ZCHC4_XENLA
ID ZCHC4_XENLA Reviewed; 489 AA.
AC Q6DCD7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-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; BC078110; AAH78110.1; -; mRNA.
DR RefSeq; NP_001087167.1; NM_001093698.1.
DR AlphaFoldDB; Q6DCD7; -.
DR SMR; Q6DCD7; -.
DR MaxQB; Q6DCD7; -.
DR PRIDE; Q6DCD7; -.
DR DNASU; 447056; -.
DR GeneID; 447056; -.
DR KEGG; xla:447056; -.
DR CTD; 447056; -.
DR Xenbase; XB-GENE-1007158; zcchc4.S.
DR OMA; EFCLYNM; -.
DR OrthoDB; 709190at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 447056; Expressed in egg cell and 19 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; IPR001878; Znf_CCHC.
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.
DR PROSITE; PS50158; ZF_CCHC; 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..489
FT /note="rRNA N6-adenosine-methyltransferase ZCCHC4"
FT /id="PRO_0000150954"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 323..343
FT /note="Regulatory loop"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT REGION 455..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Basic residues"
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 489 AA; 56035 MW; 61ECC7E3762AC58F CRC64;
MEAAEGSENY DGIQVLLSRE VIDTAPQCPH GPTLLFVKVS QGKEQGRRFY ACSACRDRKD
CHFFQWEDEK VSQARLAARE EYNKSHQPPM THAEYARSFQ EFTALPLAKR KFCCDCQQLL
LQTNWETHSR HRVLGDISLS QLKRPSQLLH PLENKKANAQ YLFADRSCTF LLDTIIALGF
RRVLCVGTPR LHELIKLRAC KGTTPPIKSL LLDIDFRYSQ FYSEEEFSHY NMFNHHFFGG
EAAKLVCQKF LQEEDGNGAL LVTDPPFGGL VEPLAFSFKR LREMWKDSNP ENANNLPIFW
MFPYFFESRI LQCFPDFAML DYQVDYDNHA LYKHGKTGRK QSPVRIFTDL PLDKIVLPAS
EGYRFCSVCE RFVCSENKHC DICNRCTSKD GRSWKHCSQC KKCVKPSWSH CSACNHCALP
GHPCGTAGDG CFLCGGKGHK RRGCPHLSVS ADGERMKRNL KQRSIKGNMK KQPTATTSKK
KKRKRNNPC
