ID A0A310U4K0_XENLA Unreviewed; 776 AA.
AC A0A310U4K0; A0A974BQX1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=AFG3-like protein 1 isoform X1 {ECO:0000313|RefSeq:XP_018097708.1};
GN Name=afg3l2.L {ECO:0000313|RefSeq:XP_018097708.1,
GN ECO:0000313|Xenbase:XB-GENE-6251993};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018097708.1};
RN [1] {ECO:0000313|RefSeq:XP_018097708.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018097708.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018097708.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_018097708.1; XM_018242219.2.
DR AlphaFoldDB; A0A310U4K0; -.
DR STRING; 8355.A0A310U4K0; -.
DR PaxDb; 8355-A0A310U4K0; -.
DR GeneID; 443667; -.
DR KEGG; xla:443667; -.
DR AGR; Xenbase:XB-GENE-6251993; -.
DR CTD; 443667; -.
DR Xenbase; XB-GENE-6251993; afg3l2.L.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 443667; Expressed in heart and 20 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:SF7; AFG3-LIKE PROTEIN 1; 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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT DOMAIN 320..459
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 71..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 86585 MW; 002D0B5DAB5D1E89 CRC64;
MTAGIGRLVS AGVFGVSRRL RLCSLYGRAA LRECSSRSIT THICQSWRWN PCLSSVFCKP
PKGFEKYFQK NEKDSGSKNG SGEGNAKEEE TQRTSGGPNN RKDGNKEESA WWRRLQKGDF
PWDDKDFRNL AILAAGVASG FLFFYLHDPG REINWKEFVH LYLARGVVDR LEVVNKRFVR
VIPTAGTTPE KYVWFNIGSV DRFERNLENA QDELGIEQAQ RTSVIYSSES DGSFLMSLIP
TLLLVGFLLF SLRRGAMGPG RGGRGGGLFG VGETTAKILK GNIDVKFKDV AGCEEAKLEI
MEFVNFLKNP KQYQDLGAKI PRGAMLTGPP GTGKTLLAKA TAGEANVPFI TVNGSEFLEM
FVGVGPARVR DMFAMARKNA PCILFIDEID AVGRKRGRGN FGGQSEQENT LNQLLVEMDG
FNSSTNVVIL AGTNRPDILD PALMRPGRFD RQIYIGPPDI KGRASIFKVH LRPLKMSESL
SKDALSRKLA ALTPGFTGAD IANVCNEAAL IAARYLQDYV VEKHFEQAIE RVIGGLEKKT
QVLQPEEKRT VAYHEAGHAV VGWFLQHADP LLKVSIIPRG KGLGYAQYLP KEQYLYTREQ
LFDRMCMMLG GRVSEQLFFG RITTGAQDDL KKVTQSAYAQ IVQFGMSEKV GQVSFDLPRQ
GEMLAEKPYS EATAELIDQE ARNLINSAFE RTLELLTRCK DQVEKVAKRL LEKEVLEKSD
MVELLGARPF PEKSSYEEFV EGTGGFEEDT SLPEGLKDWN QEREDVQEHK RQENIS
//
