ID   ATD3A_XENLA             Reviewed;         593 AA.
AC   Q58E76;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=ATPase family AAA domain-containing protein 3-A;
GN   Name=atad3-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for mitochondrial network organization,
CC       mitochondrial metabolism and cell growth at organism and cellular
CC       level. May play an important role in mitochondrial protein synthesis.
CC       May also participate in mitochondrial DNA replication. May bind to
CC       mitochondrial DNA D-loops and contribute to nucleoid stability.
CC       Required for enhanced channeling of cholesterol for hormone-dependent
CC       steroidogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}. Mitochondrion matrix,
CC       mitochondrion nucleoid {ECO:0000250}. Note=In the mitochondrial inner
CC       membrane, enriched in sites with the potential to form contacts with
CC       the outer membrane. The N-terminal domain interacts with the inner
CC       surface of the mitochondrial outer membrane and the C-terminal domain
CC       localizes in a specific matrix compartment, where it is associated with
CC       nucleoids (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC092039; AAH92039.1; -; mRNA.
DR   RefSeq; NP_001089330.1; NM_001095861.1.
DR   AlphaFoldDB; Q58E76; -.
DR   SMR; Q58E76; -.
DR   BioGRID; 592161; 1.
DR   GeneID; 734380; -.
DR   KEGG; xla:734380; -.
DR   CTD; 734380; -.
DR   Xenbase; XB-GENE-6251449; atad3a.S.
DR   OrthoDB; 357201at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 734380; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042645; C:mitochondrial nucleoid; 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:0007005; P:mitochondrion organization; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR039188; ATAD3.
DR   InterPro; IPR021911; ATAD3_N.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23075; PTHR23075; 2.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF12037; DUF3523; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Mitochondrion nucleoid; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..593
FT                   /note="ATPase family AAA domain-containing protein 3-A"
FT                   /id="PRO_0000311982"
FT   TOPO_DOM        1..242
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..593
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          52..215
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        34..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         348..355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   593 AA;  66894 MW;  D7D055DEBCDA842E CRC64;
     MSWLFGLNKG QQEPPGVPGF PEPPSPPGGS GDGGDKNKPK DKWSNFDPTG LERAAKAARE
     LDQSRHAKEA INLAKVQEET LQMEQQAKIK EYEAAVEQLK NEQIRVQAEE RRKTLNEETK
     QHQARAQYQD KLARQRYEDQ LRQQQLQNEE NLRRQEDSVQ KQEAMRRATV EHEMELRHKN
     EMLRIEAEAR AQAKVERENA DIIREQIRLK AAEHRQTVLE SIKTAGTVFG EGFRTFISDW
     DKVTATVAGL TLLAVGVYTA KNATGVAGRY IEARLGKPSL VRDTSRITVA EAVKHPIKIT
     KRLYSKIQDA LEGVILSPRL EERVRDIAIA TRNTKANKGL YRNILMYGPP GTGKTLFAKK
     LAMHSGMDYA IMTGGDVAPM GREGVTAMHK VFDWAGTSKR GLLLFVDEAD AFLRKRSTEK
     ISEDLRATLN AFLYRTGEQS NKFMLVLASN QPEQFDWAIN DRIDEIVHFD LPGLEERERL
     VRLYFDKYVL QPASEGKQRL KVAQFDYGKK CSELSKLTEG MSGREISKLG VAWQAAAYAS
     EDGILTEAMI DARVADAIRQ HQQKMAWLKA EGKEGAKEIG KNPLQPLLEG TQV