ID   A0A0V1I266_9BILA        Unreviewed;       290 AA.
AC   A0A0V1I266;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 16.
DE   SubName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB-like protein 2 {ECO:0000313|EMBL:KRZ16892.1};
GN   Name=Alkbh2 {ECO:0000313|EMBL:KRZ16892.1};
GN   ORFNames=T11_13067 {ECO:0000313|EMBL:KRZ16892.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ16892.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ16892.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ16892.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
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:KRZ16892.1}.
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DR   EMBL; JYDP01000009; KRZ16892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1I266; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; 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; IPR032852; ALKBH2.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR31573; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 2; 1.
DR   PANTHER; PTHR31573:SF1; DNA OXIDATIVE DEMETHYLASE ALKBH2; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000313|EMBL:KRZ16892.1};
KW   Oxidoreductase {ECO:0000313|EMBL:KRZ16892.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT   DOMAIN          188..290
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   BINDING         158..160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         195
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         197
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         207
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         271
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ   SEQUENCE   290 AA;  33634 MW;  F1A460BD672C5B30 CRC64;
     MSENVKTITH FKNKIIKCIT SNFEIIKIQF YFAGIQTIYI PTIFLENIFF SRSGILPMDK
     FLMRENENED DATLLVNSIS QISADACFIT RKLHSNNDHF DVIYYKQILP KKLADSLLIY
     CEKNIKYFTG NLARVFLFNQ WRPIPRKQMA MGHPNLHYRF SGNVIPAKPW NAVILALRNL
     VSEIAKCDFN FVLINRYKDG HDYIGEHRDN EKELDPSTPI ASVTVGEKRD FIFKHYKLNH
     HPASASEKVC IALEHGSLLL ISADTNRHWS HSLPKRRHCQ NSADKNAHLK
//