ID K1VMI3_TRIAC Unreviewed; 1422 AA.
AC K1VMI3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=A1Q2_00302 {ECO:0000313|EMBL:EKD05400.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD05400.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD05400.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD05400.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKD05400.1}.
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DR EMBL; AMBO01000092; EKD05400.1; -; Genomic_DNA.
DR STRING; 1220162.K1VMI3; -.
DR eggNOG; ENOG502RXJJ; Eukaryota.
DR HOGENOM; CLU_267875_0_0_1; -.
DR InParanoid; K1VMI3; -.
DR OrthoDB; 2788075at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
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:SF4; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT DOMAIN 1306..1420
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1315
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 1324
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 1402
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ SEQUENCE 1422 AA; 155603 MW; 0E9595E53342E5D7 CRC64;
MASHLPAPSA TGDALRRRAP APPHELAGQD GPGTNGAGGL GRAPNEQAGP NTANVCDTVP
AVDTDACPER LAASVLTGWT PEPGRCQEDG TQDLGRLQPH HHRCAYLGHC EELQRRTVES
EPATTAGTRW TEWAESAHWR RSAHEREKKH RCSHQEAAAQ ARSPSASLAH HGPGVDGAET
AGESSDHRVE VYVAVEVGGV EKEGEGRSTA ASLGERGRQA ADKKVPEEDM TRYRQAATDH
TMGRHPCLDD KYIPPGLEHI LLQAQHPDRT WNPEALQVAG SILQEAVESD PTQAALEHEW
EAHLSPVPHR VDRVFKAQVL SAFLRRKRAD AVKLLEQRRS DISGATKRAV RGSESSQTSC
VTKSQKRRAQ KRLSATVSEL SSPPSTCYAA SPRLTPEGIS PAVQGQTSAE GAVAAARVLT
KRDVGRSRGL KRDRAQTAPC SNDSGLKARQ PAVSAPPVWR IPGNPTSERS FSPQRNHRLP
ATVGTATRQA VHDDEGHSMS QNKKLRRRRK PKRLNSQQGS IDSTAAAKTS PETGVEVATP
QPVLWDGEED TLRYDNKGRP LRLKRPPKRL LEEMEGGADS ATGAKKTKQE ARLPAPTSTD
TPSNFDDDAS TPKLHGSQRQ KKRANLVRKL SAPNEHGIVV EEAENAGSAP LSLSKRRRAP
RKTCNDKKIS KHVLELLGIP VANLPSSTKA GGKSSDKPTP ITKRKKIETY PEPPSATTAE
QCATACPFTP TEVAEATSKT DDLLPVRVSG IRSSVFTSVM RIVSGVCPLQ PSPRLDRLCR
PSVAPPVWAQ TGAVRDAAVL PRLPIGDVHV QGRRLRIPAR RISDTARHLG GRRKGHRFTW
AARTLDGRGR EYVTLSADHT PRDARIATLL LAAQRRCPLI LIAGDGYALL PWDLGCTYAV
LGCRYWVSAA WYEPEACAPG VKAPPGRDYF RRLKVRFDWV QAQGTPWWLE RSGTSWNPPS
DRQQPKTQPS PDCTRFQDST TPVEASIDQS ARVQAVDALA TTVVKGPGGR DIINLPTPPL
TPEVNISEGE LQEALWHGTF TSENSERERV LAGKYASPCL LRESEPGSGS LMDCFARKPG
SVTPPPHLYD EGWTCLNIDC DRYWLLETPT GFWPIPPGMA LRYRPTFLKN VPTPNEAQTV
PYSVVPEPPL TRAQEAGTRS LWRGWVCECG RANCRYRWEV CECRSCGRQT GRLGEADMLL
ASEVCRPRDD VVGEQDEGTV HHVLHDANAV DQIWEGYQRS AIETTEPLFQ RRALKSKALK
GDLLSQQYAI NSGASYKYIV ETLSYSFEES PRIKQSVTRV LGTQVDFNEI LSVTYREGQK
MAWHDDGEPG LGPVVAALSL GASATMSFRP KTRTSSKSQN HMKAVKQERT KDGPGGGSVL
NLTLSHGDVV IMEGRQIQHM YHHRVIPTGL RAAATARVIS EE
//
