BCD1_PONAB
ID BCD1_PONAB Reviewed; 465 AA.
AC Q5RF97;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Box C/D snoRNA protein 1;
DE AltName: Full=Zinc finger HIT domain-containing protein 6;
GN Name=ZNHIT6; Synonyms=BCD1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA
CC processing, snoRNA transport to the nucleolus and ribosome biogenesis.
CC {ECO:0000250|UniProtKB:Q9NWK9}.
CC -!- SUBUNIT: Interacts with FBL, SNU13, NOP58, NUFIP1, RUVBL1, RUVBL2 and
CC TAF9 (By similarity). Interacts (via HIT-type zinc finger) with the
CC RUVBL1/RUVBL2 complex in the presence of ADP (By similarity).
CC {ECO:0000250|UniProtKB:Q9NWK9}.
CC -!- SIMILARITY: Belongs to the BCD1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR857264; CAH89560.1; -; mRNA.
DR RefSeq; NP_001124682.1; NM_001131210.1.
DR AlphaFoldDB; Q5RF97; -.
DR SMR; Q5RF97; -.
DR STRING; 9601.ENSPPYP00000001381; -.
DR PRIDE; Q5RF97; -.
DR GeneID; 100171529; -.
DR KEGG; pon:100171529; -.
DR CTD; 54680; -.
DR eggNOG; KOG2858; Eukaryota.
DR InParanoid; Q5RF97; -.
DR OrthoDB; 678600at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR007529; Znf_HIT.
DR Pfam; PF04438; zf-HIT; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..465
FT /note="Box C/D snoRNA protein 1"
FT /id="PRO_0000280241"
FT ZN_FING 215..249
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
SQ SEQUENCE 465 AA; 53327 MW; 9D6C45CEE6777638 CRC64;
MEFAAENEGK SGGGLHSVAE GVRLSPEPGR EGVRDLAGAE EFGGGEEGKG LTGVKEIGDG
EEGSRQRPEE IPMDLTVVKQ EIIDWPGTEG RLAGQWVEQE VEDRPEVKDE NAGVLEVKQE
TDSSLVVKEA KVGDLEVKEE VMDSSEVKEE KDNLEIKQEE KFVGQCIKEE LMHGECVKEE
KDFLKKEIVD DTKVKEEPPI NHPVGCKRKL AMSRCETCGT EEAKYRCPRC MRYSCSLPCV
KKHKAELTCN GVRDKTAYIS IQQFTEMNLL SDYRFLEDVA RTADHISRDA FLKRPISNKH
MYFMKNRARR QGINLKLLPN GFTKRKENST FFDKKKQQFC WHVKLQFPQS QAEYIEKRVP
DDKTINEILK PYIDPEKSDP VIRQRLKAYI RSQTGVQILM KIEYMQQNLV RYYELDPYKS
LLDNLRNKVI IEYPTLHVVL KGSNNDMKVL RQVKSESTKN LGNEN
