ID A0A2K5YM04_MANLE Unreviewed; 1310 AA.
AC A0A2K5YM04;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Tudor domain containing 9 {ECO:0000313|Ensembl:ENSMLEP00000016602.1};
GN Name=TDRD9 {ECO:0000313|Ensembl:ENSMLEP00000016602.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000016602.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000016602.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR STRING; 9568.ENSMLEP00000016602; -.
DR Ensembl; ENSMLET00000040073.1; ENSMLEP00000016602.1; ENSMLEG00000032473.1.
DR GeneTree; ENSGT00940000157035; -.
DR OMA; FWMHYIF; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0071547; C:piP-body; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0034587; P:piRNA processing; IEA:Ensembl.
DR GO; GO:0141006; P:piRNA-mediated retrotransposon silencing by heterochromatin formation; IEA:Ensembl.
DR GO; GO:0141007; P:siRNA-mediated retrotransposon silencing by heterochromatin formation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd17988; DEXHc_TDRD9; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR CDD; cd20431; Tudor_TDRD9; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047384; Tudor_TDRD9.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF113; ATP-DEPENDENT RNA HELICASE TDRD9; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT DOMAIN 70..236
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 305..472
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 872..932
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
SQ SEQUENCE 1310 AA; 148142 MW; BD9FD0CD16D1519F CRC64;
SLSQRSSEVE YINKYRQLEA QELDVCGSVQ PTSGPGPRPS LAKLSNVTCI PGTTYKYPDL
PISRYKEEVV SLIESNSVVI IHGATGSGKS TQLPQYILDH YVQRSAYCSI VVTQPRKIGA
SSIARWISKE RAWTLGGVVG YQVGLEKIAT EDTRLIYMTT GVLLQKVVSA KSLMEFTHII
IDEVHERTEE MDFLLLVVRK LLRTNSRFVK VVLMSATINC KEFADYFAVP VQNKMNPAYI
FEVEGKPHSV EEYYLNDLGH IHHSKLSPHL LEEPVITKDI YEVAISLIQM FDDLDMKENG
NKAWSGAQFV LERSSVLVFL PGLGEINYMH ELLTNLVHKR LQVYPLHSSV ALEEQNNVFL
SPVPGYRKII LSTNIAESSV TVPDVKYVID FCLTRTLVCD EDTNYQSLRL SWASKTSCNQ
RKGRAGRVSR GYCYRLVHKD FWDHSIPDHV VPEMLRCPLG STILKAKLLN MGEPRALLAT
ALSPPGLSDI ERTILLLKEV GALAVSGQRE DENPHDGELT FLGRVLAQLP VNQQLGKLIV
LGHVFGCLDE CLIIAAALSL KNFFAMPFRQ HLDGYRNKVN FSGSSKSDCI ALVEAFKTWK
ACRQRGELRY PKDELNWGRL NYIQIKRIRE VAELYEELKT RISQFNMHVD SRRPVMDQEY
IYKQRFILQV VLAGAFYPNY FTFGQPDEEM AVRELAGKDP KTTVVLKHIP PYGFLYYKQL
QSLFRQCGQV KSIVFDGAKA FVEFSRNPTE RFKTLPAVYM AIKMSQLKVS LELNVHSAEE
IEGKVQGMNV SKLRNTRVNV DFQKQTVDPM QVSFNTSDRS QTVADLLLTI DVTEVVEVGH
FWGYRIDEKN LEILKKLTAE INQLTLMPLP THPHPDLVCL APFADFGKQR YFRAQVLYVS
GNSAEVFFVD YGNRSHVDLH LLMEIPCQFL ELPFQALEFK ICKMRPSAKS LVCGEHWSDG
ASQWFSSLVS GCTLLVKVFS VVHSVLHVDV YQYSGVQDAI NIRDVLIQQG YAELTEESYE
SKQSHEVLKG LFSKSVENVT DGCAPFPMKD DEKYLIRILL ESFSSNKLGT PNCKAVLHGP
FNPYELKCHS LTRISKFRCV WIEKESINSV IISDAPEDLH QRMLVAASLS INATGSTMLL
RETSLMPHIP GLPALLSMLF APVMELRIDQ NGKYYTGVLC GLGWNPTTGA SILPEHDMEL
AFDVQFSVED VVEVNILRAA INKLVCDGPN GCKCLGPERV AQLQDSARQK LLGLFCQSKP
REKIVPKWHE KPYEWNQVDP KLVMEQADRE SSRGKNTFLY QLHKLVVLGT
//
