ID   A0A1X7RW48_ZYMTR        Unreviewed;       486 AA.
AC   A0A1X7RW48;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:SMQ51648.1};
GN   ORFNames=ZT3D7_G6801 {ECO:0000313|EMBL:SMQ51648.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ51648.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ51648.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT853697; SMQ51648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7RW48; -.
DR   STRING; 1276538.A0A1X7RW48; -.
DR   Proteomes; UP000215127; Chromosome 6.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR032854; ALKBH3.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR010666; Znf_GRF.
DR   PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   PANTHER; PTHR31212:SF4; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS51999; ZF_GRF; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215127};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01343}.
FT   DOMAIN          276..390
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          401..446
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  53638 MW;  CD02AEA5BAA650D6 CRC64;
     MSQAASEPQA KRLKSCSTEV EDSGQMGIKH EEISQPPIKA EDVNTATDED EDAESTELKL
     AILSSLHPNK AQDVLMDYLL AYNGDVEKVS EALSSSSAAG SKSKRQHSAL NGYQSSIDTF
     AASSGGPKPV ATATTKSLVQ KGKTLHLYSP ADIERHTPCS LVHNFLPQPL ASALLEELLA
     ESATFLRNEF QMFERTVTTN HTWRLYLDDD SSFESQQSAM QYDGTANPLN VRKSPPEMIK
     VSHLVKDAVN AEVARRTRDY QPASRRLKFQ SPDAWSPNAS IVNCYDGAKE GMGFHADTLT
     QLGTMPIIGS LSMGVTREFR VRRIVAQDDA STTRADEQGQ IAIHLPHNSL LVMHASMQEE
     WKHCIAPTAT ITQHPVAGSK RFNITYRHFP AYMNPQYTPK CRCGVACVLR CVMKSKETRG
     RYMWQCISDR APGGKSCGLF LWAVLDEDGR PEWAEGFKGN ANGTAKIPED KGDKCPVRNK
     DRSLQA
//