ID   A0A229TGR2_9PSEU        Unreviewed;       605 AA.
AC   A0A229TGR2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Carbamoyl transferase {ECO:0000313|EMBL:OXM70442.1};
GN   ORFNames=CF165_05025 {ECO:0000313|EMBL:OXM70442.1};
OS   Amycolatopsis vastitatis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM70442.1, ECO:0000313|Proteomes:UP000215199};
RN   [1] {ECO:0000313|Proteomes:UP000215199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA   Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA   Kalinowski J., Ziemert N.;
RT   "Comparative genome mining reveals phylogenetic distribution patterns of
RT   secondary metabolites in Amycolatopsis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NodU/CmcH family.
CC       {ECO:0000256|ARBA:ARBA00006129}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXM70442.1}.
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DR   EMBL; NMUL01000005; OXM70442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229TGR2; -.
DR   OrthoDB; 9780777at2; -.
DR   Proteomes; UP000215199; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.90.870.20; Carbamoyltransferase, C-terminal domain; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR031730; Carbam_trans_C.
DR   InterPro; IPR038152; Carbam_trans_C_sf.
DR   InterPro; IPR003696; Carbtransf_dom.
DR   PANTHER; PTHR34847; NODULATION PROTEIN U; 1.
DR   PANTHER; PTHR34847:SF1; NODULATION PROTEIN U; 1.
DR   Pfam; PF16861; Carbam_trans_C; 1.
DR   Pfam; PF02543; Carbam_trans_N; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:OXM70442.1}.
FT   DOMAIN          3..378
FT                   /note="Carbamoyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF02543"
FT   DOMAIN          428..597
FT                   /note="Carbamoyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16861"
FT   REGION          451..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  66701 MW;  863FA503E39B652A CRC64;
     MYVLGISRVH DSAAALVRDG EIVAFAEEER FTRVKHDGGF PAEAIKFCLE RGGITLADVD
     HVAYYWQRWK EGIHAAKVFA RYFPGTLEVF RNANGDEGGK SAGMVDTFKT GGGSGSDDYH
     VGGAVLAHLK RSYTLEKDVK EAAGWTGPTK FKTHLVDHHR AHAASGYFIS PWDESAVLTF
     DGIGSDGTAT YLAHGRGDRI VDLRRIKFPH SLGAMYAGVT GYLGFYPTRD EGKIMGLAPF
     GEDTYVDAFK QLIHLNDDGG FELDLSWFGH HRTGKHVMSK KFTDTFGPAR PKTRVTADNP
     VPQHYRDIAY ALQVTLEEAG LHLARWLQRE TGSKRLCVAG GVALNSVMNG RILLETPFED
     FFAQPAAADD GCALGAALEV SVGKYGRPRP RDGYTYTGPD YTDAEMEQAL QDAGVEYTRV
     DDIAAHTAAK VAEGRIVGWV QGRMECGPRA LGNRSLVADP RDPESKTRMN EKVKHREAFR
     PFAPSCLVER AGEYFVSDYP SPVMLLVFDV LPHKRDEVPA ITHVDGTARV QTVSEQDNPL
     YWRMISEFEK LTGVPMVVNT SFNDNNEPIV ASPADAIACY LKTDVDALAL GPFWAEKPRL
     EEDTE
//