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Database: UniProt
Entry: A0A1G2NCE4_9BACT
LinkDB: A0A1G2NCE4_9BACT
Original site: A0A1G2NCE4_9BACT 
ID   A0A1G2NCE4_9BACT        Unreviewed;       593 AA.
AC   A0A1G2NCE4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Carbamoyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2938_00415 {ECO:0000313|EMBL:OHA33757.1};
OS   Candidatus Taylorbacteria bacterium RIFCSPLOWO2_01_FULL_48_100.
OC   Bacteria; Candidatus Taylorbacteria.
OX   NCBI_TaxID=1802322 {ECO:0000313|EMBL:OHA33757.1, ECO:0000313|Proteomes:UP000177797};
RN   [1] {ECO:0000313|EMBL:OHA33757.1, ECO:0000313|Proteomes:UP000177797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHA33757.1}.
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DR   EMBL; MHSA01000025; OHA33757.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2NCE4; -.
DR   Proteomes; UP000177797; 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; 2.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          3..69
FT                   /note="Carbamoyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF02543"
FT   DOMAIN          91..370
FT                   /note="Carbamoyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF02543"
FT   DOMAIN          423..592
FT                   /note="Carbamoyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16861"
SQ   SEQUENCE   593 AA;  66431 MW;  4F989BFF6D9777AB CRC64;
     MNILGLKVTS HDTGAALISG KRVVAIAEER LCRVKHSHNI FPARSISYCL KECGLSPADI
     DIVVIDQIGR TEGVRMREIL ERNTGGAFSR AAIHIINHHD SHAAHAFFCS PFNDAAVLVI
     DGAGEKFMTN LGILGTETET LYSGIGNRVV QIRKAMHIRR KTRFPYTTGI GKFYALLSEE
     YLNFGHYNEG KMMGLAPYGD LRVFHQYPVE HWVKEYNGDI LCNPRFRFVG EETIQKKRES
     FFMRALRAFM RISGLYRLWL RFSPLGEEMV AEPAFFPEIK FEKPQRPRAA PLPEPYYAAV
     ARAGQEVLER AMILWGKKIK EITGAENLCV AGGVGLNIDA NRRFLEEVGF KRIFVQPAAS
     DTGIALGCAL WGAHIIAGLP RFWEMKSASL GRAYSENEIA ASIEKYKDKI SARCSSAITE
     ETARLIVGGK IVGWFQGGSE YGPRALGNRS IIGDARDPEM ANIINKKVKH RESWRPFAAS
     ILSEKQREWF ELEHPSPFML LAAQVVKEKR ARVPSIVHVD GSCRIQSVTR EQNAPYYELL
     SAFEKETGVP LVLNTSFNDA GEPIVETPED ALRCFLNTEM DALAIGDYLI LKK
//
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