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Database: UniProt
Entry: A0A0A1U3Z7_ENTIV
LinkDB: A0A0A1U3Z7_ENTIV
Original site: A0A0A1U3Z7_ENTIV 
ID   A0A0A1U3Z7_ENTIV        Unreviewed;      1234 AA.
AC   A0A0A1U3Z7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Chromodomain helicase hrp1, putative {ECO:0000313|EMBL:ELP87418.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:ELP87418.1};
GN   ORFNames=EIN_096850 {ECO:0000313|EMBL:ELP87418.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP87418.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP87418.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP87418.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KB206860; ELP87418.1; -; Genomic_DNA.
DR   RefSeq; XP_004254189.1; XM_004254141.1.
DR   AlphaFoldDB; A0A0A1U3Z7; -.
DR   EnsemblProtists; ELP87418; ELP87418; EIN_096850.
DR   GeneID; 14886233; -.
DR   KEGG; eiv:EIN_096850; -.
DR   VEuPathDB; AmoebaDB:EIN_096850; -.
DR   OrthoDB; 22878at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
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; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF11; KISMET, ISOFORM C; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
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   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ELP87418.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:ELP87418.1}.
FT   DOMAIN          212..260
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          302..477
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          613..765
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1234 AA;  143777 MW;  CD510FBB81033D2F CRC64;
     MKPDNLPSLS NSQLLSKAPK LSLPPLSTPL NLAPISLHSL DATPSQLLKQ KSSESQALPS
     FFGNSERAKA VPVAKPKTKR KNAVLEEMEE EPTEMHYELR KRSRQPSALI DEDDDIDETL
     EKKKKEKTYE NGIPDSIGQP KILDKIIGIK EENSQRFVLV KWRGMSYLHV DTLPENVFLT
     MDGNVNANKQ KIKRFLQKKK EEEEEMIPQE YTTIDRVISM SKDKTRCLVK WQKLGYNEAT
     WENTEEITEN DGSKIEEYYR YNNYQFVQPL KERVWNKKIE SPVYKNNNTL RSYQLEGHNW
     MVYNWCKGRG CILADEMGLG KTVQVVTFLE HLHSYQKLHG PFLIVMPLGM VEHWHREISE
     WTDLNVILYS GSKENRKLVK KYEWFYTDEE GNKNTNQTKF NVMVTTYETL IADFEDLQQI
     SWFVVVIDEA QRLKNKDSKL LKTLSSLKTD HKILLTGTPI QNNLGELWTL LNYIEPKKFG
     SLEEFDKMYG NIDNNPEQVT ELQKSIKPFL LRRVKSDVEK SIPPKEETVI EVELTMVQKQ
     YYRALYEKNR EFLNKGCVGS NMPNLQNLMM QLRKVCNHPY LISGVEEKDT AQFAENSEEY
     FKQLIKSSGK LVLLDKLLPK LYEDKHKVLI FSQLKKVLNI IEKYLKYKGY LYERLDGSIR
     ALDRQNAIDR FMNPEMNKFV FLLCTRAGGF GINLSEADTV IIYDSDWNPQ NDLQAQARCH
     RIGQKKEVKV YRLVSKNTYE RYMFERASKK LGLDQAVLAN VTSSNDSKEK TQLSKAEIES
     LLKYGAYGVF KDDEESSSKF CEEDIEQILE KRSSKVVWKG DSVTGGSFST ATFQVEADAV
     DVNDKNFWEK VLPRNMSVSE LSKEFSDIFE GRGGRSAEKK RKVWMEEKKD EFMKEIFGHI
     DTIVGEYESK GKISSERDAL NALIEDILKY SESFETSEVE RLKGGLEGLK FTRYRRSTVN
     RISSATIGDE LTKDEEIVLE IGKKKRKKEV KEEMSEENKR MWYDAVIDYG RINWTILRDR
     ARVGEEVNQE YLHVISVRFL QNCIGSCSEQ NLEKKYFVKL LVCFYELKGK RESEVSEIEE
     YPLEDEFRWI ASNVKSWGNK LKFINRLSTL FENSADVVKA LIEIPNENCN FNQLTKWWNN
     DCDKDLVIGI YKYGFSCGEY LQQDKKLCFA EMMQQDEEDD HGKDDESEDE DGINFVVKLP
     KEFPNAKDLD RQGRSIIAWL DKYLKKMKRA DDDD
//
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