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Database: UniProt
Entry: T0LAL4_COLGC
LinkDB: T0LAL4_COLGC
Original site: T0LAL4_COLGC 
ID   T0LAL4_COLGC            Unreviewed;       429 AA.
AC   T0LAL4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   28-JUN-2023, entry version 28.
DE   SubName: Full=GRF zinc finger {ECO:0000313|EMBL:EQB45280.1};
GN   ORFNames=CGLO_15868 {ECO:0000313|EMBL:EQB45280.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB45280.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB45280.1}.
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DR   EMBL; AMYD01003770; EQB45280.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0LAL4; -.
DR   STRING; 1237896.T0LAL4; -.
DR   eggNOG; ENOG502QUQ4; Eukaryota.
DR   HOGENOM; CLU_026011_0_0_1; -.
DR   OMA; IDPHPLA; -.
DR   OrthoDB; 325143at2759; -.
DR   Proteomes; UP000015530; 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:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
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   Pfam; PF06839; zf-GRF; 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   Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01343}.
FT   DOMAIN          241..357
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          368..413
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  48000 MW;  2896DBD25F92961B CRC64;
     MEPEKKRKLS PASTQRAEED DEPTEVKLAM LSSLHPNAEQ EMLLDVLLVH NGSVAESLEA
     LATPTSVKKP SGVMGAQSSL RNFATKSVEN GTGAESPAKR RLLSKKGTTL HLYDPDDIAE
     HTPCSVIHNF LPAEEANDLL RELLREAETF EKNVTFKLFD NVVASPHTTS FYVESYDEIQ
     RQKTDYLYNG AKLTDIRRIT PQLIKVKPKV AEAVNAEIQK RIATHYPGGK KLRFQSPKPW
     APNSAFVNCY DGPQENVGYH SDQLTYLGPR AVIGSLSIGV AREFRVRRII PKDGDSNSAE
     DPDAEGQISI HLPHNSLLVM HAEMQEEWKH SIAPAQSIDP HPVAGNKRIN ITYRDYKANM
     HPRYTPKCDC GIPCVLRVVQ RKKESHGKYF WMCHGGNAPG KESCSFFQWG KFDDDGNPIW
     THARPKPSA
//
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