ZCHC4_BOVIN
ID ZCHC4_BOVIN Reviewed; 516 AA.
AC E1BGQ2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
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 {ECO:0000250|UniProtKB:Q9H5U6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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 -!- SUBUNIT: Interacts with components of the ASC-1 complex TRIP4, ASCC1,
CC ASCC2 and ASCC3. Interact with AHCYL1 and AHCYL2. Interact with YTHDC2.
CC {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; DAAA02017163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02017164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BGQ2; -.
DR SMR; E1BGQ2; -.
DR STRING; 9913.ENSBTAP00000009526; -.
DR PaxDb; E1BGQ2; -.
DR PRIDE; E1BGQ2; -.
DR eggNOG; KOG4399; Eukaryota.
DR HOGENOM; CLU_034589_0_0_1; -.
DR InParanoid; E1BGQ2; -.
DR OrthoDB; 709190at2759; -.
DR TreeFam; TF313872; -.
DR Proteomes; UP000009136; Unplaced.
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 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..516
FT /note="rRNA N6-adenosine-methyltransferase ZCCHC4"
FT /id="PRO_0000417068"
FT DOMAIN 398..448
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ZN_FING 38..84
FT /note="GRF-type"
FT /evidence="ECO:0000255"
FT ZN_FING 446..463
FT /note="CCHC-type"
FT REGION 339..360
FT /note="Regulatory loop"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT REGION 472..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 174..177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 245..246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 278
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
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="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
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 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9H5U6"
SQ SEQUENCE 516 AA; 59485 MW; C05C1254852EF6FC CRC64;
MATSRDRLGT LEAEGSSGRQ GYSGVEVVLS SDPATPAPLC PHELGPTLLF VKVNQGKEET
RRFYACSACR DRKDCNFFQW EDEKLSGARL AAREAHNRSC QPPLSRSQCV ERYLKFIELP
LSQRKFCQSC QQLLLPDDEE KHHEHQVVGD VSITQLKRPS KLLYPLENKK TNAQYLFADR
SCLFLVDLLS NLGFRRVLCV GTPRLHELIR LKESGGTKSN IRSLLLDIDF RYSQFYMEDS
FCHYNMFNHH FFDGKAALEV CKTFLQEDKG EGVIMVTDPP FGGLVEPLAV TFKKLIAMWK
EGHSQDNSQK ELPIFWIFPY FFESRICQFF PSFCMLDYQV VDYDNHALYK HGKTGRKQSP
VRIFTNIPPN KIILPIEEGY RFCPLCQRYV SLENQHCEHC NSCTSKDGRK WNHCFLCKKC
VKPSWIHCSI CNHCALPDHS CKGPKDGCFI CGELDHKRSA CPNISTSKKV NKAVRKQKQR
KSNKMKMETT KGQSMNHTSA TRKKKRRERT HQYLCS
