1
Metal bindingi1563Zinc 3; via carbamate groupBy similarity1
Metal bindingi1597Zinc 3; via pros nitrogenBy similarity1
Metal bindingi1620Zinc 2By similarity1
Metal bindingi1621Zinc 3; via tele nitrogenBy similarity1
Metal bindingi1644Zinc 2By similarity1
Binding sitei1668N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi1693Zinc 1By similarity1
Binding sitei1693N-carbamoyl-L-aspartateBy similarity1
Binding sitei1697N-carbamoyl-L-aspartateBy similarity1

<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 functionAllosteric enzyme, Hydrolase, Ligase, Multifunctional enzyme, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

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

More...UniPathwayi		UPA00070;UER00115
UPA00070;UER00116
UPA00070;UER00117

<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:
CAD protein
Including the following 3 domains:
Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.5)
Aspartate carbamoyltransferase (EC:2.1.3.2)
Dihydroorotase (EC:3.5.2.3)
<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:CAD
<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>OrganismiSqualus acanthias (Spiny dogfish)
<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 identifieri7797 [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 › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalomorphii › Squaliformes › Squalidae › Squalus

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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_00001995081 – 2242CAD proteinAdd BLAST2242

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 residuei1563N6-carboxylysineBy similarity1

Keywords - PTMi

Phosphoprotein

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Present in the testis but not in the liver.1 Publication

<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

Homohexamer.

<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		Q91437

Database of comparative protein structure models

More...ModBasei		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>Domaini177 – 363Glutamine amidotransferase type-1Add BLAST187
Domaini522 – 714ATP-grasp 1Add BLAST193
Domaini1057 – 1248ATP-grasp 2Add BLAST192
Domaini1313 – 1469MGS-likePROSITE-ProRule annotationAdd BLAST157

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 365GATase (Glutamine amidotransferase)Add BLAST365
Regioni366 – 397LinkerAdd BLAST32
Regioni398 – 1462CPSase (Carbamoyl-phosphate synthase)Add BLAST1065
Regioni398 – 937CPSase AAdd BLAST540
Regioni938 – 1462CPSase BAdd BLAST525
Regioni1463 – 1796DHOase (dihydroorotase)Add BLAST334
Regioni1797 – 1934LinkerAdd BLAST138
Regioni1935 – 2242ATCase (Aspartate transcarbamylase)Add BLAST308

<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

In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.Curated

Keywords - Domaini

Repeat

Family and domain databases

Conserved Domains Database

More...CDDi		cd01744, GATase1_CPSase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.1370, 2 hits
3.40.50.1380, 1 hit
3.40.50.880, 1 hit
3.50.30.20, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00001, Asp_carb_tr, 1 hit
MF_01209, CPSase_S_chain, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006680, Amidohydro-rel
IPR006132, Asp/Orn_carbamoyltranf_P-bd
IPR006130, Asp/Orn_carbamoylTrfase
IPR036901, Asp/Orn_carbamoylTrfase_sf
IPR002082, Asp_carbamoyltransf
IPR006131, Asp_carbamoyltransf_Asp/Orn-bd
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR006275, CarbamoylP_synth_lsu
IPR005480, CarbamoylP_synth_lsu_oligo
IPR036897, CarbamoylP_synth_lsu_oligo_sf
IPR006274, CarbamoylP_synth_ssu
IPR002474, CarbamoylP_synth_ssu_N
IPR036480, CarbP_synth_ssu_N_sf
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR005483, CbamoylP_synth_lsu_CPSase_dom
IPR029062, Class_I_gatase-like
IPR035686, CPSase_GATase1
IPR002195, Dihydroorotase_CS
IPR017926, GATASE
IPR011059, Metal-dep_hydrolase_composite
IPR032466, Metal_Hydrolase
IPR011607, MGS-like_dom
IPR036914, MGS-like_dom_sf
IPR016185, PreATP-grasp_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01979, Amidohydro_1, 1 hit
PF02786, CPSase_L_D2, 2 hits
PF02787, CPSase_L_D3, 1 hit
PF00988, CPSase_sm_chain, 1 hit
PF00117, GATase, 1 hit
PF02142, MGS, 1 hit
PF00185, OTCace, 1 hit
PF02729, OTCace_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00100, AOTCASE
PR00098, CPSASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01096, CPSase_L_D3, 1 hit
SM01097, CPSase_sm_chain, 1 hit
SM00851, MGS, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48108, SSF48108, 1 hit
SSF51338, SSF51338, 1 hit
SSF51556, SSF51556, 1 hit
SSF52021, SSF52021, 1 hit
SSF52317, SSF52317, 1 hit
SSF52335, SSF52335, 1 hit
SSF52440, SSF52440, 2 hits
SSF53671, SSF53671, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00670, asp_carb_tr, 1 hit
TIGR01369, CPSaseII_lrg, 1 hit
TIGR01368, CPSaseIIsmall, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50975, ATP_GRASP, 2 hits
PS00097, CARBAMOYLTRANSFERASE, 1 hit
PS00866, CPSASE_1, 2 hits
PS00867, CPSASE_2, 2 hits
PS00482, DIHYDROOROTASE_1, 1 hit
PS00483, DIHYDROOROTASE_2, 1 hit
PS51273, GATASE_TYPE_1, 1 hit
PS51855, MGS, 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.

Q91437-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATLFLDDGS SFKGRLFGAS STVSGEVVFQ TGMVGYPEAL TDPSYLSQIL 
        60         70         80         90        100
VLTYPLIGNY GIPKDEEDEH GLSKWFESAK IHAAALVIGE NSQNPSHWSS 
       110        120        130        140        150
VRSLDQRLKE HGIPALEGID TRSLTKKIRE KGTLLGKLVI DGTDENSLPY 
       160        170        180        190        200
DDPNKRHLVK EVSIKEPKVY HPSGNVKIMA VDCGMKYNQI RSLCKRGAAV 
       210        220        230        240        250
TVVPWDYLFD SNEFDGLFIS NGPGDPEYCQ QTINNVKKAI SEEKPKPLFG 
       260        270        280        290        300
ICLGHQILSL AIGAKTYKMK YGNRGHNQPC IHEGTQRCFY TSQNHGFAVE 
       310        320        330        340        350
PCSLPRDWSV LFTNANDQSN EGIIHNSKPL FSVQFHPEHK AGPTDLVDLF 
       360        370        380        390        400
DIFLECARDV KLGVNLDKTV KGRVISHYSF KNGTENSKTP PGRIQPHKVL 
       410        420        430        440        450
ILGSGGLSIG QAGEFDYSGS QAIKALKEEN VQSVLINPNI ATVQTSKGLA 
       460        470        480        490        500
DKVYFLPITP EYVTQVIMNE RPDGILLTFG GQTALNCGVE LQKRGVLEKY 
       510        520        530        540        550
HVRVLGTPVS SIEMTEDRKI FVEKMAEINE YVVPSEAAFT LEQAQGAAER 
       560        570        580        590        600
LGYPVLVRAA FALGGLGSGF AQNKEELVTL VTQAFAHTSQ ILVDKSLKGW 
       610        620        630        640        650
KEIEYEVVRD AYDNCITVCN MENVDPLGIH TGESIVVAPS QTLNDKEYNL 
       660        670        680        690        700
LRTTAIKVIR HLGVVGECNI QYALSPESEQ YFIIEVNARL SRSSALASKA 
       710        720        730        740        750
TGYPLAYVAA KLALGIPLPV LRNSVTNSTT ANYEPSLDYC VVKVPRWDLS 
       760        770        780        790        800
KFLRLSTKIG SSMKSVGEVM AIGRNFEEAF QKALRMVDEN CVGFDHTLKP 
       810        820        830        840        850
ASDEELETPT DKRIFVLAAA LRAGYEIDRL YELTKIDKWF LHKMKNIVEY 
       860        870        880        890        900
SLKLSELYMK DEVPRHDLLK VKRLGFSDKQ IAMAIQSTEL AVRRLRQEWK 
       910        920        930        940        950
ILPVVKQIDT VAAEWPAQTN YLYLTYNGEG HDLDFTKPHV MVIGSGVYRI 
       960        970        980        990       1000
GSSVEFDWCA VRCIQQLRKM GYKTRMVNYN PETVSTDYDM CDRLYFDEIS 
      1010       1020       1030       1040       1050
FEVVMDIYEL ENPEGIILSM GGQLPNNIAM DLHRQQCRIL GTSPESIDTA 
      1060       1070       1080       1090       1100
ENRFKFSRML DTIGISQPRW KELSDTESSK QFCTKVGYPC LIRPSYVLSG 
      1110       1120       1130       1140       1150
VAMNVAYSDN DLEKFLSSAV AVSKEHPVVI SKFIQEAKEI DVDAVACDGV 
      1160       1170       1180       1190       1200
VIAVAISEHV ENAGVHSGDA TLVTPPQDLN QKTTERIKAI VHAIGQELQA 
      1210       1220       1230       1240       1250
TGPFNLQLIA KDDQLKVIEC NVRVSRSFPF VSKTLGVDMI ALATKVIMGE 
      1260       1270       1280       1290       1300
EVEPVGLMTG TGVVGVKVPQ FSFSRLAGAD VVLGVEMTST GEVACFGENR 
      1310       1320       1330       1340       1350
YEAYLKAMLS TGFKIPKKNI LLSIGSYKNK SELLSTVQSL EQLGYNLYAS 
      1360       1370       1380       1390       1400
LGTADFYTEH GVKIKAVDWP FEDTDNGCPL KERHRNIMDY LEENHFDLVI 
      1410       1420       1430       1440       1450
NLSMRNSGGR RLSSFVTKGY RTRRLAVDYS VPLIIDIKCT KLFVEALRLV 
      1460       1470       1480       1490       1500
GDTPPVKTHI DSMSSHKLIR LPGLIDVHVH LREPGGTHKE DFASGTAAAL 
      1510       1520       1530       1540       1550
AGGVTMVCAM PNTNPAITDQ TSFALVQKLA TAGARCDFAL FLGASSDNAD 
      1560       1570       1580       1590       1600
VLPLISNSAA GLKMYLNDTF STLKMDNVSL WMEHFEKWPK HLPIVVHAER 
      1610       1620       1630       1640       1650
QTVAAILMVA QLYQRPVHIC HVARKEEIQI IRAAKQKGVQ VTCEVAPHHL 
      1660       1670       1680       1690       1700
FLNEEDLESI GHGKGQVRPM LSTKEDVNAL WENLDVIDCF ATDHAPHSVE 
      1710       1720       1730       1740       1750
EKNSDSPPPG YPGLETMLPL LLTAVSEGRL TIDDLVKRLY ENPRKIFSLP 
      1760       1770       1780       1790       1800
VQENTYVEVD LEQEWIIPSY MQFTKSKWTP FEGKKVKGRV RRVVLRGEVA 
      1810       1820       1830       1840       1850
YIDGQVLVPP GYGQDVRAWP LGVPLPPPPT TVKTPEHSKP TQTETVRTRT 
      1860       1870       1880       1890       1900
ASPRRLASSG PAVDARFHLP PRIHRCSDPG LPNAEGEYKE KPVKKFIEQD 
      1910       1920       1930       1940       1950
TVSQDGYIYP PPVSRLLSPQ NLAAQAVPHP YSLLLHPFVG QHILSVKRFT 
      1960       1970       1980       1990       2000
KDQLSHLFNV AHNLRLTVQK DRSLDILKGK VMASMFYEVS TRTSSSFRAA 
      2010       2020       2030       2040       2050
MHRLGGSVIH FSEATSSVQK GESLLDSVQT MSCYVDVVVL RHPEPGAVEL 
      2060       2070       2080       2090       2100
AAKHSRKPII NAGDGVGEHP TQALLDIFTI REELGTVNGM TITMVGDLKH 
      2110       2120       2130       2140       2150
GRTVHSLAYL LTLYRVNLRY VTPRNLRMPP NIIRFLASRG IKQEEFDSLE 
      2160       2170       2180       2190       2200
EALPDTDVLY MTRIQKERFA SEEEYEACFG QFILTPHIMT KGKKKMVVMH 
      2210       2220       2230       2240 
PLPRVNEVSV EVDSDPRAAY FRQAENGMYV RMALLATVLG KF
Length:2,242
Mass (Da):249,393
Last modified:November 1, 1996 - 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:i99F1986BA41244EA
GO

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
U18868 mRNA Translation: AAA74569.1

Protein sequence database of the Protein Information Resource

More...PIRi		A57541

<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
U18868 mRNA Translation: AAA74569.1
PIRiA57541

3D structure databases

SMRiQ91437
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00070;UER00115
UPA00070;UER00116
UPA00070;UER00117

Family and domain databases

CDDicd01744, GATase1_CPSase, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.1370, 2 hits
3.40.50.1380, 1 hit
3.40.50.880, 1 hit
3.50.30.20, 1 hit
HAMAPiMF_00001, Asp_carb_tr, 1 hit
MF_01209, CPSase_S_chain, 1 hit
InterProiView protein in InterPro
IPR006680, Amidohydro-rel
IPR006132, Asp/Orn_carbamoyltranf_P-bd
IPR006130, Asp/Orn_carbamoylTrfase
IPR036901, Asp/Orn_carbamoylTrfase_sf
IPR002082, Asp_carbamoyltransf
IPR006131, Asp_carbamoyltransf_Asp/Orn-bd
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR006275, CarbamoylP_synth_lsu
IPR005480, CarbamoylP_synth_lsu_oligo
IPR036897, CarbamoylP_synth_lsu_oligo_sf
IPR006274, CarbamoylP_synth_ssu
IPR002474, CarbamoylP_synth_ssu_N
IPR036480, CarbP_synth_ssu_N_sf
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR005483, CbamoylP_synth_lsu_CPSase_dom
IPR029062, Class_I_gatase-like
IPR035686, CPSase_GATase1
IPR002195, Dihydroorotase_CS
IPR017926, GATASE
IPR011059, Metal-dep_hydrolase_composite
IPR032466, Metal_Hydrolase
IPR011607, MGS-like_dom
IPR036914, MGS-like_dom_sf
IPR016185, PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF01979, Amidohydro_1, 1 hit
PF02786, CPSase_L_D2, 2 hits
PF02787, CPSase_L_D3, 1 hit
PF00988, CPSase_sm_chain, 1 hit
PF00117, GATase, 1 hit
PF02142, MGS, 1 hit
PF00185, OTCace, 1 hit
PF02729, OTCace_N, 1 hit
PRINTSiPR00100, AOTCASE
PR00098, CPSASE
SMARTiView protein in SMART
SM01096, CPSase_L_D3, 1 hit
SM01097, CPSase_sm_chain, 1 hit
SM00851, MGS, 1 hit
SUPFAMiSSF48108, SSF48108, 1 hit
SSF51338, SSF51338, 1 hit
SSF51556, SSF51556, 1 hit
SSF52021, SSF52021, 1 hit
SSF52317, SSF52317, 1 hit
SSF52335, SSF52335, 1 hit
SSF52440, SSF52440, 2 hits
SSF53671, SSF53671, 1 hit
TIGRFAMsiTIGR00670, asp_carb_tr, 1 hit
TIGR01369, CPSaseII_lrg, 1 hit
TIGR01368, CPSaseIIsmall, 1 hit
PROSITEiView protein in PROSITE
PS50975, ATP_GRASP, 2 hits
PS00097, CARBAMOYLTRANSFERASE, 1 hit
PS00866, CPSASE_1, 2 hits
PS00867, CPSASE_2, 2 hits
PS00482, DIHYDROOROTASE_1, 1 hit
PS00483, DIHYDROOROTASE_2, 1 hit
PS51273, GATASE_TYPE_1, 1 hit
PS51855, MGS, 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 nameiPYR1_SQUAC
<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: Q91437
<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: July 15, 1998
Last sequence update: November 1, 1996
Last modified: December 2, 2020
This is version 139 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 programChordata 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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