ID   A0A0N8GLN4_9CHLR        Unreviewed;      1185 AA.
AC   A0A0N8GLN4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=ACT domain-containing protein {ECO:0000259|PROSITE:PS51671};
GN   ORFNames=ADM99_05700 {ECO:0000313|EMBL:KPL72986.1};
OS   Leptolinea tardivitalis.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Leptolinea.
OX   NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL72986.1, ECO:0000313|Proteomes:UP000050430};
RN   [1] {ECO:0000313|EMBL:KPL72986.1, ECO:0000313|Proteomes:UP000050430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL72986.1,
RC   ECO:0000313|Proteomes:UP000050430};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KPL72986.1}.
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DR   EMBL; LGCK01000007; KPL72986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8GLN4; -.
DR   STRING; 229920.ADM99_05700; -.
DR   PATRIC; fig|229920.5.peg.1113; -.
DR   Proteomes; UP000050430; Unassembled WGS sequence.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
DR   PROSITE; PS51671; ACT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050430};
KW   Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT   DOMAIN          656..735
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          545..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1185 AA;  134707 MW;  96A5D978C41D700C CRC64;
     METKNPNFKQ ITPIFLSVLG TAADPDRSLV NFERFIENYG VDLIPLLEEN TRVIEILITL
     FSASHFLTEI LLRNPRSVDL LLDRQKLTQR KTIEQIQTEA EAAVRTASTD IEKKDALRRY
     QQNELLRIGA SDFLDLYDLS AVVSQISRTA IALTRTCLNL ACTQTGISST GFSVLAMGKL
     GGRELNYSSD IDLVFIVRDD PSRFIPLAQK LIDNLASTTS NGFLYRIDLR LRPWGNDGPL
     IPTLAGFCQY LEKNARLWEK QALLKLRPIA GDLPLGEEFR EMSYPFIVNL PPQQVKTEVF
     TMKQRTEEIL REKGRDWGEV KLGVGSIRDI EFVLQYLQLV NLREYPQIRT RASLKAISYL
     RSAGLLSSAD ARILHDGYIF LRTIEHYLQM MDYRQTYSLP SDSMAIRILA RRLGFEDGDH
     FIERYEEHCQ AIRAIFMKYI GVPQKAPPLT PEVHQHISRM DTSYIKAFTP EEIENHARLA
     RELSPSKPVI VDTSFSSDET YRVTVVAYDY PGELSVICGL LFVHGMNIID GYAFTYEPAE
     KAAGQSEKGL LSPGTTTNGT KNTAIKKNHE ETRQKIVDVL TVRPANHKPV DQSVWDDYRD
     DLHRMLDMFQ SGLRREARGS LAKRVGAAFQ SIPGTVAPLL PIDIEIINEP SSRYTILRID
     APDTFGFLYE FTNALAFTRT NIARMVVRSI GNRAQDVFYV TDENGNRIED PGKQRELRAA
     IVLIKHFTHL LPNSPNPEIA LLHFREFLGH LFQRPNWTDE IASLEQSDVL KALAHILGVS
     EFLWDDFLRM QYANLFPVVK DVGALAAAKP RMELRNEVTL AIETKIVGGI GYPDWRAAIN
     AYKDRELFRI DMRHILELTS EFWDFAAELT ELAEVIISSV VNLCLEELTF RYGKPTGEDG
     SAGKYSVVAL GKCGGRELGF ASDIELMFIY DGTGYTDGPE KIEISEFYEK LVRSVISSIH
     ARQEGIFQID LRLRPYGNAG SMAVSLEAFR RYFSPDGPAW AYERQALVKL RPIHGDKQLG
     DEICRLRDDF IYSNGIFDVT AMRAMRERQV RHLVIGGTFN AKYSPGGLVD VEYLIQGLQI
     IYGKDIPALR VTNIREAMLC LYENKILSDI DYAKLRKAHT FLRWLIDSLR VVRGNAKDIT
     VPPFGSEEFS FLARRLRYGN DIDRLRDDLL VYQTDVQEIN TRLLG
//