ID A0A2T5LZ54_9EURO Unreviewed; 740 AA.
AC A0A2T5LZ54;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=P175DRAFT_0508527 {ECO:0000313|EMBL:PTU21567.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU21567.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU21567.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU21567.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:PTU21567.1}.
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DR EMBL; MSFN02000003; PTU21567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5LZ54; -.
DR VEuPathDB; FungiDB:P175DRAFT_0508527; -.
DR OrthoDB; 1380829at2759; -.
DR Proteomes; UP000244073; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1.
DR PANTHER; PTHR40088:SF1; PECTATE LYASE PEL9; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 174..290
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 740 AA; 80978 MW; 1066155F9297CB81 CRC64;
MTVVSESFTT IPILDFSLST APETKASFLA DLRNALVNVG FFYLTNAPVA PHVTQELVAK
TKEIFDLPLE KKREIEMVHS KHFLGYSRLG AEITARKPDY REQFDFATEL PAPPPEAPLY
RNIRGPNQWP DEAVIPGFRR SVEAYLAELS PVADQFQGLI AEALHLHPAA LKPFFEVPLQ
QKMKLIKYPP PSTEAEAQGV GAHKDSEFLT FLLQVPPHRG LEVQNKSGDW ISAPPIEGSL
VVNIGRALEA ITGGVCTATT HRVSLEPSNY VDAQGRPLGP RFSIPVFQGM SLDLSAEDIS
LDIPEHIQDL ILDKRVRSDA EATFNSMFRS RVGEGTLIHR VISHQDVGRR WYPEVLARAL
GEYDKQNPLS LQYITKKMRL FYVLALVLPA VFGKDIYVSP TGSDNAAGTI DAPLKSIQLA
VDRATGGTTI YLRGGRYSPT ANIQITKSGT SPAPYILRAY GGESVMIDGE GLPGTPAGSD
ASLPNKERGI LHIEKADYWE FYDLELINGP YGVYAQDSSN NHYERIVTRD NYETGFHLQG
DSSNNLVLYL DSYANRDPRK NGESADGEFK SGVTIEDTIS WGNGFNRWNF APFKGDGNGF
KLGGGNDGDI GPANHRVINS IAFGNSKDGF TDNSQPGKFE LLRNTAWNNG AMGFRFHTAA
ATLTGNIAAS NGEAPTSLSK AQISRGNSWN DGKTWNDASF VSVDTRLVQG ARDIHGKIKP
SDFLLPTSGG TIGATTDWND
//
