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Database: UniProt
Entry: A4HDD3_LEIBR
LinkDB: A4HDD3_LEIBR
Original site: A4HDD3_LEIBR 
ID   A4HDD3_LEIBR            Unreviewed;      1126 AA.
AC   A4HDD3;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Putative DNA repair and recombination protein RAD54 {ECO:0000313|EMBL:CAM42253.1};
GN   ORFNames=LBRM_24_0770 {ECO:0000313|EMBL:CAM42253.1};
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:CAM42253.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM42253.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM42253.1,
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:CAM42253.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM42253.1,
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).
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DR   EMBL; FR798999; CAM42253.1; -; Genomic_DNA.
DR   RefSeq; XP_001565343.1; XM_001565293.1.
DR   AlphaFoldDB; A4HDD3; -.
DR   STRING; 5660.A4HDD3; -.
DR   GeneID; 5415922; -.
DR   KEGG; lbz:LBRM_24_0770; -.
DR   VEuPathDB; TriTrypDB:LbrM.24.0770; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_240013600; -.
DR   InParanoid; A4HDD3; -.
DR   OMA; TITCASQ; -.
DR   Proteomes; UP000007258; Chromosome 24.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   CDD; cd18004; DEXHc_RAD54; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007258}.
FT   DOMAIN          453..623
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          800..956
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1126
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1126 AA;  123481 MW;  39886015FFD748B4 CRC64;
     MRKSTAGSGV ANGTFRPPTT SGEDKPAARK PSVHPLLPAT SASAVPRFMT GWRALSSGSC
     KAPGSGDSRN TNDSAADLPG PTVALVTSTG VRREVMYPTV TPHSAGSTAN NDLLAHRLAR
     RSQIDYHQPE SASKAVVART LQAAAAAQGK TGDEAEDCED QGSGAAKLIR VEAGAGGVKS
     VPSAPEAADG NAASAAKGSH EAAAAAANDD AIPTDKVVSC YPASPYGKLY FQVETDGATR
     HESVGIVIID TELLGVMMYD RVGRQYGNRP DPGYPIKQEE VDNAKAGSTL KVGTKHVLLI
     TALTEEAFRS GEFFLRSEHD LRVREDKAKA KADAAAAEEA KARKPEMSFG ISLGNNSAFA
     SILFRRRPKD GETGFVVPVA GRPKMGKNGI IMNELRPLHD PDREKAVVLF RADYKRDLHG
     RRQVSVVVDP IIGDKLRPHQ IIGVKFLFDC ITGERMLGYH GAILADEMGL GKTIQTVATI
     YTCLKQGKHG QPTARKCLVV TPSSLVKNWC NEFDKWLGEG AVKHFAISES TPKGDRIISR
     FDGDGDVLVI SYDQLRKYID RLSRLRFVEL VVCDEGHRLK NAEVKTTKAV DMLPTRNRII
     LSGTPIQNDL SEFHAMVNFV NPGILGNRDL FTRVFEEPVS LGRDPDCPDH LKSLGRDRAH
     YLSMLTQRFI LRRTQSINES YLPPKVDVTV FVRLGAKQEQ AYQKLADIVE SAECTPLVLI
     SALRKLCNHM DLFHDAVHLS HQVGNGIGAS AQQQQAGRRR GRSSAADEPQ GIPFSVLPKG
     FKPGSLSMDY GSKMHFVSLV LDELRENGEH DKLVIVSNFT QTLDIIAALC NSKRIAYFQL
     DGSTPIKKRQ QLVDYFNVPD SQEVVFLLSS KAGGVGLNLI GANRLILFDP DWNPANDAQA
     MGRVWRDGQK KRVFIYRLLS TGTIEEKIYQ RQVSKQGLSA NVVDMQEDSK QHFTLEELKS
     LFKYKVDTLC DTHDLLGCTS CEAAEPLATS DRGSRSKQAE ELKMQFRKVG QPKKKSGPRM
     DELKAWRHIS SVASFNLDSV TRAVARHAPS LLSFLFADER DNTKMPRPVV STRVKVDRPA
     FEDDEETITC ASQAAIQQQE SEMEIEVIDD DDEEEGEFDS SEEESD
//
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