ID   A0A1Y1ZP16_9FUNG        Unreviewed;       877 AA.
AC   A0A1Y1ZP16;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Glutathione synthetase ATP-binding domain-like protein {ECO:0000313|EMBL:ORY11767.1};
GN   ORFNames=LY90DRAFT_708765 {ECO:0000313|EMBL:ORY11767.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY11767.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY11767.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY11767.1,
RC   ECO:0000313|Proteomes:UP000193920};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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:ORY11767.1}.
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DR   EMBL; MCOG01000378; ORY11767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1ZP16; -.
DR   STRING; 1754190.A0A1Y1ZP16; -.
DR   OrthoDB; 5474086at2759; -.
DR   Proteomes; UP000193920; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:ORY11767.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:ORY11767.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193920}.
FT   DOMAIN          18..326
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          797..868
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   877 AA;  100659 MW;  27BBE81E83B31DF2 CRC64;
     MSETKIISLN SKELADISQV GGKGYSLIKL SSLNLNVPPG IVLTVGFFED WIKKIKNSDL
     YKEFILQLSQ NNNECQIILN KIKDWSLNNL VLSSSDKQDI EDNLKKLFPD DYNKILYAVR
     SSSPEEDLAG ASFAGNYETY LGTQFDLLEE FILKSFISCI DYRVFKYKLE KGFTASDIKI
     AIVIMKQVNC DVSGVGFSIN PLNNDYDEAV ITSNFGLGES VVGGIITPDE YIVNKISKKV
     ITEKLGSKDK IVKLNEDNGT SVLEQNSENQ KKSSLSKEQI IQIVDKIIVI ENSYNVPIDI
     EFGIENDILY ILQARPITTY NKLPEEFLTK PNEQRQLYFD VTVAKLIPGI ENIDNLKESA
     FDGIGGKLLL NLSNVMTKFE IETITNYTSN INNLISETLL NHGSEYKNKT ECKALKINKF
     NIIRKVPIIR VIFAKYFAKS SKSNFENQMS RFITESEEYI QKNIDSNVPI FTILEHLINN
     LVTYFRSYAI PVLANGIFFG YMKLKNLFEP YLKDNSELRQ DFNNLIKCFP FVTILMGLDT
     YKLSTYLDKN QYKNKTQDEF YQDYLDKKFP KEFYIEFETF MKKYGFRGEG EIDIVNKRYS
     ENPKTIINQV FSALLEYDES NNPQKDFDDT NSNRPEIFRK LYKFASKKGF ASEFEKAYFF
     TVNFFQYRES PKYYIVFVIG SVRKLILKRA EVLLQRNLID DIDDIFKLKI KSLDHILENV
     DVLTKEKVGN KIHEDNKCRE IITTWKRQPI MFDSRGRIFS HERKEASKKN QLIGDSVSYG
     KVRGKAKVLK TVNEKVFNPG EILVTKATDP GWTPLIINCG GIILEVGGML QHGALVSREF
     NKPCVVGIEN ITDIIKDGEE IEVDAIEGII TLLDREE
//