ID A0A091UXP9_NIPNI Unreviewed; 775 AA.
AC A0A091UXP9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
DE Flags: Fragment;
GN ORFNames=Y956_15477 {ECO:0000313|EMBL:KFQ95759.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ95759.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ95759.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ95759.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; KL410289; KFQ95759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UXP9; -.
DR STRING; 128390.A0A091UXP9; -.
DR eggNOG; KOG2004; Eukaryota.
DR Proteomes; UP000053283; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:InterPro.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03121; lonp2_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027501; Lonp2_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 2.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR001174-
KW 2};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000256|RuleBase:RU000591};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR001174-2,
KW ECO:0000256|RuleBase:RU000591}; Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000053283};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 1..143
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 574..760
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 507..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 666
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 709
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 298..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ95759.1"
FT NON_TER 775
FT /evidence="ECO:0000313|EMBL:KFQ95759.1"
SQ SEQUENCE 775 AA; 86425 MW; 112E6304E94BE1E6 CRC64;
RIGTAALAVQ VVGSNWPKPH YTLLVTGLCR FQILQLLKEK PYPVAEVEQL DRLEQFTNEH
KSEEELGELS EQFYKYAVQL VEMLDMSVPA VAKLRRLLDN LPREALPDIL TSIIRTSNQE
KLQILDAVRL EERFKMTIPL LVRQIEGLKL LQKTRKPKQD DDKRVVAIRP NRRINHIPSI
AEDEEEEEDH DDVVMLEKKI RTSSMSEQAL KVCLKEIKRL KKMPQSMPEY ALTRNYLELM
VELPWNKSTK DRLEIRAARI LLDNDHYAME KLKKRVLEYL AVRQLKNNLK GPILCFVGPP
GVGKTSVGRS IAKTLGREFH RIALGGVCDQ SDIRGHRRTY VGSMPGRIIN GLKTVGVNNP
VFLLDEVDKL GKSLQGDPAA ALLEVLDPEQ NHGFTDHYLN VAFDLSQVLF IATANTTATI
PPALLDRMEI IQVPGYTQEE KIEIAHRHLI PKQLEQHGLT PQQIQIPQVT TLDIITRYTR
EAGVRSLDRK LGAICRAVAV KVAEGQHKET KPDRAEVGEG EDCKEHVAED AKPESISDTA
DLALPPEMPI LIDFHALKDI LGPPMYETEV SERLSQPGVA IGLAWTPLGG EIMFVEASRM
DGEGQLTLTG QLGDVMKESA HLAISWLRSN AKRYQLTNAS GSFDLLDNTD IHLHFPAGAV
TKDGPSAGVT IVTCLASLFS GRLVCSDVAM TGEITLRGLV LPVGGIKDKV LAAHRAGLKR
VIIPRRNEKD LEEIAVNVRQ DLTFVMASCL DEVLNAAFDG GFAVKPRAER LNSKL
//