DDX3Y_PANTR
ID DDX3Y_PANTR Reviewed; 660 AA.
AC Q6GVM6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hughes J.F., Pyntikova T., Skaletsky H., Minx P.J., Rozen S., Wilson R.K.,
RA Page D.C.;
RT "The DNA sequence of the chimpanzee Y chromosome.";
RL Submitted (MAY-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; AY633112; AAT46349.1; -; mRNA.
DR RefSeq; NP_001008986.1; NM_001008986.1.
DR RefSeq; XP_016800148.1; XM_016944659.1.
DR AlphaFoldDB; Q6GVM6; -.
DR SMR; Q6GVM6; -.
DR STRING; 9598.ENSPTRP00000038771; -.
DR PaxDb; Q6GVM6; -.
DR PRIDE; Q6GVM6; -.
DR Ensembl; ENSPTRT00000041996; ENSPTRP00000038771; ENSPTRG00000022488.
DR GeneID; 449508; -.
DR KEGG; ptr:449508; -.
DR CTD; 8653; -.
DR VGNC; VGNC:13341; DDX3Y.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000154443; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q6GVM6; -.
DR OrthoDB; 595675at2759; -.
DR TreeFam; TF300364; -.
DR Proteomes; UP000002277; Chromosome Y.
DR Bgee; ENSPTRG00000022488; Expressed in testis and 13 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
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..660
FT /note="ATP-dependent RNA helicase DDX3Y"
FT /id="PRO_0000055013"
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 579..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..30
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 90..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..625
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 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 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62095"
FT MOD_RES 590
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 615
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 630
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 660 AA; 73191 MW; B84FDEC14235AC74 CRC64;
MSHVVVKNDP ELDQQLANLD LNSEKQSGGA SRASKGRYIP PHLRNREASK GFHDKDSSGW
SCSKDKDAYN SFGSRDSRGK PGYFSERGSG SRGRFDDRGR SDYDGIGNRD RPGFGRFERN
GHSRWCDKSD EDDWSKPLPP SERLEQELFS GGNTGINFEK YDDIPVEATG SNCPPHIENF
GDIDMGEIIM GNIQLTRYTR PTPVQKHAIP IIKGKRDLMA CAQTGSGKTA AFLLPILSQI
YTDGPGEALK AVKENGRYGR RKQYPISLVL APTRELAVQI YEEARKFSYR SRVRPCVVYG
GADIGQQIRD LERGCHLLVA TPGRLVDMME RGKIGLDFCK YLVLDEADRM LDMGFEPQIR
RIVEQDTMPP KGVRHTMMFS ATFPKEIQML ARDFLDEYIF LAVGRVGSTS ENITQKVVWV
EDLDKRSFLL DILGAAGTDS LTLVFVETKK GADSLEDFLY HEGYACTSIH GDRSQRDREE
ALHQFRSGKS PILVATAVAA RGLDISNVRH VINFDLPSDI EEYVHRIGRT GRVGNLGLAT
SFFNEKNINI TKDLLDLLVE AKQEVPSWLE NMAYEHQYKG GSRGRSKSNR FSGGFGARDY
RQSSGSSSSG FGASRGSSSR SGGGGYGNSR GFGGGGYGGF YNSDGYGGNY NSQGVDWWGN
