UniProt: A0A0K0DCZ6

Database: UniProt
Entry: A0A0K0DCZ6_ANGCA

LinkDB:  A0A0K0DCZ6_ANGCA 
Original site:  A0A0K0DCZ6_ANGCA

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein domain (16)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (3)   
   SMART (2)   
All databases (21)   

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ID   A0A0K0DCZ6_ANGCA        Unreviewed;       470 AA.
AC   A0A0K0DCZ6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=ATP-dependent RNA helicase DDX1 {ECO:0000256|ARBA:ARBA00014916};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=DEAD box protein 1 {ECO:0000256|ARBA:ARBA00032348};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000851701-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000851701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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|ARBA:ARBA00001556};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic granule
CC       {ECO:0000256|ARBA:ARBA00004463}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008765}.
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DR   AlphaFoldDB; A0A0K0DCZ6; -.
DR   STRING; 6313.A0A0K0DCZ6; -.
DR   WBParaSite; ACAC_0000851701-mRNA-1; ACAC_0000851701-mRNA-1; ACAC_0000851701.
DR   Proteomes; UP000035642; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; IPR003877; SPRY_dom.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF186; ATP-DEPENDENT RNA HELICASE DDX1; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035642};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          1..167
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   DOMAIN          199..337
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          407..470
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   470 AA;  52593 MW;  5DCB4D9B1BC664AF CRC64;
     MTPHVSVVKF NHAAETGSGK TGAFSLPVVQ IVWERRKDAT SPPSVGNARK YYYEVKITRD
     GLCRIGWSAA SASLDLGTDY KSFGFGGTGM KSTQRKFEKY GESFSTGDVL GCYLDLDNGR
     IWWSKNGKEF EVAFRLDPEF SSPHCALHPA VLVQNSSVEL NFGATPFAFP PKAAPDSLVK
     WRELDVQSNR NEAAGAPVCI VLEPTKELIE QTHENLVKFS KHVDIPKIRC VSLAAGANMA
     QILSELNKGI DIVTGGVGRV LDMVETNKLS MGELNFIVID EADQILSSFT SQLERLLKLV
     PTVASNGMRV QVIACSATLH NQKITQFADK YMNFPQWIDL KGMDSVAETV HHVVCMVDAV
     GDKQWIRIMH GKNTLQHDYV HERDNIRFNT TEKNTLSLGT KILKGCYVLK AIEALKMEQC
     IIFCRTKQQC DQMETYLRKN NYRAACLHGD RSPRERSQAL ADFKVFFNFF
//

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