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Database: UniProt
Entry: A0A090MW92_STRRB
LinkDB: A0A090MW92_STRRB
Original site: A0A090MW92_STRRB 
ID   A0A090MW92_STRRB        Unreviewed;       993 AA.
AC   A0A090MW92;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Transcriptional regulator ATRX {ECO:0000313|EMBL:CEF63543.1, ECO:0000313|WBParaSite:SRAE_1000180400.1};
GN   ORFNames=SRAE_1000180400 {ECO:0000313|EMBL:CEF63543.1,
GN   ECO:0000313|WBParaSite:SRAE_1000180400.1,
GN   ECO:0000313|WormBase:SRAE_1000180400};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF63543.1};
RN   [1] {ECO:0000313|EMBL:CEF63543.1, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_1000180400.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF63543.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_1000180400.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; LN609528; CEF63543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090MW92; -.
DR   STRING; 34506.A0A090MW92; -.
DR   EnsemblMetazoa; SRAE_1000180400.1; SRAE_1000180400.1; WBGene00258413.
DR   WBParaSite; SRAE_1000180400.1; SRAE_1000180400.1; WBGene00258413.
DR   WormBase; SRAE_1000180400; SRP04209; WBGene00258413; -.
DR   eggNOG; KOG1015; Eukaryota.
DR   OMA; WERECTE; -.
DR   OrthoDB; 12329at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
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: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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035682}.
FT   DOMAIN          361..544
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          713..897
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          87..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   993 AA;  115307 MW;  2D4682A2407A231F CRC64;
     MLYDEDDEDE GVSNDNQDFT KNKRNFRLSI QRFLKLNEIF NISSAAEDTE KLQLYDEIKD
     EGENIIAYIK LLMKIGEKNL CVNSKKLNKD DRNNCNEEDS DSTDNESPSA GSYENFNTSN
     DEILRIIDDK GLDYSSDDEI DAVVHLPSAS EDYIVNGDDI IQCTGDGDPD FSAPIKKFNK
     KRRRLSSSSS IEERNPPRKN YKLCDIDDEE LNNYSKEIID VSSDSSRSEV EIEKVYNSSE
     SIETIYLSGD DEPENDSNLL KKKHQRKILT NNQLAQSTRE AKKLNEIYRK EYSQRRESKK
     IIFYSTENDG IPYYDRRVEA IVLYDDGKHK VCVDKAFVKV LKPHQAEGID FLFFTTIRSL
     KYIDDPGNGG ILAHCMGLGK SLQVIAYLQT IFFDPIISKR ISKGLLLVPT NVINNWEREC
     TEKSSGDIHD NYLSAIEGWI NSSRPSIIIV GYEMFRNLIN FGDGKRNKMN SKKQQSMANK
     YCEYLQKCPH IVICDEAHRL KNISSKIASA VNEISTRRRI CLTGTPIQNN LREYYTMINF
     VRPSLLGTYK EFSNQFVNPI EKGIKIGAAP HDVRLMKRRY VVLWKLLEHV VNRKDASFLY
     STLPPKEEYL IYCSASATQV KLLNGLVEIF PFNNSCIRMK PVMSYICTHP YILKKVYVDN
     VSARIYDDQD NSDLENIDDK VKISEWLRDK CDSLKDIALN NFELSSKILI LFDILRYAER
     VGDKVLVFVQ YRETISYIEE SLKYFAKNDL WYDECPTLNT RELKKNEFRK RTWELYKDYF
     IITGETSLQE RSFIESRINM RRTKSTRPRL VLMTTKASSV GTNFIGANRV VLFESGFNPS
     DNLQALHRVY RIGQNKRTFV YRLITQGTID QRVQEKHILK EGISKCSIDK HNIRDLYNDE
     DTRWNKIDCI DVMSPTFSRG TLSKPNDDLL SYLIFEEGLT DEEKEKEWND YIEEQRRFEG
     TEFVSTFTNF PLNNEPEDVS LPFLRQLLQT SLS
//
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