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UniProtKB/Swiss-Prot entry Q91437

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PYR1_SQUAC
Primary accession number Q91437
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 74)
Name and origin of the protein
Protein name CAD protein
Synonyms None
Includes Glutamine-dependent carbamoyl-phosphate synthase
     (EC 6.3.5.5)
Aspartate carbamoyltransferase
     (EC 2.1.3.2)
Dihydroorotase
     (EC 3.5.2.3)
Gene name
Name: CAD
From
Squalus acanthias (Spiny dogfish) [TaxID: 7797] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; Elasmobranchii; Squalea; Hypnosqualea; Squaliformes; Squaloidei; Squalidae; Squalus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen, and Testis;
DOI=10.1074/jbc.270.23.14130; PubMed=7775474 [NCBI, ExPASy, EBI, Israel, Japan]
Hong J., Salo W.L., Anderson P.M.;
"Nucleotide sequence and tissue-specific expression of the multifunctional protein carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase (CAD) mRNA in Squalus acanthias.";
J. Biol. Chem. 270:14130-14139(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U18868; AAA74569.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A57541; A57541.
3D structure databases
HSSP P77918; 1ML4. [HSSP ENTRY / PDB]
ModBase Q91437.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004088; Molecular function: carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity (inferred from electronic annotation from EC).
GO:0004151; Molecular function: dihydroorotase activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006680; Amidohydro_1.
IPR006220; Anth_synthII.
IPR006130; Asp/Orn_carbamoyltranf.
IPR006132; Asp/Orn_carbamoyltranf_P_bd.
IPR006131; Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082; Aspartate_carbamoyltransf_euk.
IPR011761; ATP-grasp.
IPR013816; ATP_grasp_subdomain_2.
IPR001317; CarbamoylP_synth_GATase.
IPR005483; CarbamoylP_synth_lsu.
IPR005479; CarbamoylP_synth_lsu_ATP-bd.
IPR006275; CarbamoylP_synth_lsu_Gln-dep.
IPR005481; CarbamoylP_synth_lsu_N.
IPR005480; CarbamoylP_synth_lsu_oligo.
IPR006274; CarbamoylP_synth_ssu.
IPR002474; CarbamoylP_synth_ssu_N.
IPR004722; DHOmult.
IPR002195; Dihydroorotase_CS.
IPR011702; GATASE.
IPR012998; GATase_1_AS.
IPR000991; GATase_class1_C.
IPR011607; MGS.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.
Gene3D G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
G3DSA:3.40.50.20; Pre-ATP_grasp; 2.
Pfam PF01979; Amidohydro_1; 1.
PF00289; CPSase_L_chain; 2.
PF02786; CPSase_L_D2; 2.
PF02787; CPSase_L_D3; 1.
PF00988; CPSase_sm_chain; 1.
PF00117; GATase; 1.
PF02142; MGS; 1.
PF00185; OTCace; 1.
PF02729; OTCace_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00097; ANTSNTHASEII.
PR00100; AOTCASE.
PR00101; ATCASE.
PR00098; CPSASE.
PR00099; CPSGATASE.
PR00096; GATASE.
TIGRFAMs TIGR00670; asp_carb_tr; 1.
TIGR01369; CPSaseII_lrg; 1.
TIGR01368; CPSaseIIsmall; 1.
TIGR00857; pyrC_multi; 1.
PROSITE PS50975; ATP_GRASP; 2.
PS00097; CARBAMOYLTRANSFERASE; 1.
PS00866; CPSASE_1; 2.
PS00867; CPSASE_2; 2.
PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q91437.
ProtoNet Q91437.
Phylogenomic databases
HOVERGEN Q91437; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Allosteric enzyme; Cytoplasm; Hydrolase; Ligase; Metal-binding; Multifunctional enzyme; Phosphoprotein; Pyrimidine biosynthesis; Repeat; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   2242  2242     CAD protein. PRO_0000199508
DOMAIN   177    363  187     Glutamine amidotransferase type-1. 
DOMAIN   522    714  193     ATP-grasp 1. 
DOMAIN   1057   1248  192     ATP-grasp 2. 
REGION   1    365  365     GATase (Glutamine amidotransferase). 
REGION   366    397  32     Linker. 
REGION   398   1462  1065     CPSase (Carbamoyl-phosphate synthase). 
REGION   398    937  540     CPSase A. 
REGION   938   1462  525     CPSase B. 
REGION   1463   1796  334     DHOase (dihydroorotase). 
REGION   1797   1934  138     Linker. 
REGION   1935   2242  308     ATCase (Aspartate transcarbamylase). 
ACT_SITE   252    252        For GATase activity (By similarity). 
ACT_SITE   336    336        For GATase activity (By similarity). 
ACT_SITE   338    338        For GATase activity (By similarity). 
METAL   1478   1478        Zinc (Potential). 
METAL   1480   1480        Zinc (Potential). 
Sequence information
Length: 2242 AA [This is the length of the unprocessed precursor] Molecular weight: 249393 Da [This is the MW of the unprocessed precursor] CRC64: 99F1986BA41244EA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MATLFLDDGS SFKGRLFGAS STVSGEVVFQ TGMVGYPEAL TDPSYLSQIL VLTYPLIGNY 

        70         80         90        100        110        120 
GIPKDEEDEH GLSKWFESAK IHAAALVIGE NSQNPSHWSS VRSLDQRLKE HGIPALEGID 

       130        140        150        160        170        180 
TRSLTKKIRE KGTLLGKLVI DGTDENSLPY DDPNKRHLVK EVSIKEPKVY HPSGNVKIMA 

       190        200        210        220        230        240 
VDCGMKYNQI RSLCKRGAAV TVVPWDYLFD SNEFDGLFIS NGPGDPEYCQ QTINNVKKAI 

       250        260        270        280        290        300 
SEEKPKPLFG ICLGHQILSL AIGAKTYKMK YGNRGHNQPC IHEGTQRCFY TSQNHGFAVE 

       310        320        330        340        350        360 
PCSLPRDWSV LFTNANDQSN EGIIHNSKPL FSVQFHPEHK AGPTDLVDLF DIFLECARDV 

       370        380        390        400        410        420 
KLGVNLDKTV KGRVISHYSF KNGTENSKTP PGRIQPHKVL ILGSGGLSIG QAGEFDYSGS 

       430        440        450        460        470        480 
QAIKALKEEN VQSVLINPNI ATVQTSKGLA DKVYFLPITP EYVTQVIMNE RPDGILLTFG 

       490        500        510        520        530        540 
GQTALNCGVE LQKRGVLEKY HVRVLGTPVS SIEMTEDRKI FVEKMAEINE YVVPSEAAFT 

       550        560        570        580        590        600 
LEQAQGAAER LGYPVLVRAA FALGGLGSGF AQNKEELVTL VTQAFAHTSQ ILVDKSLKGW 

       610        620        630        640        650        660 
KEIEYEVVRD AYDNCITVCN MENVDPLGIH TGESIVVAPS QTLNDKEYNL LRTTAIKVIR 

       670        680        690        700        710        720 
HLGVVGECNI QYALSPESEQ YFIIEVNARL SRSSALASKA TGYPLAYVAA KLALGIPLPV 

       730        740        750        760        770        780 
LRNSVTNSTT ANYEPSLDYC VVKVPRWDLS KFLRLSTKIG SSMKSVGEVM AIGRNFEEAF 

       790        800        810        820        830        840 
QKALRMVDEN CVGFDHTLKP ASDEELETPT DKRIFVLAAA LRAGYEIDRL YELTKIDKWF 

       850        860        870        880        890        900 
LHKMKNIVEY SLKLSELYMK DEVPRHDLLK VKRLGFSDKQ IAMAIQSTEL AVRRLRQEWK 

       910        920        930        940        950        960 
ILPVVKQIDT VAAEWPAQTN YLYLTYNGEG HDLDFTKPHV MVIGSGVYRI GSSVEFDWCA 

       970        980        990       1000       1010       1020 
VRCIQQLRKM GYKTRMVNYN PETVSTDYDM CDRLYFDEIS FEVVMDIYEL ENPEGIILSM 

      1030       1040       1050       1060       1070       1080 
GGQLPNNIAM DLHRQQCRIL GTSPESIDTA ENRFKFSRML DTIGISQPRW KELSDTESSK 

      1090       1100       1110       1120       1130       1140 
QFCTKVGYPC LIRPSYVLSG VAMNVAYSDN DLEKFLSSAV AVSKEHPVVI SKFIQEAKEI 

      1150       1160       1170       1180       1190       1200 
DVDAVACDGV VIAVAISEHV ENAGVHSGDA TLVTPPQDLN QKTTERIKAI VHAIGQELQA 

      1210       1220       1230       1240       1250       1260 
TGPFNLQLIA KDDQLKVIEC NVRVSRSFPF VSKTLGVDMI ALATKVIMGE EVEPVGLMTG 

      1270       1280       1290       1300       1310       1320 
TGVVGVKVPQ FSFSRLAGAD VVLGVEMTST GEVACFGENR YEAYLKAMLS TGFKIPKKNI 

      1330       1340       1350       1360       1370       1380 
LLSIGSYKNK SELLSTVQSL EQLGYNLYAS LGTADFYTEH GVKIKAVDWP FEDTDNGCPL 

      1390       1400       1410       1420       1430       1440 
KERHRNIMDY LEENHFDLVI NLSMRNSGGR RLSSFVTKGY RTRRLAVDYS VPLIIDIKCT 

      1450       1460       1470       1480       1490       1500 
KLFVEALRLV GDTPPVKTHI DSMSSHKLIR LPGLIDVHVH LREPGGTHKE DFASGTAAAL 

      1510       1520       1530       1540       1550       1560 
AGGVTMVCAM PNTNPAITDQ TSFALVQKLA TAGARCDFAL FLGASSDNAD VLPLISNSAA 

      1570       1580       1590       1600       1610       1620 
GLKMYLNDTF STLKMDNVSL WMEHFEKWPK HLPIVVHAER QTVAAILMVA QLYQRPVHIC 

      1630       1640       1650       1660       1670       1680 
HVARKEEIQI IRAAKQKGVQ VTCEVAPHHL FLNEEDLESI GHGKGQVRPM LSTKEDVNAL 

      1690       1700       1710       1720       1730       1740 
WENLDVIDCF ATDHAPHSVE EKNSDSPPPG YPGLETMLPL LLTAVSEGRL TIDDLVKRLY 

      1750       1760       1770       1780       1790       1800 
ENPRKIFSLP VQENTYVEVD LEQEWIIPSY MQFTKSKWTP FEGKKVKGRV RRVVLRGEVA 

      1810       1820       1830       1840       1850       1860 
YIDGQVLVPP GYGQDVRAWP LGVPLPPPPT TVKTPEHSKP TQTETVRTRT ASPRRLASSG 

      1870       1880       1890       1900       1910       1920 
PAVDARFHLP PRIHRCSDPG LPNAEGEYKE KPVKKFIEQD TVSQDGYIYP PPVSRLLSPQ 

      1930       1940       1950       1960       1970       1980 
NLAAQAVPHP YSLLLHPFVG QHILSVKRFT KDQLSHLFNV AHNLRLTVQK DRSLDILKGK 

      1990       2000       2010       2020       2030       2040 
VMASMFYEVS TRTSSSFRAA MHRLGGSVIH FSEATSSVQK GESLLDSVQT MSCYVDVVVL 

      2050       2060       2070       2080       2090       2100 
RHPEPGAVEL AAKHSRKPII NAGDGVGEHP TQALLDIFTI REELGTVNGM TITMVGDLKH 

      2110       2120       2130       2140       2150       2160 
GRTVHSLAYL LTLYRVNLRY VTPRNLRMPP NIIRFLASRG IKQEEFDSLE EALPDTDVLY 

      2170       2180       2190       2200       2210       2220 
MTRIQKERFA SEEEYEACFG QFILTPHIMT KGKKKMVVMH PLPRVNEVSV EVDSDPRAAY 

      2230       2240 
FRQAENGMYV RMALLATVLG KF
Q91437 in FASTA format

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