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Database: UniProt
Entry: D0A8V8_TRYB9
LinkDB: D0A8V8_TRYB9
Original site: D0A8V8_TRYB9 
ID   D0A8V8_TRYB9            Unreviewed;       650 AA.
AC   D0A8V8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=TbgDal_XI12280 {ECO:0000313|EMBL:CBH18109.1};
OS   Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH18109.1, ECO:0000313|Proteomes:UP000002316};
RN   [1] {ECO:0000313|Proteomes:UP000002316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX   PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA   Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA   Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA   Barry J.D., Berriman M., Hertz-Fowler C.;
RT   "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT   chronic human african trypanosomiasis.";
RL   PLoS Negl. Trop. Dis. 4:E658-E658(2010).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the alkB family.
CC       {ECO:0000256|ARBA:ARBA00007879}.
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DR   EMBL; FN554974; CBH18109.1; -; Genomic_DNA.
DR   RefSeq; XP_011780373.1; XM_011782071.1.
DR   AlphaFoldDB; D0A8V8; -.
DR   GeneID; 23866385; -.
DR   KEGG; tbg:TbgDal_XI12280; -.
DR   VEuPathDB; TriTrypDB:Tbg972.11.12280; -.
DR   OrthoDB; 169579at2759; -.
DR   Proteomes; UP000002316; Chromosome 11.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR032862; ALKBH6.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR46030; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 6; 1.
DR   PANTHER; PTHR46030:SF1; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 6; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          360..500
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          20..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          574..643
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   650 AA;  71719 MW;  B88758972035ACD2 CRC64;
     MRRCLILPVL TTASKSSFAS CRHSSSGDGR NGGVGSSASS SATTIRESMK SAGFNFNTPN
     FCLEGATESD VADTAGELIT SPVTSLNFVR DMYGPWLVLT EEIQGELFID HDKMVYLRPA
     NGLGFGVGRI DTGEPCSSGT AFLMSLEWYT YPATTSMPPN NACKTEVTGV VKHVHSSSMD
     YSTFTLVASW RSSSGTSGKF NAAKLSPWDP VGGVKRWTPN GDLMQVFHQV FPTPLRLTSH
     IKRATAARQV GSRSGGLGEG ELGSSPHHLS LEQYRVGELP DLYYIPNYIS EEEEQEMMEA
     VRSTPRELKT QLTKRTVQEW GCSMCETCNK SFVSDRNMPP WVEACTDMQV YDGIFTPSVF
     PNSVRVHEYH PHEGIAPHCD GPIYVPRVSV LSLGTPCVMF FYSRREPYSE PMEHYNDTFR
     FKEGIAKESP IQSVVLEPRS LLVFAGDVFH YYPHGTCDRK IVPLTTEVAG RVVNRHLLQD
     PDIKEVHKGF RVSVTTRNLL PRCNHQPERA EYGMKRAWFI YNQLPVPQQL FTSPPLAPDA
     KTGNAGGEEK AKPFDASAGK SAAGSAHPGT DENMANIEKK LDQLLKQQNA LSQQLDEVRQ
     LIAGDAGFRH EVSTVLGHLT STVLQIESKL EDLEDNRARE MGETGGQTTA
//
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