ID   ATD3B_XENLA             Reviewed;         593 AA.
AC   Q6PAX2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=ATPase family AAA domain-containing protein 3-B;
GN   Name=atad3-b;
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=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) 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}.
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DR   EMBL; BC060012; AAH60012.1; -; mRNA.
DR   RefSeq; NP_001083126.1; NM_001089657.1.
DR   AlphaFoldDB; Q6PAX2; -.
DR   SMR; Q6PAX2; -.
DR   DNASU; 398759; -.
DR   GeneID; 398759; -.
DR   KEGG; xla:398759; -.
DR   CTD; 398759; -.
DR   Xenbase; XB-GENE-946134; atad3a.L.
DR   OMA; KTCSKMA; -.
DR   OrthoDB; 357201at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 398759; Expressed in blastula 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-B"
FT                   /id="PRO_0000311983"
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   REGION          109..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          51..215
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        14..28
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..164
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;  66960 MW;  9AB7020718996FE3 CRC64;
     MSWLFGLNRG QPEPPGVPGF PEPPSPPGGS GDGGDKNRPK DKWSNFDPTG LERAAKAARE
     LDQSRHAKEA LNLAKVQEET LQMEQQAKIK EYEAAVEQIK NEQIRVQSEE KRKTLNEETK
     QHQARAQYQD KLARQRYEDQ LRQQQLQNEE NLRRQEESVQ KQEAMRKATV EHEMELRHKN
     DMLRIEAEAH ARAKVERENA DIIREQIRLK AAEHRQTVLE SIKTAGTVFG EGFRTFISDW
     DKVTATVAGL TLLAVGVYTA KNGTGVAGRY IEARLGKPSL VRDTSRITVV EAIKHPIKIS
     KRIFSKIQDA LEGVILSPRL EERVRDIAIA TRNTKANKGL YRNILMYGPP GTGKTLFAKK
     LAMHSSMDYA IMTGGDVAPM GREGVTAMHK VFDWAGTSKR GLLLFVDEAD AFLRKRSTEK
     ISEDLRATLN AFLYRTGEQS NKFMLVLASN QPEQFDWAIN DRIDEIVHFD LPGLEERERL
     VRLYFDKYVL QPASEGKQRL KVAQFDYGKK CSELATLTEG MSGREISKLG VAWQAAAYAS
     EDGILTEAMI DARVADAIRQ HQQKMEWLKA EGKESTKEIG KNPLQPLLEG TPV