ID C1G1J9_PARBD Unreviewed; 475 AA.
AC C1G1J9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PADG_00739 {ECO:0000313|EMBL:EEH44450.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH44450.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH44450.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH44450.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275957; EEH44450.1; -; Genomic_DNA.
DR RefSeq; XP_010756475.1; XM_010758173.1.
DR AlphaFoldDB; C1G1J9; -.
DR STRING; 502780.C1G1J9; -.
DR GeneID; 22580529; -.
DR KEGG; pbn:PADG_00739; -.
DR VEuPathDB; FungiDB:PADG_00739; -.
DR eggNOG; ENOG502QUQ4; Eukaryota.
DR HOGENOM; CLU_026011_0_0_1; -.
DR InParanoid; C1G1J9; -.
DR OMA; IDPHPLA; -.
DR OrthoDB; 325143at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; 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; IPR003892; CUE.
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; PS51140; CUE; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 38..81
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 257..388
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 399..444
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 305..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 53213 MW; 7E24BE3A2A6C5F3D CRC64;
MRMTLLEIRP AMDRFLPRKR PREQSPPNEE ILANEEESTD VKLAVLASLF PDLQQDILLD
TLIASDGSVT TACSTLSSIA PPGNNKKRAT NGALRIQSSL SAFGVKAINS STSIISPKSV
TKRGRTLHLF DPEDISKCTS CTIIHNFLPA NEANDLLREL LEEAKTFQRQ TFQLFENTVQ
SPHSAGFYVA SAEEQEQQRH DYSYNGTYRT DVRQLTPELR RVSVKVQEAV NNEIQKRIKY
YYPGGKKLKY QSPRTWVPNA AFVNCYDGPS ESVGYHSDEL TYLGPRPVIG SLSLGVSREF
RVRRIVPPDD PDDNEKATGA AGAAGAAATQ TRADIQGQIS IHLPHNSLLV MHAETQEEYK
HSISPSQTIS PHPIAGNKRI NITYRWYRES LHPRFTPKCR CGMPCVLRCV QRKKETRGRY
MWMCYAGYAV GNTSCSFFQW AEFDEDGEPV WANEGKAKGI GVEAGANNDH VQEKQ
//
