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Database: UniProt
Entry: A4HAN8_LEIBR
LinkDB: A4HAN8_LEIBR
Original site: A4HAN8_LEIBR 
ID   A4HAN8_LEIBR            Unreviewed;      1944 AA.
AC   A4HAN8;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=ATP-dependent RNA helicase-like protein {ECO:0000313|EMBL:CAM38470.1};
GN   ORFNames=LBRM_20_1240 {ECO:0000313|EMBL:CAM38470.1};
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:CAM38470.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM38470.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM38470.1,
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).
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DR   EMBL; FR798994; CAM38470.1; -; Genomic_DNA.
DR   RefSeq; XP_001564408.1; XM_001564358.2.
DR   STRING; 5660.A4HAN8; -.
DR   GeneID; 5414955; -.
DR   KEGG; lbz:LBRM_20_1240; -.
DR   VEuPathDB; TriTrypDB:LbrM.20.1240; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_200021300; -.
DR   InParanoid; A4HAN8; -.
DR   OMA; CFMHAEQ; -.
DR   Proteomes; UP000007258; Chromosome 20.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd00048; DSRM_SF; 1.
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   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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:SF235; DEAH-BOX RNA HELICASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 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; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:CAM38470.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007258}.
FT   DOMAIN          910..1075
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          177..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1108..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1270..1289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1297..1316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1902..1944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1907..1936
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1944 AA;  211797 MW;  CB06713024DAD678 CRC64;
     MTIRCLAFAV ASPRLPSTHH HTRQQNDAES VRALLHIRFS SSVCVCVHSH GAIGGARSTG
     SSSTPLSEMP HACWQNSVFP LLSRHRLLGY PLFFAPSPLP HPISFSLADM GTFSHFFIRG
     SGLCVIATVP GMCSSMSCPC WRPWRMQTRQ WEGRSCVLLT VATVACHLSN GRAGTAHVPG
     NSGAFSHTSS SAPRYRSQEC GAIDSRASPQ PHRVVRCCLK RTTPSPAKEA VSPAVKSSSR
     DESSLAALLI SLETVGPSNT QRQQSALPTS SRKRTPRLTP TLFSPAKSQA RAEPKPTPVL
     SPSSSCFPNN STAASELKRT GNPTQRPPHK CAEMNRYSDK PLQEGTFSSM GEQREQRVQL
     RRARRRMSRT PQASRIRSLP GGRLEDATGV SPLAVDRGAE KRVVEMLRRS QQQTSPDAEF
     AMRDPTVHHI PHSKLMRCVL ELPLSSRCDG DGAEQKEVFA IGQSRKAKIA RALCFMHAEQ
     LLDHYMSSRG RPSSPTAGAS AVPPPLEEAV LPPLPKTPQP HEYRSWDEYV DASAAYVQAV
     AAHVKQEGYM REEVLQSGHP VVDRATELLR RYPKRYCRPT ALQDLNESLR DASSLMTTAH
     LAGTVFVATL VLDSRTGLTA TGVAKNMKTA KRQCAAHALC ILQLLKEDVE RQQEADGTGH
     SRRRGAQKGS SGSSTKKGLS HQPSAPLESI LRQLQPAYRR IVQYHHLLFG KASLTPQTSF
     TKESNTTSGS NSTITYRCHL TLNGLCCDAT GINRFEAERA AMEAAMTNLM LYDERLQAVQ
     AFVNAHLSIS PESIPSAALP AELVFQLQAQ LRQVTQQPED VAADAATDVA TGKTGSDDGA
     DIADDRSDRA RGMSERALLD LTQRSFARDP SYAAQMLQSM LALRRNPVYL TQFHPCRSTL
     AMATVKAQLL DAVQRHRVTV VCGTTGCGKT TQVPQYILDY EIEHGRGGLC NILVTQPRRL
     SSFSIAERIA QERLGTVGED VGYAVRLDAR PGRHITICTT GVLLQIFSTH PELEHISHLI
     IDEVHERDIN CDVVLALVKQ LLARNLRLRV VLMSATMQAD VFARYFGTDT PVVQVEGAVY
     PVTIRYLEDI AAEAATAQFC SPSLDAVSSA DSDQQDEGKK REHTTPIPLV KSSTTASRRV
     NTRKYLKIDY NLIAYLVHRS VQVDLQNNTD GKSILVFLPG WKELTSAMAA IMEYSGPYAL
     PDAKGRFYII LLHSTVDNAK QRECFMPAPP GTVKVVLATN IAESGITIDD AAVVIDTGLI
     KTTSWESRPT LPCHQGTTDT IGSSTSRRPT VAHVPLEKVP EDGRAGGSRG SGDTAASTPF
     FSTQLTLGYA SQANCTQRKG RAGRTQGGMC YRLFTKELWN SLPAFPEADI HRVPLMQVLL
     KLLSLGHANP KATLQTFLEP PSSTNVDASM EVLRGISAVG KTDALTPLGE YLALLPCDPR
     IGKMIIVGAV LRCLDSVLTV AACTDVCPYV TSRDVAAEAR KRRYLLSRSS QSDHISFLNA
     YNAFCANGEK EDFARLNLLH LGNLRVISKY KAQYRDILRH AGLISAQDEL EEDGEMVDSI
     DAAGDPVHGH LGGDSGTIKE TAVHSEGGKL NLSSGDSRTQ DVRVPGWVPL SYPGTLCVDT
     SALSRHSFDV ALVKACVCAA LFPNVALLRP PANTLSSMRR LHAARKVELR TKHFFSIKPT
     KDSVCRRVDG PRGGDAPGRD ELLRELRRDS QAVTTDSTTS STSPVQPVPA LFYVFQDVFG
     VRDPRRDFLT SLSAVSLWAL LLFGASESTT EYNAELSICV VDGWIAVHID RATYALVTQL
     RQSLFQCLRR KYHNPQDPQN NSALKTVTEV CRRLLKAPVL EMPAAKSLDT AGSTTCKTAA
     GRQQSPWQLV DMGTIIDPLV HLRHGDSADG SATAVAGENA LLNLDGGGDG DEDDDNEGLP
     NFNSVDGDDD DNDGNATEDG DQLK
//
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