ID A0A0K9NMA1_ZOSMR Unreviewed; 828 AA.
AC A0A0K9NMA1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=ATP-dependent zinc metalloprotease FTSH 8, mitochondrial {ECO:0000313|EMBL:KMZ57197.1};
GN ORFNames=ZOSMA_88G00180 {ECO:0000313|EMBL:KMZ57197.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ57197.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase.
CC {ECO:0000256|ARBA:ARBA00003497}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ57197.1}.
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DR EMBL; LFYR01002101; KMZ57197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NMA1; -.
DR STRING; 29655.A0A0K9NMA1; -.
DR OMA; RDDTFEM; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
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: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; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF33; WRKY DOMAIN-CONTAINING PROTEIN; 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|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:KMZ57197.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KMZ57197.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 372..512
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 104..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 91657 MW; 1FFB19BE8746FD83 CRC64;
MIFSRIGRSN LARSARSRFQ NISPSGGGRR GGDSIVRSSC VSSEKVFNYP ILCRLCHGYS
MASAARNAFV AGRRNQCLGF EYFSLANPRF RRFFSSESSP NKKNFKNYYP KGKSTKKNGE
KKANMKEGPN SDGGPSYEII FKLKSSNLIA PFILMGLLYL TNITGFRSSD QKEISFQDFK
NHLLEPGLVD HIVVSNKEVA KIYTRRLQQI NNPSKGDGIQ ASTVDISAKG NDIQCKFYFN
IGSVESFEDK LEEAQQVLGL DPHDHIPVTY ESRVLWGREL LKFAPTLLFW AVLWGLARKM
QGGFGIGGSG GSSGARGIFN IGKAHVTKMD KNSKNKTYFK DVAGCDEAKQ EIMEFVHFLK
NPKKYELLGA KIPKGALLVG PPGTGKTLLA KATAGESEVP FLSISGSDFM EMFVGVGPSR
VRSLFQEARQ CAPSIIFIDE IDAIGRARGR GGLSGSNDER ESTLNQLLVE MDGFGTTTGV
VILAGTNRPD ILDKALLRPG RFDRQITLDK PDIKGREQIF RIYLKKLKLD NEPEFFSQRL
AALTPGFAGA DISNVCNEAA LVAARNEKTL ISMQHFESAI DRVIGGLEKK NKVISKLERR
TVAYHESGHA VTGWFLEHAE PLLKVTIVPR GTAALGFAQY VPNENLLMTK EQLFDMTCMT
LGGRASEEVL IGKISTGAQN DLEKVTKMTY AQVAVYGFSE KVGLLSFPQK DDGFNMTKPY
SSKTGAVIDI EVREWVAKAY ERTLELIKEH KDQVAQIAEL LLEKEVLHQD DLLRVLGERP
FKSSEPTNYD RFKKGFQDEE TSIGSGGDDK IPLDAPQQSQ QVFPTPSI
//
