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Database: UniProt
Entry: A0A067FDL5_CITSI
LinkDB: A0A067FDL5_CITSI
Original site: A0A067FDL5_CITSI 
ID   A0A067FDL5_CITSI        Unreviewed;       612 AA.
AC   A0A067FDL5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=CISIN_1g005284mg {ECO:0000313|EMBL:KDO61552.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO61552.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO61552.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KK784924; KDO61552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067FDL5; -.
DR   MEROPS; M41.A06; -.
DR   Proteomes; UP000027120; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR   PANTHER; PTHR43655:SF19; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 12, CHLOROPLASTIC; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        107..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..346
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   612 AA;  69723 MW;  4BE7C7762DD8C76D CRC64;
     MKEVEKSLRK DMVEKVTETQ GTRALWIAKR WWRYRPKLPY TYFLEKLDSS EVAAVVFTED
     LKRLYVTMKE GFPLEYVVDI PLDPYLFETI ASSGAEVDLL QKRQIHYFLK VLIALLPGIL
     ILSLIRETVM LLHITSSRLL YKKYNQLFDM AYAENFILPV GYVSDTKSMY KEVVLGGDVW
     DLLDELMIYM GNPMQYYERG VQFVRGVLLS GPPGTGKTLF ARTLAKESGL PFVFASGAEF
     TDSEKSGAAR INEMFSIARR NAPAFVFVDE IDAIAGRHAR KDPRRRATFE ALIAQLDGDK
     ERTGIDRFSL RQAVIFICAT NRPDELDLEF VRPGRIDRRL YIGLPDAKQR VQIFDVHSAG
     KQLAEDVNFE ELVFRTVGFS GADIRNLVNE SGIMSVRKGH SKIQQQDIVD VLDKQLLEGM
     GVLLTEEEQQ KCEQSVSFEK KRLLAVHEAG HIVLAHLFPR FDWHAFSQLL PGGKETAISV
     FYPREDTIDQ GYTTFGYLKM QMVVAHGGRC AERLVFGDDV TDGGKDDLEK ITKIAREMVI
     SPQNARLGLA GLTRRVGLLD RPDSSDGDLI KYRWDDPQVI PTDMTLELSE LFTRELTRVI
     IKKKNCFILN EL
//
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