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Protein Overview: CPA2

General Information:
Name(s) found: CPA2 / YJR109C [SGD]
Description(s) found:
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  • pir||SYBYCP carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) arginine-specific large chain - yeast (Saccharomyces cerevisiae) [NCBI NR]
  • gi|6322569|ref|NP_012643.1| Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor; Cpa2p [Saccharomyces cerevisiae] [NCBI NR]
  • gi|171310|gb|AAA66902.1| carbamyl phosphate synthetase large subunit [NCBI NR]
  • gi|115631|sp|P03965.1|CARB_YEAST RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain; AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, ammonia chain [NCBI NR]
  • gi|1015822|emb|CAA89639.1| CPA2 [Saccharomyces cerevisiae] [NCBI NR]
  • Carbamoyl-phosphate synthase arginine-specific large chain OS=Saccharomyces cerevisiae GN=CPA2 PE=1 SV=1 [Swiss-Prot]
  • CPA2 Arginine-specific carbamoylphosphate synthase, large chain [mips]
  • Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor [SGD]
  • CPA2, Chr X from 629278-632634, reverse complement [yeast_orfs2]
  • Chr X from 629278-632634, reverse complement [yeastorf3.fasta]
  • Chr X from 629279-632635, reverse complement [yeastorf4.fasta]
  • Chr X from 632636-629280, reverse complement [yeastorf5.fasta]
  • (P03965) Carbamoyl-phosphate synthase, arginine-specific, large chain (EC 6.3.5.5) (Arginine-specific carbamoyl-phosphate synthetase, ammonia chain) [4932.FASTACCERV.txt]
  • CPA2 SGDID:S0003870, Chr X from 632856-629500, reverse complement, Verified ORF [yeastflysequest.fasta]
  • Cpa2p [Saccharomyces cerevisiae]gi|1015822|emb|CAA89639.1| CPA2 [Saccharomyces cerevisiae]gi|115631|sp|P03965|CARB_YEAST Carbamoyl-phosphate synthase, arginine-specific, large chain (Arginine-specific carbamoyl-phosphate synthetase, ammonia chain)gi|68 [nrdb_11152004_Chlamydomonas]
  • CPA2 SGDID:S000003870, Chr X from 632856-629500, reverse complement, Verified ORF, "Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor" [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
  • CPA2 SGDID:S000003870, Chr X from 632935-629579, reverse complement, Verified ORF, "Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor" [yeast-contam.fasta]
  • CPA2 SGDID:S000003870, Chr X from 632932-629576, reverse complement, Verified ORF, "Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor" [SGD_S-cerevisiae_na_08-19-2008_con_reversed.fasta]
  • CPA2 SGDID:S000003870, Chr X from 632931-629575, reverse complement, Verified ORF, "Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor" [yeast-200209-contam.fasta]
  • CPA2 [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • Carbamoyl-phosphate synthase arginine-specific large chain (Arginine-specific carbamoyl-phosphate synthetase, ammonia chain) [nr-271106-contam.fasta]
  • carbamyl phosphate synthetase large subunit [nr-271106-contam.fasta]
  • Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor; Cpa2p [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • [chemostatdb.fasta]
  • Carbamoyl-phosphate synthase arginine-specific large chain OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=CPA2 PE=1 SV=1 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
  • CPA2 SGDID:S000003870, Chr X from 632941-629585, Genome Release 64-1-1, reverse complement, Verified ORF, "Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor" [yeast-030211-contam.fasta]
  • CPA2 SGDID:S000003870, Chr X from 632941-629585, Genome Release 64-2-1, reverse complement, Verified ORF, "Large subunit of carbamoyl phosphate synthetase; carbamoyl phosphate synthetase catalyzes a step in the synthesis of citrulline, an arginine precursor" [20141208_orf_trans.fasta]
  • TR6569|c0_g1_i1|g.4768 ORF TR6569|c0_g1_i1|g.4768 TR6569|c0_g1_i1|m.4768 type:complete len:1119 (+) TR6569|c0_g1_i1:238-3594(+) [DBVPG6044_S_cerevisiae-Sep2015-contam.fasta]
  • YJR109C SGDID:S000003870, Chr X from 632941-629585, Genome Release 64-1-1, reverse complement, Verified ORF, "Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
  • asmbl_5889|g.4541 ORF asmbl_5889|g.4541 asmbl_5889|m.4541 type:complete len:1119 (+) asmbl_5889:239-3595(+) [DBVPG6044_Trinity_v2_2_0_PASA_6May2016-contam.fasta]
  • ID=asmbl_5883|g.3684 ORF ID=asmbl_5883|g.3684 ID=asmbl_5883|m.3684 type:complete len:1119 (+) ID=asmbl_5883:239-3595(+) [DBVPG6044_quiverGenomes_Trinity_v2_2_0_PASA_2June2016-contam.fasta]
    • Organism: Saccharomyces cerevisiae
    Length: 1118 amino acids

    Gene Ontology:
    Cellular Component: carbamoyl-phosphate synthase complex [ISSLink to PubMed article]
    Biological Process: arginine biosynthetic process [TASLink to PubMed article]
    Molecular Function: carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [IMPLink to PubMed article][ISSLink to PubMed article]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MTSIYTSTEP TNSAFTTEDY KPQLVEGVNS VLVIGSGGLS IGQAGEFDYS GSQAIKALKE  60
   61 DNKFTILVNP NIATNQTSHS LADKIYYLPV TPEYITYIIE LERPDAILLT FGGQTGLNCG 120
  121 VALDESGVLA KYNVKVLGTP IKTLITSEDR DLFASALKDI NIPIAESFAC ETVDEALEAA 180
  181 ERVKYPVIVR SAYALGGLGS GFANNASEMK ELAAQSLSLA PQILVEKSLK GWKEVEYEVV 240
  241 RDRVGNCITV CNMENFDPLG VHTGDSMVFA PSQTLSDEEF HMLRSAAIKI IRHLGVIGEC 300
  301 NVQYALQPDG LDYRVIEVNA RLSRSSALAS KATGYPLAYT AAKIGLGYTL PELPNPITKT 360
  361 TVANFEPSLD YIVAKIPKWD LSKFQYVDRS IGSSMKSVGE VMAIGRNYEE AFQKALRQVD 420
  421 PSLLGFQGST EFGDQLDEAL RTPTDRRVLA IGQALIHENY TVERVNELSK IDKWFLYKCM 480
  481 NIVNIYKELE SVKSLSDLSK DLLQRAKKLG FSDKQIAVTI NKHASTNINE LEIRSLRKTL 540
  541 GIIPFVKRID TLAAEFPAQT NYLYTTYNAT KNDVEFNENG MLVLGSGVYR IGSSVEFDWC 600
  601 AVNTAKTLRD QGKKTIMINY NPETVSTDFD EVDRLYFEEL SYERVMDIYE LEQSEGCIIS 660
  661 VGGQLPQNIA LKLYDNGCNI MGTNPNDIDR AENRHKFSSI LDSIDVDQPE WSELTSVEEA 720
  721 KLFASKVNYP VLIRPSYVLS GAAMSVVNNE EELKAKLTLA SDVSPDHPVV MSKFIEGAQE 780
  781 IDVDAVAYNG NVLVHAISEH VENAGVHSGD ASLVLPPQHL SDDVKIALKD IADKVAKAWK 840
  841 ITGPFNMQII KDGEHTLKVI ECNIRASRSF PFVSKVLGVN FIEIAVKAFL GGDIVPKPVD 900
  901 LMLNKKYDYV ATKVPQFSFT RLAGADPFLG VEMASTGEVA SFGRDLIESY WTAIQSTMNF 960
  961 HVPLPPSGIL FGGDTSREYL GQVASIVATI GYRIYTTNET TKTYLQEHIK EKNAKVSLIK1020
 1021 FPKNDKRKLR ELFQEYDIKA VFNLASKRAE STDDVDYIMR RNAIDFAIPL FNEPQTALLF1080
 1081 AKCLKAKIAE KIKILESHDV IVPPEVRSWD EFIGFKAY

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Riffle et al. (2010) (Unpublished Data) CPA1 CPA2
    View Details (MIPS) Mewes HW, et al. (2004) CPA1 CPA2
    View Details Krogan NJ, et al. (2006) CPA1 CPA2 URA2
    View Details Gavin AC, et al. (2002) ACC1 ARO1 CCT8 CLU1 CPA2 FDH1 GCN20 GFA1 GUS1 HSC82 IDH2 ILV1 KAP123 LYS12 MKT1 MRPL3 PFK1 PSA1 RAD51 RAD52 RFA1 RPA135 RPB2 RPN10 RPN11 RPN12 RPN8 RPN9 RPT3 RPT5 RPT6 RVB2 SAM1 SEC27 SMC3 TCB1 TIF1, TIF2 TSA1 TUB3 URA7 VAS1 YHB1 YOL098C
    View Details Ho Y, et al. (2002) AAC1 AAC3 ACC1 ACH1 ADE5,7 ADR1 AHA1 ARC1 ARO1 ARP2 ATG11 ATG12 ATG17 ATP3 CAR2 CCT3 CDC15 COP1 CPA2 CPR6 DBP8 DEF1 FET4 FOL2 GAL7 GCD11 GFA1 GUS1 HEF3 IDH1 IPP1 KGD1 LSC1 LST8 LYS12 OYE2 PFK1 PGM2 PHO86 POR1 PPX1 PRB1 PTC7 REP1 REX2 RFC2 RNR1 RNR2 RPN1 RPN10 RPN11 RPN12 RPN3 RPN5 RPN6 RPN7 RPT1 RPT3 RRP3 SEC18 SEC26 SIP1 SLC1 SRP1 STI1 TCB1 THI22 TIF1, TIF2 TYR1 YBT1 YDL086W YHR020W YHR033W YKU80 YML020W YNL208W

    Mass Spectrometry Data

    The following runs contain data for this protein:

      BAIT COMMENTS PUBLICATION
    View Run MLP2 #24 Asynchronous Prep3-TiO2 Phosphopeptide enrichment Keck JM, et al. (2011)
    View Run MLP2 #32 Asynchronous Prep-No Phosphopeptide enrichment Keck JM, et al. (2011)
    View Run MLP2 #31 Asynchronous Prep (Protease cleavage) Keck JM, et al. (2011)

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    SHOWING SINGLE HITS. [ Hide Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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      PROTEIN(S) PUBLICATION
    View Data CPA2 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..682] PSI-BLAST 11000.0 Carbamoyl phosphate synthetase, large subunit connection domain; Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain; Carbamoyl phosphate synthetase (CPS), large subunit PreATP-grasp domains; Carbamoyl phosphate synthetase (CPS), large subunit ATP-binding domains
    2 View Details [683..961]
    [1076..1118]    		 PSI-BLAST 11000.0 Carbamoyl phosphate synthetase, large subunit connection domain; Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain; Carbamoyl phosphate synthetase (CPS), large subunit PreATP-grasp domains; Carbamoyl phosphate synthetase (CPS), large subunit ATP-binding domains
    3 View Details [962..1075] PSI-BLAST 11000.0 Carbamoyl phosphate synthetase, large subunit connection domain; Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain; Carbamoyl phosphate synthetase (CPS), large subunit PreATP-grasp domains; Carbamoyl phosphate synthetase (CPS), large subunit ATP-binding domains

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • carbamoyl-phosphate synthase activity
    		•  10.3961907577933 bayes_pls_golite062009
  • carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
    		•  10.3817460390594 bayes_pls_golite062009
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
    		•  7.55690629692775 bayes_pls_golite062009
  • ligase activity, forming carbon-nitrogen bonds
    		•  6.95559501787172 bayes_pls_golite062009
  • ligase activity
    		•  1.91091941710895 bayes_pls_golite062009
  • phosphoribosylaminoimidazole carboxylase activity
    		•  1.57708889650281 bayes_pls_golite062009
  • catalytic activity
    		•  1.08688404807699 bayes_pls_golite062009
  • phosphoribosylamine-glycine ligase activity
    		•  1.04915286326924 bayes_pls_golite062009
  • carbon-oxygen lyase activity, acting on phosphates
    		•  0.964679554894316 bayes_pls_golite062009
  • phosphoribosylaminoimidazolecarboxamide formyltransferase activity
    		•  0.898425265043358 bayes_pls_golite062009
  • acid-amino acid ligase activity
    		•  0.730894973410499 bayes_pls_golite062009
  • carbon-oxygen lyase activity
    		•  0.482425669839603 bayes_pls_golite062009
  • lyase activity
    		•  0.432948879967458 bayes_pls_golite062009
  • ligase activity, forming carbon-sulfur bonds
    		•  0.37779550230552 bayes_pls_golite062009
  • hydroxymethyl-, formyl- and related transferase activity
    		•  0.2431211195117 bayes_pls_golite062009
  • glutathione synthase activity
    		•  0.0685848191991462 bayes_pls_golite062009
  • biotin carboxylase activity
    		•  0.0172732430077291 bayes_pls_golite062009
    2 No functions predicted.
    3 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: 0.97

    Source: Reynolds et al. (2008)

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