ID I1RR72_GIBZE Unreviewed; 602 AA.
AC I1RR72; A0A098DP24;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Chromosome 4, complete genome {ECO:0000313|EMBL:CEF83119.1};
GN Name=FG06586.1 {ECO:0000313|EnsemblFungi:CEF83119};
GN ORFNames=FGRAMPH1_01T22649 {ECO:0000313|EMBL:CEF83119.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF83119.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|EnsemblFungi:CEF83119, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF83119};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF83119, ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF83119};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3] {ECO:0000313|EMBL:CEF83119.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC {ECO:0000313|EMBL:CEF83119.1};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4] {ECO:0000313|EnsemblFungi:CEF83119}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF83119};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000256|ARBA:ARBA00009375}.
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DR EMBL; HG970335; CEF83119.1; -; Genomic_DNA.
DR RefSeq; XP_011326202.1; XM_011327900.1.
DR AlphaFoldDB; I1RR72; -.
DR SMR; I1RR72; -.
DR STRING; 229533.I1RR72; -.
DR EnsemblFungi; CEF83119; CEF83119; FGRRES_06586.
DR GeneID; 23553712; -.
DR KEGG; fgr:FGSG_06586; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G22649; -.
DR eggNOG; KOG2553; Eukaryota.
DR HOGENOM; CLU_021971_1_0_1; -.
DR InParanoid; I1RR72; -.
DR OrthoDB; 12038at2759; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:InterPro.
DR CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1.
DR Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR041708; PUS1/PUS2-like.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR NCBIfam; TIGR00071; hisT_truA; 1.
DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11142:SF4; PSEUDOURIDYLATE SYNTHASE 1 HOMOLOG; 1.
DR Pfam; PF01416; PseudoU_synth_1; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000070720};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 391..496
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..602
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR641708-1"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR641708-2"
SQ SEQUENCE 602 AA; 68145 MW; D0D9E14C590C2B73 CRC64;
MAADNEGTAA SGTNDSRPSG DSNAAQNNDN GNRRNPRHDH RKPGKGRSEK GRGEWGREKG
DKRKKNDEFK EFKRRKLNKK GESADGESSN NPFSKDEIAA EERRPKRKVA VMIGYAGTGY
KGMQVNGNEK TIEADLFKAF VAAGAISKAN ADDPKKSSLV RCARTDKGVH AAGNVISLKL
IIEDEDIVDK INAELPEQIR IWGLQRTNNA FSCYQTCDSR WYEYLMPSYC LLPPHPETFL
GRKLVELAKE HGVEDELTAR MADVKDFWTE VEEKEIKPIL ARLDPETRAA VLEKVHVTDD
EEIAARKAAA RETDEAEPSE EKPATEAPAE ATEQTTEPEA QQSTVVLESH KPKNRELGPI
DFALRDIKAA YMAAKRRYRV STERLERLQE ALNMYNGTRN FHNYTVQKSF FDASAKRHIK
SFIVNPKPII INDTEWLSLK VHGQSFMMHQ IRKMVGLASL IVRCGTPMER IKESYQNQKM
AIPKAPGLGL LLERPVFHNY NRKATESLGK EGIDFDKYDD KIQAFKDKQI YTRIFSVEEK
DNSFHMFFNQ IDQFKTNHFL WLTAGGMKAA ELTRDTTGEK VQRDVDKELG DEDEEDPEGG
EG
//
