ID A0A2X0MF74_9BASI Unreviewed; 1128 AA.
AC A0A2X0MF74;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=BZ3500_MvSof-1268-A1-R1_Chr1-3g01707 protein {ECO:0000313|EMBL:SCZ89985.1};
GN ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR1-3G01707
GN {ECO:0000313|EMBL:SCZ89985.1};
OS Microbotryum saponariae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ89985.1, ECO:0000313|Proteomes:UP000249723};
RN [1] {ECO:0000313|Proteomes:UP000249723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMWP01000014; SCZ89985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0MF74; -.
DR STRING; 289078.A0A2X0MF74; -.
DR Proteomes; UP000249723; 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 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000249723}.
FT DOMAIN 836..974
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT /evidence="ECO:0000259|Pfam:PF13532"
FT REGION 1..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 884
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 892
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ SEQUENCE 1128 AA; 124882 MW; C0179E95C2DD51B5 CRC64;
MSPRQGIAAM RSIIPHHSEP LQDQVPDSDA SSDLTSLDPS SDNDSDSDHS DQQDTATTPW
WWSAYDRRPS LRCRPGREVH SKIILDTPPT SPKQEPLAST FRSSSSSSAA DVDHRRLRKR
PARTIEPAPS RRQSRRIKAH LQTPRVHEGD KCSIWIDIPT VGSPSSPIQT CPPENDTQPS
SEPRPALQFP TPSSPSLCLE RSLYSPSLLA PDSPRPPSES FGTNPELSCD SPTPSSPILT
CPPYDLDGSF DHIEDSETER EEEQAKHKAL LQHHTIEGPA DAGASNVVPP KNNAILNLTS
NSTTPTNPPP PYTPSFAMSP TADTSAPNAL RAILSLAPVH ENDTRKTFSI DKSEWVQPEK
DLKISEEGFP PIWCQSRQEL CEALPYFRAY QGGHYDLGER CIGYLLDGYP APGDRCEAKG
KIIISHGGGC SEGDGNEFRL VRDQTRENIR VRALINCHKT QTPVVLLAGK KYVPQGSTAI
GRTDGRFTDQ FHLCVHSYAH FPWLGTRDVR YCVLGYYMVR DFWVEAEPSK TTSGSGYFTR
FKFLFEWVSS QGQPWFEQFI GPMNGKRSAL SPTAEQIVAS GESGKKWCAA CQRWTPDVFE
QAVACLDERC EAFFKIPIHG LEWSETPRSS LSDLNYRSSL FQPRHTPLSQ QTIHVPLPIY
PPALQDLRTS LVDYSRSSWR GFWCRQCGRL SSRSQWFSLV CSNPSCKETI DLERRIISAD
ELRSRKPRKA PSLSDPTWLS KIEPNEDWEG WVIDLGDDTR ILQLWAKVGS SREGLADELL
EQYQSRDVGE LLKRNMLTSH KVSGGFLTSQ FSFNTGQSYN HVVSVESYPF SDQPNSSNAS
PSRTAPPCVT TARNHLHSAV RSLCPGSSVL QPGGFNEVLS VAYYQGGKMS YHDDGEHGVG
PIVASLSLGA DATMSFRRKI KGASNTTLIS KDVMEGGVRK AKAVAQLQLR HGDVMIMHGG
GVQRNLDHMV EPVNLRFGEY QNEAATARFI HPSNGSTKTG RKKKTTPMSD ALALATSSVI
APPTPTSIPA TFRPISNLTT PVVPQAFEHT LPTFPVDPAS LLQTHIYNLP PLPPSCSPIS
SYDNRPSYVL SGEYHPRSFV LPPQATASSF ESQYGRGSTT PYWPPPRR
//