GenomeNet

Database: UniProt
Entry: A4HMX7_LEIBR
LinkDB: A4HMX7_LEIBR
Original site: A4HMX7_LEIBR 
ID   A4HMX7_LEIBR            Unreviewed;       860 AA.
AC   A4HMX7;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Probable eukaryotic initiation factor 4A {ECO:0000256|ARBA:ARBA00024417};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=ATP-dependent RNA helicase eIF4A {ECO:0000256|ARBA:ARBA00030297};
GN   ORFNames=LBRM_34_3010 {ECO:0000313|EMBL:CAM43518.1};
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM43518.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM43518.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43518.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM43518.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43518.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC       varies with external and internal environmental conditions. It is
CC       composed of at least EIF4A, EIF4E and EIF4G.
CC       {ECO:0000256|ARBA:ARBA00025917}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FR799009; CAM43518.1; -; Genomic_DNA.
DR   RefSeq; XP_001568407.1; XM_001568357.1.
DR   AlphaFoldDB; A4HMX7; -.
DR   SMR; A4HMX7; -.
DR   STRING; 5660.A4HMX7; -.
DR   GeneID; 5419361; -.
DR   KEGG; lbz:LBRM_34_3010; -.
DR   VEuPathDB; TriTrypDB:LbrM.34.3010; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_340038700; -.
DR   InParanoid; A4HMX7; -.
DR   OMA; NCHDEAK; -.
DR   Proteomes; UP000007258; Chromosome 35.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF40; EUKARYOTIC INITIATION FACTOR 4A-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CAM43518.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007258}.
FT   DOMAIN          405..433
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          436..615
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          643..788
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           405..433
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  94393 MW;  F8DA41B8B18073A0 CRC64;
     MDYISDKKTS DTEYQRYGAV EGDEVSTFRD DRREYSRGGR GRRGGAHRSD NWRFDPSGGG
     PNGDDSGEYR GGRGGYRGGR GGRGGGRGSR GSYNTWTNRE TRDEDNAIPA TSDVAGANTP
     STTLTPTSAP AETGGVVAPA QESCEAPCEY GNREDDLGYS RGGRGGYRGG GRSYDSGYGG
     RGGRGGRRYC DPEEEGEEGG YSQSYNSGYG GGGYRRGGYG GRGGRRYYDD EGDYAEGGDR
     ACGRGYEDDD HDDGGSDPYR RSSAPWRRGN YGRDFDYDRP RGRGGRGGRR DFRSFRNEND
     AMEESGAAQD NAWTSLPAPT EAPTVPRESP PAPAKAEEGV PSPAPQQTQS GIRRVTRASH
     LRRNCHDEAK VMELFEHRHR QTGISLDNYD SIPVEMVPRD VKPVEDFADL LVEPALAANI
     ERCGYKKPTP VQRYGIPVAL AGSDLMACAQ TGSGKTAAFL IPVVQYMLVH GVSPARQRKS
     YPIALVLAPT RELAVQIFDE VRKLTFNTDI FYDVVYGGTR YPQRFEQDIL VACPGRLRDM
     FNEEYLSFSA IKFLILDEAD RMLEMGFEEQ IEELVASRYT DMPTVDDRQT FMFSATFPQR
     ILNLAKRYLR RKYYLLTVGR VGSTTKNITQ TIEHVPDNEK MDRLLQIIYG HEMSDMVLIF
     VETKKMAEDV NRRLHREGIS STTIHGDRRQ QDREAALEDF KQKVTPILVA TDVASRGLDI
     PDVAHVVQFD LPQEMDDYTH RIGRTGRAGN KGIATAFYNR NNRRLALDLH KYFSEHGQEI
     PKWFQQEAEL VEGEALLSRD IGGGGRRRGG GGGGGGGGGH RSGGSGGRGG GGGGGSWGDS
     RPSAPSGGGR RGCGMDDGGF
//
DBGET integrated database retrieval system