ID A0A2K6V0K1_SAIBB Unreviewed; 762 AA.
AC A0A2K6V0K1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=AFG3 like matrix AAA peptidase subunit 2 {ECO:0000313|Ensembl:ENSSBOP00000037683.1};
GN Name=AFG3L2 {ECO:0000313|Ensembl:ENSSBOP00000037683.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000037683.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000037683.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6V0K1; -.
DR Ensembl; ENSSBOT00000054627.1; ENSSBOP00000037683.1; ENSSBOG00000034911.1.
DR GeneTree; ENSGT00940000159566; -.
DR Proteomes; UP000233220; Unplaced.
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:0016043; P:cellular component organization; IEA:UniProt.
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:SF9; AFG3-LIKE PROTEIN 2; 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:UP000233220};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 111..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 305..444
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 42..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 85166 MW; F00C81A597E37425 CRC64;
CLRTLYRYVT TQARDSRNSL LTDVIAAYQR FCSRPPKGFE KYFPNGKNGK KNSEPKEVMG
EKKESKPAAM ARSSGRGGGG GKRSGKKDDS HWWSRFQKGD FPWDDKDFRM YFLWTALFWG
GVMFYFLFKR SGREITWKDF VNNYLSKGVV DRLEVVNKRF VRVNFIPGKT PVDGQYIWFN
IGSVDTFERN LETLQQELGI EGENRVPVVY IAESDGSFLL SMLPTVLIIA FLLYTIRRGP
AGIGRTGRGM GGLFSVGETT AKVLKDEIDV KFKDVAGCEE AKLEIMEFVN FLKNPKQYQD
LGAKIPKGAI LTGPPGTGKT LLAKATAGEA NVPFITVSGS EFLEMFVGVG PARVRDLFAL
ARKNAPCILF IDEIDAVGRK RGRGNFGGQS EQENTLNQLL VEMDGFNTTT NVVILAGTNR
PDILDPALLR PGRFDRQIFI GPPDIKGRAS IFKVHLRPLK LDSSLEKEKL ARKLASLTPG
FSGADVANVC NEAALIAARH LSDSINQKHF EQAIERVIGG LEKKTQVLQP EEKKTVAYHE
AGHAVAGWYL EHADPLLKVS IIPRGKGLGY AQYLPKEQYL YTKEQLLDRM CMTLGGRVAE
EIFFGRITTG AQDDLKKVTQ SAYAQIVQFG MSEKVGQISF DLPRQGDMVL EKPYSEATAR
LIDDEVRILI NDAYKRTVAL LTEKKADVEK VALLLLEKEV LDKNDMVELL GPRPFAEKST
YEEFVEGTGS LDEDTSLPEG LKDWNKEREK EKEEPPGEKV AN
//
