DDX3Y_PONAB
ID DDX3Y_PONAB Reviewed; 658 AA.
AC Q5RF43;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=ATP-dependent RNA helicase DDX3Y;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 3, Y-chromosomal;
GN Name=DDX3Y;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable ATP-dependent RNA helicase. May play a role in
CC spermatogenesis (By similarity). {ECO:0000250}.
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: May interact with TDRD3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between the nucleus and the cytoplasm in an XPO1-
CC dependent manner. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; CR857318; CAH89614.1; -; mRNA.
DR RefSeq; NP_001124720.1; NM_001131248.1.
DR AlphaFoldDB; Q5RF43; -.
DR SMR; Q5RF43; -.
DR GeneID; 100171569; -.
DR CTD; 8653; -.
DR eggNOG; KOG0335; Eukaryota.
DR InParanoid; Q5RF43; -.
DR OrthoDB; 595675at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; DNA-binding; Helicase; Hydrolase;
KW Isopeptide bond; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT CHAIN 2..658
FT /note="ATP-dependent RNA helicase DDX3Y"
FT /id="PRO_0000055014"
FT DOMAIN 209..401
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 412..573
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 178..206
FT /note="Q motif"
FT MOTIF 345..348
FT /note="DEAD box"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 222..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 100
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 103
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 109
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62095"
FT MOD_RES 588
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 613
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 628
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00571"
SQ SEQUENCE 658 AA; 73043 MW; 21237B600A5FDD6D CRC64;
MSHVVVKNDP ELDQQLANLD LNSEKQSGGA STASKGRYIP PHLRNREASK GFHDKDSSGW
SCSKDKDAYS SFGSRDSRGK SGYFSERGSG SRGRFDDRGR SDYDGIGNRD RPGFGRFERS
GHSRWCDKSD EDDWSKPLPP SERLEQELFS GGNTGINFEK YDDIPVEATG SNCPPHIENF
SDIDMGEIIM GNIELTRYTR PTPVQKHAIP IIKGKRDLMA CAQTGSGKTA AFLLPILSQI
YTDGPGEALK AVKENGRYGR RKQYPISLVL APTRELAVQI YEEARKFSYR SRVRPCVVYG
GADIGQQIRD LERGCHLLVA TPGRLVDMME RGKIGLDFCK YLVLDEADRM LDMGFEPQIR
RIVEQDTMPP KGVRHTMMFS ATFPKEIQML ARDFLDEYIF LAVGRVGSTS ENITQKVVWV
EDLDKRSFLL DLLGATGRDS LTLVFVETKK GADSLEDFLY HEGYACTSIH GDRSQRDREE
ALHQFRSGKS PILVATAVAA RGLDISNVRH VINFDLPSDI EEYVHRIGRT GRVGNLGLAT
SFFNEKNMNI TKDLLDLLVE AKQEVPSWLE NMAYEHHYKG GSRGRSKRFS GGFGARDYRQ
SSGSSSSGFG ASRGSSSRSG GSGYGNSRGF GGGGYGGFYN SDGYGGNYNS QGVDWWGN
