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Database: UniProt
Entry: A0A2K5MZH6_CERAT
LinkDB: A0A2K5MZH6_CERAT
Original site: A0A2K5MZH6_CERAT 
ID   A0A2K5MZH6_CERAT        Unreviewed;       718 AA.
AC   A0A2K5MZH6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   Name=DDX31 {ECO:0000313|Ensembl:ENSCATP00000030614.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000030614.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000030614.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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         Evidence={ECO:0000256|RuleBase:RU365068};
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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DR   AlphaFoldDB; A0A2K5MZH6; -.
DR   Ensembl; ENSCATT00000054877.1; ENSCATP00000030614.1; ENSCATG00000038462.1.
DR   GeneTree; ENSGT00550000075041; -.
DR   OMA; AVHIKAD; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000038462; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17949; DEADc_DDX31; 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; IPR025313; DUF4217.
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; PTHR24031:SF89; ATP-DEPENDENT RNA HELICASE DDX31-RELATED; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          125..154
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          157..338
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          375..561
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           125..154
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   718 AA;  80241 MW;  97A2AB2BC37F5581 CRC64;
     MAAADSSLSD NPRTFSRRPS AQASRQAKAT KRKHQASSEA PPAKRRNETS FLPAKKTSVK
     ETQRAFKGNT QKTFTPKKQS VGPSDRNQEE RPCIKTSSLF KNNPDIPELH RPVVKQVQEK
     VFTSAAFHEL GLHPHLISTI NTVLKMSSMT SVQKQSIPVL LEGRDALVRS QTGSGKTLAY
     CIPVVQSLQA MKSKIQRSDG PYALVLVPTR ELALQSFDTV QKLLKPFTWI VPGVLMGGEK
     RKSEKARLRK GINILISTPG RLVDHIKSTK NIHFSRLRWL VFDEADRILD LGFERDITVI
     LNAVNAECQK RQNVLLSATL TEGVTRLADI SLHDPVSISV LDKSHDQLNP KDKAVREVCP
     PPAGDELDNF AIPESLEQHV TVVPSKLRLV CLAAFILQKC KFEKDQKMVV FFSSCELVEF
     HYSLFLQTLL SSSGAPASGQ LPSASTRLKF LRLHGNMEQE ERTAVFQEFS HSRRGVLLCT
     DVAARGLDLP QVTWIVQYNA PSSPAEYIHR IGRTARIGCH GSSLLILAPS EAEYVNSLAS
     HKIKSHAVGP QEIRERATVL QTVFEDYVHS SERRVSWAKK ALQSFIQAYA TYPRELKHIF
     HVRSLHLGHV AKSFGLRDAP RNLSALTRKK RKAHLKRPDL HKKTQSKHSL TEILRSEYSS
     GIEPGVAKVK KQNAPGEPGS RPLWPSLQPT PCFGHGKTLK WRKTQKALQQ DSKTSQKV
//
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