ID   A0A2T3Z8E7_9HYPO        Unreviewed;       701 AA.
AC   A0A2T3Z8E7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Mur ligase central domain-containing protein {ECO:0000259|Pfam:PF08245};
GN   ORFNames=M441DRAFT_58521 {ECO:0000313|EMBL:PTB41083.1};
OS   Trichoderma asperellum CBS 433.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB41083.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB41083.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB41083.1,
RC   ECO:0000313|Proteomes:UP000240493};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276}.
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DR   EMBL; KZ679262; PTB41083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3Z8E7; -.
DR   STRING; 1042311.A0A2T3Z8E7; -.
DR   OrthoDB; 7073at2759; -.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000240493; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR001645; Folylpolyglutamate_synth.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   NCBIfam; TIGR01499; folC; 1.
DR   PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR   PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240493}.
FT   DOMAIN          53..206
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   REGION          609..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          516..570
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        612..701
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   701 AA;  77964 MW;  051F61F0E7F658FB CRC64;
     MPSAKEVNRA LARIRAVMPA EKKVASANRN IRLGLERIGH IVPKEQGWLG VHVGGTNGKG
     SVCNLISGLF RLSGISHGMY TSPAMPERHN GVTINGLYVN RRMYEMEVKH IEDKFKRIAS
     GWRFAAGEDP GNLTPFELET AAAFRVFEKM HVNYGVVEVG MGGATDATNI MRQKSVTVIT
     KIDLDHQEYL GNTIEEIAKV KAGIMRPGVP CIVDHTNPSS VMKVLRQHAN SIGTQISPSW
     KGEPLLANLD TERFKLEDYE KQNLLCATLA FRHLFPNYEI DVNKLLAMEP FPSGRKEQVR
     VAGLTGGSRE KPIIVDGAHN LLGAEALASY VQHQVRQGDE AISWVMGLSA SKSKPFAQVI
     STLVQPQDNF AFVEYLPGPN EPPPAPAELG REIGKSIVNH ESQLYDGDSR IASGVQWACE
     KAGEGPVIVT GSLYMIRNFY NLDGVEPKRK TKTRRPGAAQ LWHYIQLSQK RPLTAEEARE
     FKQARRHWYL SPTRNTAFRA VRHGGQPKSS AVPERIRALQ QQVEFHRKQA QGYRSAIESM
     EKDLAQEPTA AAANAESSDL QASLETLKRH HQEHLGAFNS AMFKLRGHTA SPEKKYMSYE
     EVFGRPAKPK VQKFPFPDDE EASTTASRQH EDTTASSESR LESRSDQIAS EEESKLEARS
     SRFGKRKSRH NDNEKEKAAT EAHDLVDKLT KGRVGSEADE P
//