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Database: UniProt
Entry: H3A9G7_LATCH
LinkDB: H3A9G7_LATCH
Original site: H3A9G7_LATCH 
ID   H3A9G7_LATCH            Unreviewed;       573 AA.
AC   H3A9G7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 2.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   Name=DDX28 {ECO:0000313|Ensembl:ENSLACP00000006288.2};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000006288.2, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000006288.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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:RU365068}.
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DR   EMBL; AFYH01221058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006010709.1; XM_006010647.2.
DR   AlphaFoldDB; H3A9G7; -.
DR   STRING; 7897.ENSLACP00000006288; -.
DR   Ensembl; ENSLACT00000006341.2; ENSLACP00000006288.2; ENSLACG00000005578.2.
DR   GeneID; 102356803; -.
DR   KEGG; lcm:102356803; -.
DR   CTD; 55794; -.
DR   eggNOG; KOG0330; Eukaryota.
DR   GeneTree; ENSGT00940000161738; -.
DR   HOGENOM; CLU_003041_1_3_1; -.
DR   InParanoid; H3A9G7; -.
DR   OMA; NGDMLMK; -.
DR   OrthoDB; 389739at2759; -.
DR   TreeFam; TF324977; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000005578; Expressed in post-anal tail muscle and 2 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR24031:SF421; ATP-DEPENDENT RNA HELICASE DDX28-RELATED; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 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; 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:RU365068};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          158..186
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          189..379
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          408..561
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   MOTIF           158..186
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ   SEQUENCE   573 AA;  61886 MW;  F5DF6DB32866D6E1 CRC64;
     MLTAGGYRKA ALGARALLPT ACRRLAETQA GGPGIAPARL LVTSAPVCSS HHHHQHPGGV
     PSESVIRVPR NLQRRADSLR QLQKSEPLRF RPSRPGRLLI ACRRPAANQT LGYTCGKFEG
     PSLASKGWKH RKAFGDYFVI NPGHQGNHPA VEEDKKASTF GSLGLCSPLI EALETLGIAR
     PTAVQLQTIP KLLRGQNVLC AAETGSGKTF SYLLPAVHAL EAEDRAGGEA PGNPRCVVLV
     PSRELADQVQ AVARSLSGFV NLNVRTIGGG RGVGSIKTAL SGDVADILVA TPGALWKALK
     RDLVTLSNLR YFILDESDTL FDDSFIELVE DIFLHTRIAS NPSETSGLER KAQLVVIGAT
     FPGGTGKLLS KVTDLGSILT VKSKRLHFLM PHVKQKFLKV KGADKATELM QLLRTLSVEK
     PNTGMLIFCN SASTVNWLGY ILDDHGIKHL RLQGQMPGAM RAGIFKTFQK GSVDVLICTD
     IASRGLDTGR VEMVVNFDFP PSLTDYIHRA GRVGRVGSKT LGTVINYVTH PWDVELVQKI
     EAAARKRTIL PGMESAIDKP LPQTEKIEFG SEV
//
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