ID A0A1R3GVB0_COCAP Unreviewed; 819 AA.
AC A0A1R3GVB0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Peptidase M41 {ECO:0000313|EMBL:OMO62022.1};
GN ORFNames=CCACVL1_23067 {ECO:0000313|EMBL:OMO62022.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO62022.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO62022.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO62022.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:OMO62022.1}.
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DR EMBL; AWWV01013355; OMO62022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3GVB0; -.
DR STRING; 210143.A0A1R3GVB0; -.
DR EnsemblPlants; OMO62022; OMO62022; CCACVL1_23067.
DR Gramene; OMO62022; OMO62022; CCACVL1_23067.
DR OMA; ARQKGNF; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
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: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; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 363..503
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 90335 MW; 149430CCE127522E CRC64;
MIFSKLGRSS SRYSSSRKSL YRGGGGGSAG ARSPGLPRLS GSVDRQNEEL GFLRRYLTSI
GARKEFSSKA YLSDLNFVLA NPRIRRFFSS ETPKKKNYEN FYPKEKKEIP KENGQKSDSK
DNSNANDQGN FQEMFLKMFQ NLVTPLLMIA LFLYSSPLSS GEQQQQISFQ DFQNKLLEPG
LVDHIVVSNK SVAKVYVRST PLSETSDDVV VQGPANGTSA RGHGGQYKYY FNIGSVDSFE
KKLKDAQEAL GIDQHDHVPV TYVSEMMWFQ ELLRFGPVLL LLGSFMYMSR RVQGGLGVGG
GGGKGARGIF NIGKAHVTKV DKNSKNKVYF KDVAGCDEAK QEIMEFVHFL KNPKKYEDLG
AKIPKGALLV GPPGTGKTLL AKATAGESGV PFLSISGSDF MEMFVGVGPS RVRNLFQEAR
QCAPSIVFID EIDAIGRARG RGGFSGSNDE RESTLNQLLV EMDGFGTTSG VVVLAGTNRP
DILDKALLRP GRFDRQISID KPDIKGREQI FKIYLKKLKL DHEPSYYSQR LAALTPGFAG
ADIANVCNEA ALIAARAEGT QITMEHFEAA IDRIIGGLEK KNRVISKLER KTVAYHESGH
AVAGWFLEHA EPLLKVTIVP RGTAALGFAQ YVPNENLLMT KEQLFDMTCM TLGGRAAEQV
LLGKISTGAQ NDLEKVTKMT YAQVAVYGFS EKVGLLSFPQ RDDGFEMSKP YSNKTGAIID
GEVREWVAKA YEKTIQLIEE HKEQVAEIAE LLLEKEVLHQ EDLTRVLGER PFKASELTNY
DRFKQGFQEE ENKSIETPAG GESAEDDGST PLDPQVVPT
//
