ZCHC4_XENTR
ID ZCHC4_XENTR Reviewed; 487 AA.
AC Q66IH9;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=rRNA N6-adenosine-methyltransferase ZCCHC4 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H5U6};
DE AltName: Full=Zinc finger CCHC domain-containing protein 4 {ECO:0000305};
GN Name=zcchc4;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: rRNA N6-methyltransferase that specifically methylates the
CC adenine in position 4220 of 28S rRNA. N6-methylation of adenine(4220)
CC in 28S rRNA is required for translation.
CC {ECO:0000250|UniProtKB:Q9H5U6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(4220) in 28S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyladenosine(4220) in 28S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58724, Rhea:RHEA-COMP:16142, Rhea:RHEA-COMP:16143,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC Evidence={ECO:0000250|UniProtKB:Q9H5U6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H5U6}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H5U6}. Note=Accumulates in
CC the nucleolus, where ribosome biogenesis takes place.
CC {ECO:0000250|UniProtKB:Q9H5U6}.
CC -!- DOMAIN: The regulatory loop blocks the catalytic center by bridging the
CC methyltransferase domain and the C-terminal CCHC-type zinc finger,
CC resulting in an autoinhibitory conformation.
CC {ECO:0000250|UniProtKB:Q9H5U6}.
CC -!- SIMILARITY: Belongs to the ZCCHC4 family. {ECO:0000305}.
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DR EMBL; BC081342; AAH81342.1; -; mRNA.
DR RefSeq; NP_001008134.1; NM_001008133.1.
DR RefSeq; XP_012810057.1; XM_012954603.2.
DR RefSeq; XP_017945078.1; XM_018089589.1.
DR AlphaFoldDB; Q66IH9; -.
DR SMR; Q66IH9; -.
DR PRIDE; Q66IH9; -.
DR DNASU; 493496; -.
DR GeneID; 493496; -.
DR KEGG; xtr:493496; -.
DR CTD; 29063; -.
DR Xenbase; XB-GENE-1007153; zcchc4.
DR eggNOG; KOG4399; Eukaryota.
DR InParanoid; Q66IH9; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000000960; Expressed in 4-cell stage embryo and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008988; F:rRNA (adenine-N6-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR041370; Mlase_EEF1AKMT1/ZCCHC4.
DR InterPro; IPR039846; ZCCHC4.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR13493; PTHR13493; 1.
DR Pfam; PF10237; N6-adenineMlase; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..487
FT /note="rRNA N6-adenosine-methyltransferase ZCCHC4"
FT /id="PRO_0000150955"
FT DOMAIN 381..431
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ZN_FING 26..70
FT /note="GRF-type"
FT /evidence="ECO:0000255"
FT ZN_FING 429..446
FT /note="CCHC-type"
FT REGION 323..343
FT /note="Regulatory loop"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT REGION 445..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 160..163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 231..232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 264
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
SQ SEQUENCE 487 AA; 55773 MW; 9ECB0A09712B8FE2 CRC64;
MEGAEGSDSC DGIQVLLSRE VIDAAPQCPH GPTLLFVKVS QGKEQGRRFY ACSACRDRKD
CHFFQWEDDK VSQARLAARE EYNKSHQPPM THAQYVGRFQ EFTELPLAKR KFCSDCQQLL
LPTNWESHSG HRVLGDISLS QLKRPSQLLH PLENKKANAQ YLFAERSCTF LMDTIIALGF
RRVLCVGTPR LHELIKLRAC EGATPPIKSL LLDIDFRYSQ FYWEEEFCHY NMFNHHFFGG
EAAKMVCQKF LQEEDGKGAL LVTDPPFGGL VEPLAFSFKR LREMWKTTNP ENESNLPILW
MFPYFFESRI LQCFPDFTML DYQVDYDNHA LYKHGKTGRK QSPVRIFTDL PPDKIVLPAI
EGYRFCSVCE RFVCSGNKHC NICNCCTSKD GRPWKHCTQC NKCVKPSWTH CSACNHCALP
DHPCGTAGRG CFLCGGKDHK RRGCPHQSVS AHGKRMENLK QKNIKGSMKK QPIAATSKKR
KRKRNNP
