ID A0A2I0M566_COLLI Unreviewed; 1305 AA.
AC A0A2I0M566;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ATP-dependent RNA helicase DHX29 {ECO:0000256|HAMAP-Rule:MF_03068};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_03068};
DE AltName: Full=DEAH box protein 29 {ECO:0000256|HAMAP-Rule:MF_03068};
GN Name=DHX29 {ECO:0000256|HAMAP-Rule:MF_03068,
GN ECO:0000313|EMBL:PKK24820.1};
GN ORFNames=A306_00010727 {ECO:0000313|EMBL:PKK24820.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK24820.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK24820.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK24820.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation initiation.
CC Part of the 43S pre-initiation complex that is required for efficient
CC initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by
CC promoting efficient NTPase-dependent 48S complex formation.
CC Specifically binds to the 40S ribosome near the mRNA entrance. Does not
CC possess a processive helicase activity. {ECO:0000256|HAMAP-
CC Rule:MF_03068}.
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|ARBA:ARBA00001556, ECO:0000256|HAMAP-
CC Rule:MF_03068};
CC -!- SUBUNIT: Part of the 43S pre-initiation complex (PIC).
CC {ECO:0000256|HAMAP-Rule:MF_03068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03068}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK24820.1}.
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DR EMBL; AKCR02000038; PKK24820.1; -; Genomic_DNA.
DR RefSeq; XP_013227617.1; XM_013372163.1.
DR STRING; 8932.A0A2I0M566; -.
DR InParanoid; A0A2I0M566; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_03068; DHX29; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR034730; DHX29.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03068}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_03068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03068};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03068}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03068};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872}.
FT DOMAIN 519..691
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 794..963
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 128..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1305 AA; 148070 MW; B4FD39E694738182 CRC64;
MGTADQTKGL CPKTYSFSST TDSSAAANLD KSVLKVMING SLEKRIIDVI NDHKKQNDDK
GMISKRLTAK KLQDVYMALQ RFSFKTEHIE EAMKNTLLYG GDLHSALDWL CLNLPDDALP
EGFSQQFEEQ QQKPRAKFCS PVTKREPPPR IVDNKKKENG PATKKEVSMK EWILRYAEQQ
SDEEKDESVK EADEEKFDPN ERYVHLAAKL SEAKEQASIS KQDKDKQGQK AAQEKIRRIQ
QEMAVLEEHP VFNPAIKISN QQQNEKKNTP SPQPQETTLN LSLLEKPDGA AKEDKVKKKE
PLDIRNFDYS ARSWTGKSPK QFLIDWCRKN FPKSPNPAFE KVPVGKYWKC RVRIIKSSDD
VMTMCPTIVT EDSMQAQHLA ATLALYHLTK GQSVHQLLPP TYRDVWLEWR DIEMKKEEEN
KIETNKPRDN FIARLLNKLK QQQQLQSEDQ PKVSEGPEDS WENLVSDEDF SSLSLETSDT
DNLEPSRILF KKLQSSSKYQ RLLKERQELP VFKHRYSIVE TLKKHRVVVV AGETGSGKST
QVPHFLLEDL LLDEGSSKCN IVCTQPRRIS AVSLATRVCE ELGCESGPGG KNSLCGYQIR
MESRTGEATR LLYCTTGVLL RKLQEDGLLS SISHVIVDEV HERSVQSDFL LVILREILHK
RSDLHLILMS ATVDSEKFSS YFSHCPILRI SGRSYPVEVF HVEDVIEATG YVLEKDSEYC
QKFLEEEEEV TINVTGKGGG ITKYQEHVPI QSGSGIDLAP YYAKYSSRTQ QAIFYMNPYK
INLELILELL AYLDRSPQFN NIEGAVLIFL PGLAHIQQLY DLISTDRRFN LRDRHRLIAL
HSVLSTQDQA AAFTIPPLGV RKIVLATNIA ETGITIPDVV FVIDTGRTKE NRYHESSQMS
SLEETFVSKA SALQRQGRAG RVRAGFCFRM YTRDRFESFM EYSVPEILRV PLEELCLHIM
KCNLGSPEDF LSRALDPPQQ QVIGNAMNLL RKIGACLLNE PKLTPLGQHL AALPVNVKIG
KMLIFGAIFG CLDPVATLAA VMTEKSPFTT PIGRKDEADL AKSSLAMAVS DHITIYNAYL
GWKKARQEGG YRAEMTYCRR NFLNRTSLLT LEDVKQELIR VVRAAGFTAP TTQCGWDRNG
ATQSLSLHEI ALLKAVLTAG LYDNVGKILY TKSVDVTEKL ACMVETAQGK AQVHPSSVNR
DLQMYGWLLY QEKVRYAKVY LRETTLISPF PILLFGGDIE VQHRERLLTV DGWIHFQAPV
KIAVIFKQLR VLIECVLKKK LENPKMSLED DKVLHIIKEL IKTEN
//
