ID A0A0G2I3Z4_9EURO Unreviewed; 465 AA.
AC A0A0G2I3Z4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKZ64935.1};
GN ORFNames=EMCG_09169 {ECO:0000313|EMBL:KKZ64935.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ64935.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ64935.1}.
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DR EMBL; LCZI01000725; KKZ64935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2I3Z4; -.
DR VEuPathDB; FungiDB:EMCG_09169; -.
DR Proteomes; UP000034164; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR CDD; cd14279; CUE; 1.
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; IPR032854; ALKBH3.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR PANTHER; PTHR31212:SF4; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 253..391
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 402..447
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 52416 MW; 95164F87EACE8E99 CRC64;
MDRFLSRKRP RDPSPPGLRD NTTPLSAKEA DEESTDIKLA ILSSLFQGVQ QDILLDTLIA
SDGSVAKACS TLSSQTPRLS KKKHTISSGL GIQSSLSLFG VTAENSSTSK PGPKPLTKRG
RTLHLFSAED ISKYTPCTII HNFLPTNEAN DLLRELLEEA KTFHRQTFQL FENTVQSPHS
AGFYVASAEE LHQQKHEYSY NGTYRTDVRQ LTPELRRVST KVQQAVNDEI QKRIELHYPG
GKKLKYQSSR TWIPNAAFVN CYDGPSESVG YHSDELTYLG PRPVIGSLSL GVAREFRVRK
IVPPDDPQDP NDNNNNNNNE ESSEGPATSK SKTTRADIQG QISIHLPHNS LLIMHAETQE
EYKHSISPAQ TISPHPIAGN KRINITYRWY RESLHPRHTP RCRCGMPCVL RCVQRKKETR
GRYMWMCYAG YAVGKTSCSF FQWAEFDEDG EPIWPEDRTG KEPGK
//