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Database: UniProt
Entry: A0A1Z9RGN2_9RICK
LinkDB: A0A1Z9RGN2_9RICK
Original site: A0A1Z9RGN2_9RICK 
ID   A0A1Z9RGN2_9RICK        Unreviewed;       736 AA.
AC   A0A1Z9RGN2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Carbamoyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CBE11_03790 {ECO:0000313|EMBL:OUX15683.1};
OS   Rickettsiales bacterium TMED251.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX   NCBI_TaxID=1986870 {ECO:0000313|EMBL:OUX15683.1, ECO:0000313|Proteomes:UP000195709};
RN   [1] {ECO:0000313|EMBL:OUX15683.1, ECO:0000313|Proteomes:UP000195709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED251 {ECO:0000313|EMBL:OUX15683.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-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:OUX15683.1}.
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DR   EMBL; NHKW01000029; OUX15683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z9RGN2; -.
DR   Proteomes; UP000195709; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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;
FT   DOMAIN          7..334
FT                   /note="Carbamoyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF02543"
FT   DOMAIN          387..553
FT                   /note="Carbamoyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16861"
SQ   SEQUENCE   736 AA;  85883 MW;  AA5BAB7B8A21D049 CRC64;
     MSKYKFILGI QSFANMDSGA SIVRADEGGN LLDYVAISEE RLLRKKHPYT FPLHSVDYCM
     KYFGIKNIED IDLLVCDWIR KKQWEFSGKT FNISEFDYLK NIFLFPRNRI RIISHHLAHA
     ASTYYTSGFK KSAILIVDGN GSDLETTSYF EGKNFKINFI KNYKFFGLGA LYNIVSTRIL
     AMGTGGEGKT MGLAPYGKSY SKSGIKFPYF SKGIINDFSN FMQRMPYSDV LNQINSSYRV
     DPINVNYKKV KYKNDVLKPY FAGTAYNLQN TLEKVIVKIS KDLYNITKNE NLCIAGGVGL
     NSVANKKILD KTKFKNIFIF PACSDSGIPF GLAIWGYYNL KELKIKKHKK LVFKNAYLGN
     KYSNKEIKSV LDRYQINYKK SNLNKVAQLI SEKKIVGWFQ GRSEYGPRSL GNRSILADSR
     SNNMKDILNK RVKHREFYRP FAPSILEEDC KKYFELDSPS PYMLLIAKVK KKTIPSVTHV
     DNTARVQTVN KYTNEKFYNL IQEFKKLTDI PCVLNTSFND AGDPIVETPE DALYTLMKCD
     MDYLYIGNFL IERKKIYNEK KMKKIYLDIL KNVEETKKII INKYFKNYSD KEKEKFISHH
     NKKSLTDLLY TAKKGLEKKL KIWQENKNKI IIIGDKKEIE FLNIKFNISK KLKCSSKIYI
     ENNNDDIFII YKDIEKKLKK QNFDEILIAS FQYNFYLEDL CIKNNLNYYK IYNSTDRSLE
     NIFKKKFIEK FEKGKL
//
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