ID A0A1S3TL15_VIGRR Unreviewed; 662 AA.
AC A0A1S3TL15;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ATP-dependent zinc metalloprotease FTSH 10, mitochondrial isoform X3 {ECO:0000313|RefSeq:XP_014494439.1};
GN Name=LOC106756494 {ECO:0000313|RefSeq:XP_014494439.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014494439.1};
RN [1] {ECO:0000313|RefSeq:XP_014494439.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014494439.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014494439.1; XM_014638953.2.
DR RefSeq; XP_014494440.1; XM_014638954.1.
DR AlphaFoldDB; A0A1S3TL15; -.
DR GeneID; 106756494; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000087766; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF2; SD01613P; 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, ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|RefSeq:XP_014494439.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003651}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 211..351
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 637..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 73499 MW; 81FA53C618DBFCC9 CRC64;
MGLFISYLSS RPREQREISF QEFKNKLLEP GLVDHIAVSN KSVAKVYLRN SPRNQTDSEG
VQGTLPAKEY EGQYKYYFNI GSVESFEEKL QDAQEDLGID PHDFVPVTYS AEMVWYQELM
RFAPTLLLLG SLLYMGRRMQ GGLGVGGGGG SKGARGIFNI GKAHVTKVDK NTKNKIYFKD
VAGCDEAKLE IMEFVHFLKN PKKYEELGAK IPKGALLVGP PGTGKTLLAK ATAGESGVPF
LSISGSDFME MFVGVGPSRV RNLFQEARQC APSIIFIDEI DAIGRARRRG GFSRSNDERE
NTLNQLLVEM DGFGTTSGVV VLAGTNRPHI LDKALLRPGR FDRQIEIDKP DIKGRDQIFQ
IYLKKIKLDH EPSYYSQRLA SLTPGFAGAD IANVCNEAAL IAARSEVTQV TMDHFEAAID
RIIGGLEKKN KVISKVERRT VAYHESGHAV AGWFLEHADP LLKVTIVPRG SAALGFAQYV
PSENLLLTKE QLFDMTCMTL GGRAAEQVLV GRISTGAQND LEKVTKMTYA QVAVYGFSDK
VGLLSFPSRM SKPYSSKTAA IIDSEVREWV NKAYERTVNL IEEHKEQVTQ IAELLLEKEV
LHQEDLRRIL GERPFKAIEP TNYDRFKEGF KEEEEKVATE STIVDVPEEG GGTSPLEPQV
VP
//
