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Database: UniProt
Entry: DDX27_BOVIN
LinkDB: DDX27_BOVIN
Original site: 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   27-MAR-2024, entry version 94.
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}.
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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; 9913-ENSBTAP00000048220; -.
DR   Ensembl; ENSBTAT00000057089.3; ENSBTAP00000048220.2; ENSBTAG00000006671.6.
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; CPTSRQT; -.
DR   TreeFam; TF314780; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000006671; Expressed in mesenteric lymph node and 107 other cell types or 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   CDD; cd17947; DEADc_DDX27; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF14; DEAD-BOX ATP-DEPENDENT RNA HELICASE 28; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
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