ID W5LYT8_LEPOC Unreviewed; 791 AA.
AC W5LYT8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Si:ch1073-174d20.2 {ECO:0000313|Ensembl:ENSLOCP00000001295.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000001295.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000001295.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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 EMBL; AHAT01010680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5LYT8; -.
DR STRING; 7918.ENSLOCP00000001295; -.
DR Ensembl; ENSLOCT00000001300.1; ENSLOCP00000001295.1; ENSLOCG00000001134.1.
DR eggNOG; KOG0731; Eukaryota.
DR GeneTree; ENSGT00940000160625; -.
DR HOGENOM; CLU_000688_23_1_1; -.
DR InParanoid; W5LYT8; -.
DR OMA; YDKQGGG; -.
DR Proteomes; UP000018468; Linkage group LG23.
DR Bgee; ENSLOCG00000001134; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..791
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004865336"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..470
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 72..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 87409 MW; FC6A72E450CE65FB CRC64;
MGLLSAAVWP LGLGSRCFAA GRSAVAAGVL SSPGSRRIFS LDRLKSFGFC EKNASFHRRL
CLKPPKGFDK YFPKNEKTPG RDRAGKTKEG KAKEAESGAG GGGGASGGGK KSGRKEESNW
WSRVQKGDFP WDEKDFRYLA IVIAGFSSGF LYFYFRDTGK EISWKDFVHY YLARGLVDRL
EVINKQFVRV ILAPGLRSSE VSYVWFNIGS VDTFERNLES AQQEMGMEPS HRVAVVYSTE
SDGSFLMSMI PTLLLIGFLL FTLRRGPMGA GRGGRGGGLF SMSESTAKMM KDNISVKFKD
VAGCEEAKIE ILEFVNFLKN PKQYQDLGAK IPKGAILSGP PGTGKTLLAK ATAGEANVPF
ITVNGSEFLE MFVGVGPARV RDMFAMARKN APCILFIDEI DAVGRKRGRG NFGGQSEQEN
TLNQLLVEMD GFNSSTNVVV LAGTNRPDIL DPALMRPGRF DRQIYIGPPD IKGRASIFKV
HLRPLKLDAS IDRDALARKL AALTPGFTAG ADIANVCNEA ALIAARHLNE FIIEKHFEQA
IERVIGGLEK KTQVLQPGEK KTVAYHEAGH AIVGWFLEHA DPLLKVSIIP RGKGLGYAQY
LPKEQYLYTR EQLFDRMCMM LGGRVAEQLF FGKITTGAQD DLKKVTQSAY AQIVQFGMSE
KVGQVSFDLP RQGEVVMEKP YSEATAQLID EEVRGLISTA YERTLRLLTE RKELVEKVGR
RLLEKEVLDK ADMVELLGPR PFTEKSTYEE FVEGTGSFEE DTSLPDGLKD WNQERASPQE
EPPLAQEKQA L
//
