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Database: UniProt
Entry: A0A2A9MPX7_9APIC
LinkDB: A0A2A9MPX7_9APIC
Original site: A0A2A9MPX7_9APIC 
ID   A0A2A9MPX7_9APIC        Unreviewed;       777 AA.
AC   A0A2A9MPX7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Alpha-ketoglutarate-dependent dioxygenase AlkB-like domain-containing protein {ECO:0000259|Pfam:PF13532};
GN   ORFNames=BESB_002730 {ECO:0000313|EMBL:PFH37932.1};
OS   Besnoitia besnoiti.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX   NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH37932.1, ECO:0000313|Proteomes:UP000224006};
RN   [1] {ECO:0000313|EMBL:PFH37932.1, ECO:0000313|Proteomes:UP000224006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH37932.1,
RC   ECO:0000313|Proteomes:UP000224006};
RA   Schares G., Venepally P., Lorenzi H.A.;
RT   "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604574-2};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604574-2};
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:PFH37932.1}.
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DR   EMBL; NWUJ01000001; PFH37932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9MPX7; -.
DR   STRING; 94643.A0A2A9MPX7; -.
DR   VEuPathDB; ToxoDB:BESB_002730; -.
DR   OrthoDB; 47845at2759; -.
DR   Proteomes; UP000224006; Chromosome i.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   InterPro; IPR004574; Alkb.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   PANTHER; PTHR16557; ALKYLATED DNA REPAIR PROTEIN ALKB-RELATED; 1.
DR   PANTHER; PTHR16557:SF2; NUCLEIC ACID DIOXYGENASE ALKBH1; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Iron {ECO:0000256|PIRSR:PIRSR604574-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604574-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224006}.
FT   DOMAIN          489..606
FT                   /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT                   /evidence="ECO:0000259|Pfam:PF13532"
FT   REGION          47..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         546
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         548
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         601
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
SQ   SEQUENCE   777 AA;  82772 MW;  0796AD65D7178D58 CRC64;
     MARCSRVEAV SAASGVDVFK QTETILRQTP WESLLLSQLR RLIAETKDAQ RPTLPPHSSR
     RVGREPCGDR NAAGHEREAT SEETVGNRRR APRGTHANRA REGENSNETS AHADRGESDA
     GWGSPGNDSR AKPQGVMEIG NEGDCKLAVI GGFPLRQQTL EFDSPQIRML LEGSRNLASV
     QPDDHPDANA SRRPSPLSSS ASPRPFVASA PSASHAGSAS PSPDNSSDAV APSGGLLSPS
     SARLFAGLSP AASVASAAPS ESGQVRGKGE GTELESVGAP SSLRPASDLS AEKVKDVHSD
     AGHSPLDDRS APVSIYEVVP GALFLPAYLS VSEQLCLACE CLSVYSMPPH VCNLCNLIHS
     SAEPSVAGAS SSSSHFSSEQ AGREAQACAD GAQGEQTETA EAEGGRDVIC RRREGETPSQ
     EAAACRRFDG NLSRASLSPF LKKQLRWVTL GRHYDWTKRS YDEETNGVGR CPSTRPLLSS
     FPTSAGATPA ISPSFAKLPA ALEKLCDDIL QLCEPYLADA REGTSRRVMD AAILNVYRSG
     DRLRGHKDDA ERAEEPLVSI SIGQPAIFLL GGDSRQVAPK ALVLRSGDVL VLSGVARWAI
     HGVPKLLYYN PVISLPAPRR RKKLRAHAST MQGGMRMSTV GLQTQMYEWR CSEDRQSSEG
     VVCAARNLVA AAGLSGFGEL HADSGMRLLA TCTRRGGRTN SGSSSWLQLL EVYRRQTGDC
     RHDSGDIRSG TGLNGHATST SDQTEPLEKI VGSQTANDVV SWLGELRLNL SCRCDES
//
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