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Database: UniProt
Entry: A0A1B8B9J3_FUSPO
LinkDB: A0A1B8B9J3_FUSPO
Original site: A0A1B8B9J3_FUSPO 
ID   A0A1B8B9J3_FUSPO        Unreviewed;       712 AA.
AC   A0A1B8B9J3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Mur ligase central domain-containing protein {ECO:0000259|Pfam:PF08245};
GN   ORFNames=FPOA_03318 {ECO:0000313|EMBL:OBS29382.1};
OS   Fusarium poae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS29382.1, ECO:0000313|Proteomes:UP000091967};
RN   [1] {ECO:0000313|EMBL:OBS29382.1, ECO:0000313|Proteomes:UP000091967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516 {ECO:0000313|EMBL:OBS29382.1,
RC   ECO:0000313|Proteomes:UP000091967};
RA   Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA   Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT   "Living apart together: crosstalk between the core and supernumerary
RT   genomes in a fungal plant pathogen.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276}.
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:OBS29382.1}.
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DR   EMBL; LYXU01000001; OBS29382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8B9J3; -.
DR   STRING; 36050.A0A1B8B9J3; -.
DR   OMA; KQARRHW; -.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000091967; 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; 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.
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:UP000091967}.
FT   DOMAIN          51..207
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   REGION          611..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          563..590
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        620..635
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  81209 MW;  F12C8E904EC101F2 CRC64;
     MSSSQEIKFA LSRINRVLKG KRTAGYRDIR LGLDRIKRVI PENQEWKGIH VAGTNGKGSI
     CTFLGAMFRM AGFGYGSFTS PAIPERHNGV LINGLYVNKR MYEMEMKHVE EKWHRIATGW
     TYQHLDDPKG LSPFEAETAT AFRVFNKMHV PYGIVEVGMG GATDATNAMT DKSVTVISKI
     GLDHQEYLGN TIENIAKVKA GIMRKKVPCI VDHTNSPAVI HVLRQHAREV GTNIILTWKG
     EPLLMTLNNE RWKLESYQVQ NLLCAAMAFR QLFPQHPIDL NKLLSSHPFL PGRLETVRVD
     SPSVETPRDI VVDGAHNMLG IETLFKHVFH RLRKQDPNVP VTWVMGMSAS KDKPILEIID
     KLVEPHDNFA MVEFTQGPND PQPAPAHYGT EHARGLVDKP DDQIYDGPPD ISAALPWACA
     KANGGPVVVT GSLYLIRQLF ELKDIHRTRE PGTRRPGRSQ LYRLSQLGRK NRLTSAERRE
     FKEARRHFEL SPRQSPIFRR VYEQKPKLRT VTMRLVWRKP TRRIQSKAAF HKHQRRGYLQ
     TIKALKKDMQ MANGTENGLI SPADTLLARI EDLEKQAEMH REQYDEAMFK LRGYKAVPHM
     KYMTHREIFG YPKKPKAPTK SPFAAKKKRK TDKPEKKNKK PVMAWKDRSQ SFSEELAAAE
     KQREWSLKEG AKVRAKQEMD AEKADQAERE KDEIFMSKME AGRRDAGGPG DP
//
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