ID U1GCC2_ENDPU Unreviewed; 451 AA.
AC U1GCC2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EPUS_00019 {ECO:0000313|EMBL:ERF75227.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF75227.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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DR EMBL; KE720815; ERF75227.1; -; Genomic_DNA.
DR RefSeq; XP_007787239.1; XM_007789049.1.
DR AlphaFoldDB; U1GCC2; -.
DR GeneID; 19235084; -.
DR eggNOG; ENOG502QUQ4; Eukaryota.
DR HOGENOM; CLU_026011_0_0_1; -.
DR OMA; IDPHPLA; -.
DR OrthoDB; 325143at2759; -.
DR Proteomes; UP000019373; 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:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; 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; 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 Pfam; PF06839; zf-GRF; 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:UP000019373};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 37..80
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 250..374
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 385..430
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 50833 MW; 7BF22BB3626BC6E3 CRC64;
MDEFVSRKRK RPTSPIQDHS TRLQMSGPAI TQDQEESTDV KLTILASLAP TISQEDLLEL
LISCDGYLDN ARAVLLYRNK APTSPRKKLT SIGLQSSLGF PTTNDPSKAQ KPLTRKGKTV
HLFSSADIAA HTPCSIIHNF LPAEDATKLL KELLAEAPTF PRATFKLFDN VVQSPHSAGF
YVSSLQERER QKSEYLYNGS YLSDVRELLP EMRKVSSKVK DAVNKEIAIR IAKHYPDGKK
LKYQCPHEWV PNAAFVNCYD GGAESVGYHS DQLSYIGPRA VIGSLSLGVA REFRVRKIVG
REEKETDAKH KEETDRSRAD EEGQIAIHLP HNSLLVMHAE MQEEWKHSIH PSSTVDLHPV
SGNKRINITY RWYRESFNPR YTPRCKCGIA TVLKCVQKKK ENRGRYMWMC QAGGIPGKQG
CGYFEWAEFT SDGEPLWKSA SAPRMQETLP A
//
