ID   A0A3B4UWY7_SERDU        Unreviewed;       667 AA.
AC   A0A3B4UWY7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=AFG3-like protein 1 {ECO:0000313|Ensembl:ENSSDUP00000023076.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000023076.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000023076.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000256|ARBA:ARBA00010044}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000256|ARBA:ARBA00010550}.
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DR   AlphaFoldDB; A0A3B4UWY7; -.
DR   STRING; 41447.ENSSDUP00000023076; -.
DR   Ensembl; ENSSDUT00000023502.1; ENSSDUP00000023076.1; ENSSDUG00000016707.1.
DR   GeneTree; ENSGT00940000160625; -.
DR   OMA; YDKQGGG; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.1690.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   NCBIfam; TIGR01241; FtsH_fam; 1.
DR   PANTHER; PTHR43655:SF7; AFG3-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; FtsH protease domain-like; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          207..346
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          623..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..657
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  73886 MW;  D723FF41F871E6AE CRC64;
     MQKGDFPWDE KDFRYMAITV AGVGSALLYF YFRDNGREIS WKDFVHRYLG RGLVDRLEVI
     NKQYVRVILM PGADADASYV WFNIGSVDTF ERNLETAHME LGLEPSHRAT VVYSTESDGS
     FLMSMLPTLL LIGFLLFTLR RGPMGGGAGG GRGGPFSMGE STAKMMKDSI DVKFKDVAGC
     EEAKVEILEF VNFLKNPQQY QDLGAKIPKG AVLSGPPGTG KTLLAKATAG EANVPFITVN
     GSEFLEMFVG VGPARVRDMF ALARKNAPCI LFIDEIDAVG RKRGGGNFGG QSEQENTLNQ
     LLVEMDGFNT ATNVVVLAGT NRPDILDPAL MRPGRFDRQI YIGPPDIKGR ASIFKVHLRP
     IKLDPNLDKD ALARKMAAAT PGFTGADIAN VCNEAALIAA RHLDPSVNGK HFEHAIDRVI
     GGLEKKTQVL QPTEKKTVAY HEAGHAIVGW FLQHADPLLK VSIIPRGKGL GYAQYLPREQ
     YLYSREQLFD RMCMMLGGRV AEEVFFDRIT TGAQDDLKKV TQSAYAQVVQ FGMSEKVGQV
     SFDLPRQGEM VMEKPYSEAT AELIDGEVRG LVDRAYERTL QLIREKKELV EMVGKRLLEK
     EVLDKADMLE LLGPRPFEEK STYEEFVEGT GSFEEDTSLP EGLRDWNQER GAEAEEAVPA
     QDKQQAV
//