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Database: UniProt
Entry: H2UNJ8_TAKRU
LinkDB: H2UNJ8_TAKRU
Original site: H2UNJ8_TAKRU 
ID   H2UNJ8_TAKRU            Unreviewed;       893 AA.
AC   H2UNJ8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=DEAD/H-box helicase 11 {ECO:0000313|Ensembl:ENSTRUP00000038519.3};
GN   Name=ddx11 {ECO:0000313|Ensembl:ENSTRUP00000038519.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000038519.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000038519.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000038519.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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DR   AlphaFoldDB; H2UNJ8; -.
DR   Ensembl; ENSTRUT00000038658.3; ENSTRUP00000038519.3; ENSTRUG00000015074.3.
DR   eggNOG; KOG1133; Eukaryota.
DR   GeneTree; ENSGT00950000182970; -.
DR   InParanoid; H2UNJ8; -.
DR   OMA; QTHQFRD; -.
DR   TreeFam; TF300435; -.
DR   Proteomes; UP000005226; Chromosome 9.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:1990700; P:nucleolar chromatin organization; IEA:Ensembl.
DR   GO; GO:1901836; P:regulation of transcription of nucleolar large rRNA by RNA polymerase I; IEA:Ensembl.
DR   GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT   DOMAIN          4..423
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          75..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  100283 MW;  4D70F1BC1127F01D CRC64;
     MDIGRTQFPF PYQPYDIQQQ FMQALYSALD QGKVGIFESP TGTGKSLSLI CGALSWLTDF
     EEKRRQETAA LLQKGEVSLS SAAPSSSTSS SAEPDWITDF VQKKAERDLV SKLKDDELKR
     QKREERLEMI RGNAQLKYAM KRKSSEDDEA FQLLQLSKDD RTEERGDEGD EELVIAEYQS
     DDESKTRSRY CADEDDAGDE LVEEHITKIY YCSRTHSQLA QFVHEVQKSP FANDISLVTL
     GSRQNLCINE EVRRLGSIQH INDRCMEMQK NKHEKQHQED GAKRKRGPAK STCPYNKAPA
     LQRMRDEILG AVQDIEQLLK LGSETRSCPY YSTRLTIPPA QLVVLPYQML LHEATRRAAG
     VQLKGQVVII DEAHNLSDTL SCIYSAELTG AQLCRAHSQL TQYTHRFKSR LKAKNLMYIK
     QILFVIEGLI RVLGGKVGQN PQSQTTKAGT EMLTINNLLF KAEIDNINLF KLQKYFQKSL
     ISRKLGGFVE KYAGTGMTLH PQSCSNKENR RTQGLNHYLQ TLQSNRTAPV SAADQQGSLE
     AEKALAASPM MQVEGFFMAL TSSNTDGRVV VNNQETLSES SVKFLLLNPA VHFAQILKEC
     RAVVIAGGTM QPVSDFKQEL LFSAGVGEER IVEFSCGHVI PPENILPLVL CNGPSGQELD
     FTFQNRDSPH MMDETGRILS NICNVVPGGV VCFFPSYEYL RRITSHWETN GTLARLANKK
     KIFHEPKKSN LVEQVLKDFS RCIQRCAADS GALTGALLFS VVGGKMSEGI NFSDDLGRCV
     VMVGMPYPNI KSPELQEKMS YLDKHLPHNG GKSPGQALIE NLCMKAVNQS IGRAIRHRGD
     YSSMVLCDRR YSRPATLAKL PAWIRDRTST HTSFGPAFAT LRKFFHERKR KQV
//
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