ID A0A091MU36_9PASS Unreviewed; 768 AA.
AC A0A091MU36;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=AFG3-like 2 {ECO:0000313|EMBL:KFP80167.1};
DE Flags: Fragment;
GN ORFNames=N310_12053 {ECO:0000313|EMBL:KFP80167.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP80167.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP80167.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP80167.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
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; KK836488; KFP80167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MU36; -.
DR MEROPS; M41.007; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
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:UP000053537};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..442
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 41..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP80167.1"
FT NON_TER 768
FT /evidence="ECO:0000313|EMBL:KFP80167.1"
SQ SEQUENCE 768 AA; 85136 MW; 8676947107635269 CRC64;
QLCENVTPGV TAADRSTVLA SVIAACRRLC SQPPKGFEKY FPNGKKANGT KGTSGETKET
KPASARQPSG PSSGGGGSGG KKGGKKEETH WWTRLQKGDI PWDVREFRMY VVGSSFFWTM
VVYYFFFRVP GREITWKDFV NNYLSKGVVD RLEVVNKRFV RVIFVPGKSP HEWYVWFNIG
SVDTFERNLE TVQQDLGIEV ENRLPVVYST ESDGSFLLSL LPTILIIGSL LYTLRRGPAG
LGRAGRGMGG LFSVGETTAK VLKDEIDVKF KDVAGCEEAK LEIMEFVNFL KNPKQYEDLG
AKIPKGAILT GPPGTGKTLL AKATAGEANV PFITVNGSEF LEMFVGVGPA RVRDLFALAR
KNAPCILFID EIDAVGRKRG RGNFGGQSEQ ENTLNQLLVE MDGFNTTTNV VILAGTNRPD
ILDPALMRPG RFDRQIYIGP PDIKGRASIF KVHLRPLKLD TVLNKDNLAR KLASLTPGFS
GADIANVCNE AALIAARHLS DAINQKHFEQ AIERVIGGLE KKTQVLQPEE KKTVAYHEAG
HAVAGWFLEH ADPLLKVSII PRGKGLGYAQ YLPKEQYLYT KEQLLDRMCM TLGGRVSEQI
FFGRITTGAQ DDLKKVTQSA YAQIVQFGMN EKVGQISFDL PRQGDMVLEK PYSEATARLI
DEEVRSLINI AYDRTLSLLT EKKAEVEKVA LRLLEKEVLD KSDMLDLLGP RPFAEKSTYE
EFVEGTGSLD EDTSLPEGLK DWNKEREKDK EETTDEQVAR QIKGGMPF
//