ID   ATRY_NOTEU              Reviewed;          96 AA.
AC   P83946;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Transcriptional regulator ATRY;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase ATRY;
DE   Flags: Fragments;
GN   Name=ATRY;
OS   Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=9315;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=11069290; DOI=10.1073/pnas.230424497;
RA   Pask A., Renfree M.B., Marshall Graves J.A.;
RT   "The human sex-reversing ATRX gene has a homologue on the marsupial Y
RT   chromosome, ATRY: implications for the evolution of mammalian sex
RT   determination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:13198-13202(2000).
CC   -!- FUNCTION: Could be a global transcriptional regulator. Modifies gene
CC       expression by affecting chromatin (By similarity).
CC       {ECO:0000250|UniProtKB:Q61687}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in developing and adult testis. Also
CC       weakly expressed in prostate and epididymis.
CC       {ECO:0000269|PubMed:11069290}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; AF303445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P83946; -.
DR   SMR; P83946; -.
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:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR025766; ADD.
DR   InterPro; IPR041430; ADD_ATRX.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF17981; ADD_ATRX; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51533; ADD; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Nucleus; Zinc; Zinc-finger.
FT   CHAIN           <1..>96
FT                   /note="Transcriptional regulator ATRY"
FT                   /id="PRO_0000074307"
FT   DOMAIN          <1..96
FT                   /note="ADD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   ZN_FING         <1..12
FT                   /note="GATA-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   ZN_FING         27..82
FT                   /note="PHD-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000303|PubMed:11069290"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:11069290"
FT   NON_TER         96
FT                   /evidence="ECO:0000303|PubMed:11069290"
SQ   SEQUENCE   96 AA;  11037 MW;  EED54BFC5F8F624F CRC64;
     VICTACGQQV NQFQKDSIYR HPTLNVLICK RWCAEGGNLI CCDSCHNAFC KKCIWRNLGR
     KEISKIMNEK NEWHCYICCP EPLLDLIAVC DSVLEN