ID F9FW57_FUSOF Unreviewed; 1041 AA.
AC F9FW57;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN ORFNames=FOXB_10638 {ECO:0000313|EMBL:EGU78849.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU78849.1};
RN [1] {ECO:0000313|EMBL:EGU78849.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU78849.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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:EGU78849.1}.
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DR EMBL; AFQF01002733; EGU78849.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FW57; -.
DR STRING; 660025.F9FW57; -.
DR PaxDb; 5507-FOXG_01865P0; -.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR CDD; cd07895; Adenylation_mRNA_capping; 1.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR InterPro; IPR013846; mRNA_cap_enzyme_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR044106; PX_Snx41/Atg20.
DR PANTHER; PTHR46979; SORTING NEXIN-41; 1.
DR PANTHER; PTHR46979:SF2; SORTING NEXIN-41; 1.
DR Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 87..206
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 405..432
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 117923 MW; 4AC05B2A9D99FED4 CRC64;
MWNDEDNNPY GTSFDRRDSQ SSSVNPTSPS TRNYQSFEPP QTPTSGSDDE HGQFGHGGGN
DDGDSAQDTG PKRKPGGYDS RIEQILYENP KLSILITDAG KSLESGGRYI VYTIKTGDLE
VRRRYSEFAS LRDALTRLHP TLIVPPIPEK HTMADYAANP TNAKQDQQII DLRKRMLAVF
LNRCRRMDEI RTDGVWWRFL DPNASWSEVL HSHPVSSIPK SILKAPPLDP ANPTPAHSYL
PIPAASAKLK TVAGTNHDNS SGHIQAGPHA FGRFPPEGHN LGEQELDPYF ISYESSIKEL
EQLLTGPMEK VNRRTLSHLS SLAADLCELG SVYNAFAVSE QAPSLGPAIE RIGQAADLSY
IATEELSGSL GASFAEPMRE HAQFAGVVRS VLKYRVLKRV QQDLTSEELN KKRALLDQLE
QSEAEARRIE NYLSSSQQIS PPPKRSTSLK EPSSHQRRDG GQDDTESIDS DFPGTHGEFS
SHTPSASQGL PERSTSAPSH KKMPSGNSIT NKIFGPIRHA VQGVVDVDPE RTRRDLIGKT
RESIGQLEQA QVVSERDVKE ASASVLKDMK RFQKDKEDDL RRYMLAYAQS QIEWAKKNLL
TMNYWSRQEG QKSDTEDRSS CLPKTWEHSM RFSSLSQQQS NLPQRILTTV IAMAQQDGPI
ASIAEPGIKA QGQLLHEMRK EVANLLNRSA TGFPGAQPVS FARQHLEELA QHDYYVVEKS
DGIRYLLYST TDENGNEAHY LIDRKNDFWF ITNRSLHFPL ENSPEAFHTN TLIDGELVWD
TGSDGKRVPM FLVFDCLVLD GALLMERTLD KRLAYFDQRF YRPYKKLYQE YPQELEFQPF
YVEMKKPQFA YAIDMMFRDI LPKLKHGNDG LIFTCRTTAY KHGTDNHILK WKPPEENTVD
CRLSLDFVEV EPNDEERREG ITEPFIDYDS VPKADLYVYA GGSGPEKYEY FNSVFISEEE
WETLKSLNDP LNWRVVECNI DEQGRWRIVR FRDDKNEANH ISTTKSVLQS IEDRVSEKDL
YRAAGEIKNA WKARASRGPA R
//
