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Protein Overview: DUR1,2

General Information:
Name(s) found: DUR1,2 / YBR208C [SGD]
Description(s) found:
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  • gi|6319685|ref|NP_009767.1| Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin [NCBI NR]
  • pir||S46082 urea carboxylase (EC 6.3.4.6) - yeast (Saccharomyces cerevisiae) [NCBI NR]
  • gi|585072|sp|P32528.2|DUR1_YEAST RecName: Full=Urea amidolyase; Includes: RecName: Full=Urea carboxylase; Includes: RecName: Full=Allophanate hydrolase [NCBI NR]
  • gi|536588|emb|CAA85172.1| DUR1,2 [Saccharomyces cerevisiae] [NCBI NR]
  • Urea amidolyase OS=Saccharomyces cerevisiae GN=DUR1,2 PE=1 SV=2 [Swiss-Prot]
  • DUR1,2 Urea amidolyase [mips]
  • Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation [SGD]
  • DUR1,2, Chr II from 636661-642168, reverse complement [yeast_orfs2]
  • Chr II from 636661-642168, reverse complement [yeastorf3.fasta]
  • Chr II from 636660-642167, reverse complement [yeastorf4.fasta]
  • Chr II from 642165-636658, reverse complement [yeastorf5.fasta]
  • (P32528) Urea amidolyase [Includes: Urea carboxylase (EC 6.3.4.6); Allophanate hydrolase (EC 3.5.1.54)] [4932.FASTACCERV.txt]
  • DUR1,2 SGDID:S0000412, Chr II from 642167-636660, reverse complement, Verified ORF [yeastflysequest.fasta]
  • DUR1,2 SGDID:S0000412, Chr II from 642205-636698, reverse complement, Verified ORF [10112005cervSGD.fasta]
  • Dur1,2p [Saccharomyces cerevisiae]gi|536588|emb|CAA85172.1| DUR1,2 [Saccharomyces cerevisiae]gi|626973|pir||S46082 urea carboxylase (EC 6.3.4.6) - yeast (Saccharomyces cerevisiae)gi|585072|sp|P32528|DUR1_YEAST Urea amidolyase [Includes: Urea carboxylas [nrdb_11152004_Chlamydomonas]
  • DUR1,2 SGDID:S000000412, Chr II from 642205-636698, reverse complement, Verified ORF, "Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repressi [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
  • Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; Dur1,2p [Sacch [nr-271106-contam.fasta]
  • DUR1,2 [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • Urea amidolyase [Includes: Urea carboxylase ; Allophanate hydrolase ] [nr-271106-contam.fasta]
  • DUR1,2 SGDID:S000000412, Chr II from 642205-636698, reverse complement, Verified ORF, "Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation" [yeast-bovrabprots.fasta]
  • [chemostatdb.fasta]
  • Urea amidolyase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=DUR1,2 PE=1 SV=2 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
  • DUR1,2 SGDID:S000000412, Chr II from 642210-636703, Genome Release 64-1-1, reverse complement, Verified ORF, "Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation" [yeast-030211-contam.fasta]
  • DUR1,2 SGDID:S000000412, Chr II from 642210-636703, Genome Release 64-2-1, reverse complement, Verified ORF, "Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress" [20141208_orf_trans.fasta]
  • YBR208C SGDID:S000000412, Chr II from 642210-636703, Genome Release 64-1-1, reverse complement, Verified ORF, "Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
    • Organism: Saccharomyces cerevisiae
    Length: 1835 amino acids

    Gene Ontology:
    Cellular Component: cytoplasm [IDALink to PubMed article]
    Biological Process: urea metabolic process [IMPLink to PubMed article]
    allantoin catabolic process [TASLink to PubMed article]
    Molecular Function: allophanate hydrolase activity [IMPLink to PubMed article]
    urea carboxylase activity [IMPLink to PubMed article]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MTVSSDTTAE ISLGWSIQDW IDFHKSSSSQ ASLRLLESLL DSQNVAPVDN AWISLISKEN  60
   61 LLHQFQILKS RENKETLPLY GVPIAVKDNI DVRGLPTTAA CPSFAYEPSK DSKVVELLRN 120
  121 AGAIIVGKTN LDQFATGLVG TRSPYGKTPC AFSKEHVSGG SSAGSASVVA RGIVPIALGT 180
  181 DTAGSGRVPA ALNNLIGLKP TKGVFSCQGV VPACKSLDCV SIFALNLSDA ERCFRIMCQP 240
  241 DPDNDEYSRP YVSNPLKKFS SNVTIAIPKN IPWYGETKNP VLFSNAVENL SRTGANVIEI 300
  301 DFEPLLELAR CLYEGTWVAE RYQAIQSFLD SKPPKESLDP TVISIIEGAK KYSAVDCFSF 360
  361 EYKRQGILQK VRRLLESVDV LCVPTCPLNP TMQQVADEPV LVNSRQGTWT NFVNLADLAA 420
  421 LAVPAGFRDD GLPNGITLIG KKFTDYALLE LANRYFQNIF PNGSRTYGTF TSSSVKPAND 480
  481 QLVGPDYDPS TSIKLAVVGA HLKGLPLHWQ LEKVNATYLC TTKTSKAYQL FALPKNGPVL 540
  541 KPGLRRVQDS NGSQIELEVY SVPKELFGAF ISMVPEPLGI GSVELESGEW IKSFICEESG 600
  601 YKAKGTVDIT KYGGFRAYFE MLKKKESQKK KLFDTVLIAN RGEIAVRIIK TLKKLGIRSV 660
  661 AVYSDPDKYS QHVTDADVSV PLHGTTAAQT YLDMNKIIDA AKQTNAQAII PGYGFLSENA 720
  721 DFSDACTSAG ITFVGPSGDI IRGLGLKHSA RQIAQKAGVP LVPGSLLITS VEEAKKVAAE 780
  781 LEYPVMVKST AGGGGIGLQK VDSEEDIEHI FETVKHQGET FFGDAGVFLE RFIENARHVE 840
  841 VQLMGDGFGK AIALGERDCS LQRRNQKVIE ETPAPNLPEK TRLALRKAAE SLGSLLNYKC 900
  901 AGTVEFIYDE KKDEFYFLEV NTRLQVEHPI TEMVTGLDLV EWMIRIAAND APDFDSTKVE 960
  961 VNGVSMEARL YAENPLKNFR PSPGLLVDVK FPDWARVDTW VKKGTNISPE YDPTLAKIIV1020
 1021 HGKDRDDAIS KLNQALEETK VYGCITNIDY LKSIITSDFF AKAKVSTNIL NSYQYEPTAI1080
 1081 EITLPGAHTS IQDYPGRVGY WRIGVPPSGP MDAYSFRLAN RIVGNDYRTP AIEVTLTGPS1140
 1141 IVFHCETVIA ITGGTALCTL DGQEIPQHKP VEVKRGSTLS IGKLTSGCRA YLGIRGGIDV1200
 1201 PKYLGSYSTF TLGNVGGYNG RVLKLGDVLF LPSNEENKSV ECLPQNIPQS LIPQISETKE1260
 1261 WRIGVTCGPH GSPDFFKPES IEEFFSEKWK VHYNSNRFGV RLIGPKPKWA RSNGGEGGMH1320
 1321 PSNTHDYVYS LGAINFTGDE PVIITCDGPS LGGFVCQAVV PEAELWKVGQ VKPGDSIQFV1380
 1381 PLSYESSRSL KESQDVAIKS LDGTKLRRLD SVSILPSFET PILAQMEKVN ELSPKVVYRQ1440
 1441 AGDRYVLVEY GDNEMNFNIS YRIECLISLV KKNKTIGIVE MSQGVRSVLI EFDGYKVTQK1500
 1501 ELLKVLVAYE TEIQFDENWK ITSNIIRLPM AFEDSKTLAC VQRYQETIRS SAPWLPNNVD1560
 1561 FIANVNGISR NEVYDMLYSA RFMVLGLGDV FLGSPCAVPL DPRHRFLGSK YNPSRTYTER1620
 1621 GAVGIGGMYM CIYAANSPGG YQLVGRTIPI WDKLCLAASS EVPWLMNPFD QVEFYPVSEE1680
 1681 DLDKMTEDCD NGVYKVNIEK SVFDHQEYLR WINANKDSIT AFQEGQLGER AEEFAKLIQN1740
 1741 ANSELKESVT VKPDEEEDFP EGAEIVYSEY SGRFWKSIAS VGDVIEAGQG LLIIEAMKAE1800
 1801 MIISAPKSGK IIKICHGNGD MVDSGDIVAV IETLA

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Gavin AC, et al. (2006) DOA4 DUR1,2 MRPL22 PRO1
    View Details Gavin AC, et al. (2002) APM1 CYM1 DOA4 DUR1,2 HSP42 LAT1 LPD1 PDA1 PDB1 PDX1 PRP46 RPN11 TCM62
    View Details Ho Y, et al. (2002) ADR1 ARC15 ARC18 ARC19 ARC35 ARC40 ARP2 ARP3 BBC1 BNI1 CDC39 CDC53 CRM1 DUR1,2 ECM29 ECM33 FAA4 GAL3 GCN1 HRT1 HYP2 IMH1 KAP122 MCM4 MCM7 MDN1 MET18 MKT1 MMS1 MYO2 PFK1 PMA2 RPA190 RPN1 RPT4 SAP185 SIT4 TIP41 TPS1 TRP3 UBI4 VPS13 YAR009C YGP1 YJR029W YLR035C-A YMR209C

    Mass Spectrometry Data

    The following runs contain data for this protein:

      BAIT COMMENTS PUBLICATION
    View Run CEP3 sample cbf3 from feb 2005 Sandall S, et all (2006)
    View Run DAD1 Dam1-765 complex purified from yeast with Dad1-TAP Shimogawa MM, et al. (2006)
    View Run RPA135 No Comments Schneider, DA, et al. (2006)
    View Run ZDS1 Sample 2- cpn2 from june 2005 McCusker D, et al (2007)
    View Run MLP2 #24 Asynchronous Prep3-TiO2 Phosphopeptide enrichment Keck JM, et al. (2011)

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

    New Feature: Upload Your Own Microscopy Data

      PROTEIN(S) PUBLICATION
    View Data DUR1,2 Huh WK, et al. (2003)

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..483] PSI-BLAST 194.980454 No description for 1gr8A_ was found.
    2 View Details [484..604] deduced N/A No confident structure predictions are available.
    3 View Details [605..735] PSI-BLAST 1882.218487 Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), C-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase, (BC), N-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), domain 2
    4 View Details [736..762]
    [833..858]
    [872..963]    		 PSI-BLAST 1882.218487 Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), C-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase, (BC), N-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), domain 2
    5 View Details [763..832]
    [859..871]
    [964..1094]    		 PSI-BLAST 1882.218487 Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), C-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase, (BC), N-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), domain 2
    6 View Details [1095..1417] Pfam 190.244125 Allophanate hydrolase subunit 2 No confident structure predictions are available.
    7 View Details [1418..1655] Pfam 3.008774 Allophanate hydrolase subunit 1 No confident structure predictions are available.
    8 View Details [1656..1751] deduced N/A Confident ab initio structure predictions are available.
    9 View Details [1752..1835] PSI-BLAST 46.09691 Biotin carboxyl carrier domain of transcarboxylase (TC 1.3S)

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • ligase activity
    		•  7.63077869457441 bayes_pls_golite062009
  • glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
    		•  7.42914157198604 bayes_pls_golite062009
  • binding
    		•  1.24905380693412 bayes_pls_golite062009
  • hydrolase activity
    		•  1.16287375250451 bayes_pls_golite062009
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
    		•  1.02750000262516 bayes_pls_golite062009
  • ligase activity, forming carbon-nitrogen bonds
    		•  0.977723384067654 bayes_pls_golite062009
  • catalytic activity
    		•  0.906509857495572 bayes_pls_golite062009
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
    		•  0.461750895886233 bayes_pls_golite062009
  • protein binding
    		•  0.276132955069873 bayes_pls_golite062009
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
    		•  0.0166505316914077 bayes_pls_golite062009
    2
    Term Confidence Notes
  • structural molecule activity
    		•  1.24470630176758 bayes_pls_golite062009
    3 No functions predicted.
    4 No functions predicted.
    5 No functions predicted.
    6
    Term Confidence Notes
  • ligase activity
    		•  6.81588178611521 bayes_pls_golite062009
  • peptidyl-prolyl cis-trans isomerase activity
    		•  1.05326644345172 bayes_pls_golite062009
  • binding
    		•  1.03084911722464 bayes_pls_golite062009
  • cis-trans isomerase activity
    		•  0.985752998974367 bayes_pls_golite062009
  • catalytic activity
    		•  0.748655649755714 bayes_pls_golite062009
  • nucleic acid binding
    		•  0.438324825951616 bayes_pls_golite062009
  • protein binding
    		•  0.130251391659493 bayes_pls_golite062009
    7 No functions predicted.
    8 No functions predicted.
    9 No functions predicted.


    Reference: Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.95

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle