DDX27_BOVIN
ID DDX27_BOVIN Reviewed; 765 AA.
AC A1A4H6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX27;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 27;
GN Name=DDX27;
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 MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable ATP-dependent RNA helicase. Component of the
CC nucleolar ribosomal RNA (rRNA) processing machinery that regulates 3'
CC end formation of ribosomal 47S rRNA. {ECO:0000250|UniProtKB:Q96GQ7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Associates with PeBoW complex, composed of BOP1, PES1 and
CC WDR12. Interacts directly with BOP1 and PES1.
CC {ECO:0000250|UniProtKB:Q96GQ7}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q96GQ7}. Chromosome
CC {ECO:0000250|UniProtKB:Q96GQ7}. Note=Associates with 60S and 90S pre-
CC ribosomal particles. {ECO:0000250|UniProtKB:Q96GQ7}.
CC -!- DOMAIN: The C-terminal domain regulates nucleolar localization.
CC {ECO:0000250|UniProtKB:Q96GQ7}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC subfamily. {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; BC126497; AAI26498.1; -; mRNA.
DR RefSeq; NP_001073740.1; NM_001080271.1.
DR AlphaFoldDB; A1A4H6; -.
DR SMR; A1A4H6; -.
DR STRING; 9913.ENSBTAP00000048220; -.
DR PaxDb; A1A4H6; -.
DR PRIDE; A1A4H6; -.
DR Ensembl; ENSBTAT00000057089; ENSBTAP00000048220; ENSBTAG00000006671.
DR GeneID; 514567; -.
DR KEGG; bta:514567; -.
DR CTD; 55661; -.
DR VEuPathDB; HostDB:ENSBTAG00000006671; -.
DR VGNC; VGNC:56183; DDX27.
DR eggNOG; KOG0338; Eukaryota.
DR GeneTree; ENSGT00550000074997; -.
DR HOGENOM; CLU_003041_3_3_1; -.
DR InParanoid; A1A4H6; -.
DR OMA; AAHTDIR; -.
DR OrthoDB; 268859at2759; -.
DR TreeFam; TF314780; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000006671; Expressed in mesenteric lymph node and 107 other tissues.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chromosome; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..765
FT /note="Probable ATP-dependent RNA helicase DDX27"
FT /id="PRO_0000282324"
FT DOMAIN 218..392
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 426..572
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 55..57
FT /note="Required for interaction with the PEBOW complex"
FT /evidence="ECO:0000250|UniProtKB:Q96GQ7"
FT MOTIF 164..169
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 187..215
FT /note="Q motif"
FT MOTIF 340..343
FT /note="DEAD box"
FT COMPBIAS 17..31
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..145
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921N6"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GQ7"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GQ7"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GQ7"
SQ SEQUENCE 765 AA; 87087 MW; E2A54114FA1F9F84 CRC64;
MLSELGFIRT IGEDEDVQVE PETDSEDEEE EGPIVLGRKQ KALQKNRSAD FNPDFVFTEK
EGMYDGSWAM ADVLSQLKKK RAATTLDEKI EKVRKKRKTE DKEAKSGKSE KEKEAKEGSE
PEEEEDLERK DVEASEDEES ETDYSSADEN ILTKADTLKI KERKKKKKKG QEAGGFFEDA
SQYDENLSFQ DMNLSRPLLK AITAMGFKQP TPIQKACIPV GLLGKDICAC AATGTGKTAA
FALPVLERLI YKPRQAPVTR VLVLVPTREL GIQVHSVTKQ LAQFCSITTC LAVGGLDVKS
QEAALRAAPD ILIATPGRLI DHLHNCPSFH LSSIEVLILD EADRMLDEYF EEQMKEIIRM
CSHHRQTMLF SATMTDEVKD LASVSLKNPV RIFVNSNTDV APFLRQEFIR IRPNREGDRE
AIVAALLMRT FTDHVMLFTQ TKKQAHRMHI LLGLMGLQVG ELHGNLSQTQ RLEALRRFKD
EQIDILVATD VAARGLDIEG VKTVINFTMP NTIKHYVHRV GRTARAGRAG RSVSLVGEEE
RKMLKEIVKA AKAPVKARIL PQDVILKFRD KIEKMEKDVY AVLQLEAEEK EMQKSEAQIN
TAQRLLEKGK EAPNPEPERS WFQTKEERKK EKIAKALQEF DLALRGKKKR KKFMKEAKKK
GEMTAEERSQ FEILKAQMFA ERLAKRNRRA KRARAMPEEE PVRAPAKKQK QVKKSVFDEE
LTNTSKKALK QYRAGPSFEE RKKLGLPHQR RGGNFKSKSR YKRRK
