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
//