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Database: UniProt
Entry: A0A1G1YLE5_9BACT
LinkDB: A0A1G1YLE5_9BACT
Original site: A0A1G1YLE5_9BACT 
ID   A0A1G1YLE5_9BACT        Unreviewed;       559 AA.
AC   A0A1G1YLE5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   03-MAY-2023, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGY52500.1};
GN   ORFNames=A3J59_01980 {ECO:0000313|EMBL:OGY52500.1};
OS   Candidatus Buchananbacteria bacterium RIFCSPHIGHO2_02_FULL_56_16.
OC   Bacteria; Candidatus Buchananbacteria.
OX   NCBI_TaxID=1797542 {ECO:0000313|EMBL:OGY52500.1, ECO:0000313|Proteomes:UP000177310};
RN   [1] {ECO:0000313|EMBL:OGY52500.1, ECO:0000313|Proteomes:UP000177310}
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   -!- 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:OGY52500.1}.
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DR   EMBL; MHIL01000002; OGY52500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1YLE5; -.
DR   STRING; 1797542.A3J59_01980; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000177310; Unassembled WGS sequence.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 2.30.30.20; Aspartate carbamoyltransferase regulatory subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.140; Aspartate carbamoyltransferase regulatory subunit, N-terminal domain; 1.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 3.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR020542; Asp_carbamoyltrfase_reg_C.
DR   InterPro; IPR036792; Asp_carbatrfase_reg_C_sf.
DR   InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR   PANTHER; PTHR45753:SF6; ASPARTATE CARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   Pfam; PF02748; PyrI_C; 1.
DR   PRINTS; PR00101; ATCASE.
DR   SUPFAM; SSF57825; Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain; 1.
DR   SUPFAM; SSF54893; Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain; 1.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   4: Predicted;
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..166
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          205..350
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   DOMAIN          498..547
FT                   /note="Aspartate carbamoyltransferase regulatory subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02748"
SQ   SEQUENCE   559 AA;  63118 MW;  2C9009580990C29A CRC64;
     MKNFIHVGLL TRDEIVAVII EALRMIPYYC QRQSPPPPPS LRALVKAKQQ RPKTVFWFEE
     LSTRTRHSFE EASELVGFRV GGAITAADSS LGKGEPAGLT LRMLIQQGAD IVVVRSKTEG
     LGMHLAQCIQ RTPADESWVR QDVSIIVAGA GTRDHPSQVL LDLVTIVAQR LGVRKQSQYI
     NLETLFRRQD AEQYLTEQIG AILDNLKIAF VGDLLHSRVV HDWIKLGKLF SIHFTFIAPP
     VFQVEVFCRP EQCAAESELT LALKADVVYT IRTQLERLKE MMPSHEAEAV ARSLMITPEF
     MERYEGFILD AQPIDGHAPT IDPCLWVHPK NLMLMESSIG IPTRMAILRL CEAGRHTEAT
     PVLEEPRIRP VVLQEGDLND HRQKLDSKYH DRDLFFTYVR NGTVIDRLRP GTASLVRRLG
     QKAGLFRGPR RQITIGEGVD SKALPGGKEI IQLHNRWPSF QLAATIGIIA PDVRFSFMRK
     DDEEKEYRRL EFPLPKAVAK LFVCPNPDCV TNCDPEAETF FWVKGQKEEP SDVSLECAYC
     QHCFDTAAII SALDHQSIR
//
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