ID A0A1V4J903_PATFA Unreviewed; 808 AA.
AC A0A1V4J903;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=AFG3-like protein 2 isoform B {ECO:0000313|EMBL:OPJ68534.1};
GN Name=AFG3L2 {ECO:0000313|EMBL:OPJ68534.1};
GN ORFNames=AV530_006156 {ECO:0000313|EMBL:OPJ68534.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ68534.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ68534.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ68534.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ68534.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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:OPJ68534.1}.
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DR EMBL; LSYS01008581; OPJ68534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4J903; -.
DR STRING; 372326.A0A1V4J903; -.
DR Proteomes; UP000190648; 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:UP000190648};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..482
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 79..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 89667 MW; 6D1EF64EC2D7991E CRC64;
MAHRYLLLAR GSCRRRGLPG VLLQQLLCGR GLLGARPCLA QLREKVTTGV PTDRSTILAS
VIAACRRLFS QPPKGFEKYF PNGKKANGTK GTAAETKEAK PASARQPNGT SSGGGGSGGK
KGGKKEETNW WTRLQKGDIP WDVREFRMYV VGSSFFWTMV VYYFFFRVPG REITWKDFVN
SYLSKGLVDR LEVVNKRFVR VIFVPGKSPH EWQYVWFNIG SVDTFERNLE AVQQDLGIEV
ENRLPVVYST ESDGSFLLSL LPTILIIGSL LYTLRRGPAG LGRTGRGMGG LFSVGETTAK
VLKDEIDVKF KDVAGCEEAK LEIMEFVNFL KNPKQYEDLG AKIPKGAILT GPPGTGKTLL
AKATAGEANV PFITVNGSEF LEMFVGVGPA RVRDLFALAR KNAPCILFID EIDAVGRKRG
RGNFGGQSEQ ENTLNQLLVE MDGFNTTTNV VILAGTNRPD ILDPALMRPG RFDRQIYIGP
PDIKGRASIF KVHLRPLKLD TVLDKDNLAR KLASLTPGFS GADIANVCNE AALIAARHLS
DAINQKHFEQ AIERVIGGLE KKTQVLQPEE KKTVAYHEAG HAVAGWFLEH ADPLLKVSII
PRGKGLGYAQ YLPKEQYLYT KEQLLDRMCM TLGGRVSEQI FFGRITTGAQ DDLKKVTQSA
YAQIVQFGMN EKVGQISFDL PRQGDMVLEK PYSEATARLI DEEVRSLINI AYDRTLRLLT
EKKAEVEKVA LRLLEKEVLD KSDMLDLLGP RPFAEKSTYE EFVEGTGSLD EDTSLPEGLK
DWNKEREKEK EETTDEQVAR QTTGGVPF
//
