ID   CARA_TRIVE     STANDARD;      PRT;   453 AA.
AC   P87183;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   07-MAR-2006, entry version 45.
DE   Carbamoyl-phosphate synthase arginine-specific small chain,
DE   mitochondrial precursor (EC 6.3.5.5) (Arginine-specific carbamoyl-
DE   phosphate synthetase, glutamine chain) (CPS-A).
GN   Name=arg2;
OS   Trichoderma virens.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea.
OX   NCBI_TaxID=29875;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98162097; PubMed=9501476; DOI=10.1006/fgbi.1997.1025;
RA   Baek J.M., Kenerley C.M.;
RT   "The arg2 gene of Trichoderma virens: cloning and development of a
RT   homologous transformation system.";
RL   Fungal Genet. Biol. 23:34-44(1998).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + CO(2) + H(2)O = 2 ADP +
CC       phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from HCO(3)(-): single step.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- MISCELLANEOUS: In eukaryotes this enzyme is synthesized by two
CC       pathway-specific (arginine and pyrimidine) under separate control.
CC   -!- SIMILARITY: Belongs to the carA family.
CC   -!- SIMILARITY: Contains 1 type-1 glutamine amidotransferase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF001029; AAB58299.1; -; Genomic_DNA.
DR   HSSP; P00907; 1M6V.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR006274; CarA_synth_small.
DR   InterPro; IPR001317; CP_synthGATase.
DR   InterPro; IPR002474; CP_synthsmall.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR000991; GATase_1.
DR   InterPro; IPR012998; GATase_1_AS.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS00442; GATASE_TYPE_I; 1.
KW   Amino-acid biosynthesis; Arginine biosynthesis; Ligase; Mitochondrion;
KW   Transit peptide.
FT   CHAIN         ?    453       Carbamoyl-phosphate synthase arginine-
FT                                specific small chain.
FT                                /FTId=PRO_0000004223.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   ACT_SITE    309    309       GATase (By similarity).
SQ   SEQUENCE   453 AA;  49434 MW;  39B644DE774F0CAA CRC64;
     MFSKLAANFA QRAAGSAAGT TRRVAFQTRF VSSQTLANGS KGRAIPFQKP GSVPATFTIR
     DGPVFRGKAF GANANISGEA VFTTSLVGYP ESMTDPSYRG QILVFTQPLI GNYGVPSNER
     DEYNLLKYFE SPHIQCAGVV VSDVALNYSH WTAVESLSEW CAREASPPSP ASDTRAIVTH
     LREQGSSLAR ISIGDEYDAD EDESFVDPGQ INLVKRVSTK APFVIESPGA DLHVALIDCG
     VKENILRQLV SRGASLTVFP YNYPIHKVAD HFDGVFISNG PGDPIHCQET VYNLARLMET
     SSIPIMGICL GHQLLAMAVG AKTIKMKYGN RAHNIPALDL TTGQCHITSQ NHGYAVDAST
     LPNDFKEYFV NLNDGSNEGM MHRTRPIFST QFHPEAKGGP MDSSYLFEKY LENVRAAKSA
     QRVYKDNRPS QYVLDVLSKE RVGVEPVPLV GFA
//