ID A0A167L1P0_CALVF Unreviewed; 697 AA.
AC A0A167L1P0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=JmjC domain-containing histone demethylation protein 1 {ECO:0000256|ARBA:ARBA00015153};
DE EC=1.14.11.27 {ECO:0000256|ARBA:ARBA00013246};
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1 {ECO:0000256|ARBA:ARBA00031083};
GN ORFNames=CALVIDRAFT_516489 {ECO:0000313|EMBL:KZO95241.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO95241.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO95241.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO95241.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36'
CC of histone H3, thereby playing a central role in histone code.
CC {ECO:0000256|ARBA:ARBA00003909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000256|ARBA:ARBA00001574};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00008037}.
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DR EMBL; KV417290; KZO95241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167L1P0; -.
DR STRING; 1330018.A0A167L1P0; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23123:SF21; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 1; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 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:UP000076738};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 32..88
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 238..398
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 78580 MW; 3634012165F7AC2E CRC64;
MPPRRTRRSG KEDSATPSSQ GDKMEEDSKD DSELCPACPA DRKHGGRKKK EVWVSCENCS
TWYHWDCVSK GEDLAPIDKW FCDNCLASNP ELQITYKANA TRKSARAKTK QDYASMNEGL
PSDPNRWVKL LKVKKFAKDK FKRMKGKDVT LEWVESNDDA LTEPIVIPDP AGLGMRMPSE
EFTVDDVAEL VGQNTPVEVI DVAQQSSAPG WTLKAWAEYY DKPASQRDKI RNVISLEVTG
TKLAEKVTPP RIVSDLDWVH KFWPTNKRGG KSQWPKVGLY CLMSVAQCWT DWHVDFAAST
VYYHILKGAK EFYFIKPTDA NLAAYEKWSG SAELQAGTWL GDMVDEVIKV SLVEGNTMII
PTGWIHAVFT PVDSLVFGGN FLHSFNVATQ LRLRQIEINT KVPRKFRFPL FQKLCWYVAE
GYCDQLKKHA EFPPRALRGV LSLADFLVSE ARLIESGIDT PQRREAKDSI PTEKVKDASA
LARELQWRAR EALGEDEEED RPAKRRKTAA MNGKGKQKRV IEDSDDEDAE PGSHKRPRFR
NWEPRKWDIQ TEHELDERSE VVPADAAGDW VLQEGALDKL GAEGTEGVEH VTTGTEWVRI
RRFKSEDGKE RVERVKITRV IENWAWGYEK PEKKPGTDGE DGKGDSDRAD TRLSEGLASY
ANGDVDMRDA GAEDTAAVPP STGSEPKTED AVMVPEP
//
