ID A0A421J4K0_9ASCO Unreviewed; 650 AA.
AC A0A421J4K0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=Altered inheritance of mitochondria protein 11 {ECO:0000313|EMBL:RLV83241.1};
GN ORFNames=JA9_003036 {ECO:0000313|EMBL:RLV83241.1};
OS Meyerozyma sp. JA9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV83241.1, ECO:0000313|Proteomes:UP000286412};
RN [1] {ECO:0000313|EMBL:RLV83241.1, ECO:0000313|Proteomes:UP000286412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA9 {ECO:0000313|EMBL:RLV83241.1,
RC ECO:0000313|Proteomes:UP000286412};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H3 family.
CC {ECO:0000256|ARBA:ARBA00010343}.
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:RLV83241.1}.
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DR EMBL; NSDU01000024; RLV83241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421J4K0; -.
DR STRING; 2028340.A0A421J4K0; -.
DR Proteomes; UP000286412; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; 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 Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032854; ALKBH3.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
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; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000286412};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 208..313
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 323..366
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
SQ SEQUENCE 650 AA; 74946 MW; CBD670B47696F334 CRC64;
MSDDQKLRAL EARFPQFEKS VLKEIYDACG GSLNQVMELL SGSAPKRKKT GLGKYQTSIT
SIFGGENTRK PKVPESVIVH NKAIQLYTPE DVAAHLGPYV SLYRNFLPSD LSNSILEYLM
SKRDRLAPNK FFLFDSWCVA NHSSGLFHDR KYKDEKYQQL IYNGKSHTKI NQFDEELSRA
ANFVNEFINE KIIPSSSPLP FQSKEKWTCD VCVVNYYEHM SNNLDWHSDR LSHIGPHNYI
ASISLGATRE FRVRKNYPPS QLYAIQVPHN SLVIMHPGCQ EEYRHSVNAL RASIQSHPIS
GNGRFNLTFR HYREEIIQNI PKCKCNMSMT LRRAFKTVEA RGKYFWTCEN KYQNKDCGTF
YWANFSNLEG NLIAEDDEDV SIWYSEHDVE KVTFVKHQSS YNFKLASASE EYKQRRKYQM
ALFMASGAAT IFAARFAFKS TLARQYVPTL FQGNHQPPTS YNFTTDAAVA VGTGTILCGS
VSSMIIFGTC WMMDVSTFQE FGWRMKTVMG GYEKQKQLAQ MPLDEESELV QNGLNDILEG
KYDDIEYTVR KRRYRPGMKA LRDIRQFQKS TELLIRKLPF ARLVKEIAEE FIGANYGIRW
QSHAVLALQE ACEAFLVHLL EDTNLCAIHA KRVTIMQKDI QLARRIRGQW
//
