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Database: UniProt
Entry: A4HH28_LEIBR
LinkDB: A4HH28_LEIBR
Original site: A4HH28_LEIBR 
ID   A4HH28_LEIBR            Unreviewed;      1591 AA.
AC   A4HH28;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=SNF2 DNA repair protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LBRM_29_0210 {ECO:0000313|EMBL:CAM39877.1};
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:CAM39877.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM39877.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM39877.1,
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:CAM39877.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM39877.1,
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; FR799004; CAM39877.1; -; Genomic_DNA.
DR   RefSeq; XP_001566369.1; XM_001566319.1.
DR   STRING; 5660.A4HH28; -.
DR   GeneID; 5417253; -.
DR   KEGG; lbz:LBRM_29_0210; -.
DR   VEuPathDB; TriTrypDB:LbrM.29.0210; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_290007400; -.
DR   InParanoid; A4HH28; -.
DR   OMA; ASHICLH; -.
DR   Proteomes; UP000007258; Chromosome 29.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR044574; ARIP4-like.
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; PTHR45797:SF1; HELICASE ARIP4; 1.
DR   PANTHER; PTHR45797; RAD54-LIKE; 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   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          72..327
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          499..652
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          452..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1376..1478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1376..1403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1420..1458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1464..1478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1591 AA;  175919 MW;  EEEBBBFBB6E3A447 CRC64;
     MSTVATDAGS SSSGCVDCSS LRHVTLELPP VMESVLRPHQ VNALEFIWKR LVLDGALRLA
     ARTFSSTIEQ RTRLYQEVFG VILAHSMGLG KTLTSLSFVL LFQAQTMLMA MKRDRVRQHQ
     QQQSERASTA VATGLVPKGA ACPALRVLVL CPRSCVLHWQ ASISEWIQPR YAGTMRVNSY
     VPSAMGISLN AMHRSSGGHS IEEVLLSYYQ KGGLLLLGYE EYQRILQYAQ AQYRSNPTNT
     WPRVWSLLDR LRLHLPLFQE VRLLDIIETA DLVILDEAHR LRRSSSNLVT ALARHLRNIQ
     LRLALTGTPL QNHLEEYNTM QSIVTGRELD TQLFHKHFIA PIERGQCVDS TYPQFLEMQR
     CIASLRRYFA DSAHHCGPEV LAATLPPRRE FLFFFRLSAA QEVAYKAMLK RFHTQVAAGE
     KGDSVLRLHH VASHICLHPA LSELEASSSS TALVSGKDGE EDGDDEDEDA TPVVSSTLPA
     AALSNLDVSV SPKLSFAFYL TLHIVREQRE KVVIFSQYLS HLRLMAQLLA REGISAPSLT
     GTSSDTERCR CIAELQSNDA CRVLLCSVRA GGVGIKLTAA SHCILLDVSW NPTDDVQATY
     RLYRYGQLRP VNVYRLATWG TSEHVVFAYA LQRAWLQKKI ADITDPRRQQ RHQTRSYFRY
     PCAVPLPEDG SGVTTDEQVT LPLSQSSLKE TLASNRRLEY ALGVCETQCA VAAHVLRMHP
     EEKGYLYTVI PQSVLLLHNE DDVIRERGRR FEDAAQKSRA SVAIPLQVTS GGAASAQSRE
     DLSLLDACEA ELVDAARQAA HLVITHVLRT REEAVSGRDA ASEVHTVDQT MCQRLQPLLI
     PALEARPPPR FLAEVLLLCY QAGAADVFRT LLQSSAYLKL RTYLASRVPA AGRRRTRDTA
     LPSRSPLEDA LLFTPVSLFK SMSSVEATYV ATELGCDRPF VGFCMLHGLQ KLWYVDGRLA
     LSETTLEALA ALLGIIPGRV DGDSDSEEVE EAVEGEDGVR VRSRRDADGA FAETVPALAQ
     SVLAAMASCL EEQWPPYEGF TLPPQHLQLE REEMRIGRAY RAASRAHMEG LLPLSQVSDL
     LRLPSYRQGQ HMYGCARCRS PLLQRLDATH LECPRCHYNA EFEVRADPRM QQQTVLYQLS
     VVANLLDAFS ITKSFAVSFS PSECGDVSAA LREVHTSQAV FEFVRRAMEE GVRAFLSEYP
     PRLVRLLGLQ LGTGGDVEEL RRVLLANGRL ASHTNVREHL RERLAQAFAD FVHPSTLTQF
     VAMPLMFLVT ALHYLARCER LSYAHELLLD ECPTPRRKLL RFASDALVKV LYVERLLKHC
     RQKPLPSSYA SSISVAASSA TLGMGTGAQQ ENVVSSNGDG AGSLTSLLMA ASSSAGSQSQ
     PCISTSSSSS FHSDSSGGSR SDNAAGARRS HKDPLLHAMD SSQNGRSGSG SRATSTTSSS
     SARPSSSSSF NSVYSGDRAS FPDGSASDAE ERDEAMRGQQ DTVTWLEELA RNTLERAAPT
     AEELESEAVQ QQRSAQYWIA FCEVYGTHSA ETLTVYIEDK ESGAKVLPPP PLSFWISQVA
     HTTMVGYCMT DMLDIFFKKV LELSQQVRVI S
//
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