ID   A0A3B4XIU5_SERLL        Unreviewed;       333 AA.
AC   A0A3B4XIU5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=ATPase family AAA domain-containing protein 1-B-like {ECO:0000313|Ensembl:ENSSLDP00000015700.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000015700.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000015700.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
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DR   AlphaFoldDB; A0A3B4XIU5; -.
DR   STRING; 1841481.ENSSLDP00000015700; -.
DR   Ensembl; ENSSLDT00000016281.1; ENSSLDP00000015700.1; ENSSLDG00000012434.1.
DR   GeneTree; ENSGT00550000074823; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45644; AAA ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G12920)-RELATED-RELATED; 1.
DR   PANTHER; PTHR45644:SF2; OUTER MITOCHONDRIAL TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          167..230
FT                   /note="ATPase AAA-type core"
FT                   /evidence="ECO:0000259|Pfam:PF00004"
FT   DOMAIN          254..294
FT                   /note="AAA ATPase AAA+ lid"
FT                   /evidence="ECO:0000259|Pfam:PF17862"
SQ   SEQUENCE   333 AA;  37563 MW;  5DAAD61DAA8E7124 CRC64;
     MVLREVPAEN IARPLGRNEV IGLLFRLTIF GAVTYFTIKW MVDAIDPTRK QKVEAQKQAE
     KLMRQIGVKN VKLSEYEMSI AAHLVDPLSM QITWRDIAGL DEVITELKET VILPVQKRHL
     FQGSRLLQPP KGQTERHDVI GSISLINLIT LISLINSISL IRLIRLINSF LRSRSSSDHE
     ATAMMKAQFM SLWDGLDTDH HCQVIIMGAT NRPQDLDSAI LRRMPTRFHI NQPSVRQREQ
     ILKLILENES VDSSVDLIDV AKETDGFSGS DLREMCRDAA LLCVRDFVHS QNDSSSEDFI
     RPIHQSDLQK SISKMKKSKS AGGHGALLHA ALD
//