ID V8PG40_OPHHA Unreviewed; 748 AA.
AC V8PG40;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
DE Flags: Fragment;
GN Name=lonp2 {ECO:0000313|EMBL:ETE72963.1};
GN ORFNames=L345_01192 {ECO:0000313|EMBL:ETE72963.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE72963.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE72963.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE72963.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix
CC {ECO:0000256|ARBA:ARBA00004253}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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:ETE72963.1}.
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DR EMBL; AZIM01000152; ETE72963.1; -; Genomic_DNA.
DR AlphaFoldDB; V8PG40; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
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; 1.
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:UP000018936};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 1..169
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 547..733
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 639
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 682
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 303..310
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:ETE72963.1"
SQ SEQUENCE 748 AA; 83326 MW; AC2845B3B789BD71 CRC64;
MVLEEWSTVR MRSLLSVSMA GTCGVYRNRI GTAALAIQVV GSNWPKPHYT LLLTGLCRFQ
ILQLVKEKPY PVADVEQLDR LEQFTNKSEE ELGELPEQFY KYAVQLVEML DMSIPAVAKL
RRLLDNLPRE ALPDIVTSII RTSNQEKLQI LDAVGLEERF KMTIPLLVRQ IEGLKLLQKT
RKHKQDDDKR EDEDHDDIII LEKKIRASRM PEQALKVCIK EVKRLKKMPQ SMPEYALTRN
YLELMVELPW SKSTKDCLDI RAARILLDND HYAMEKLKKR VLEYLAVRQL KNNLKGPILC
FVGPPGVGKT SVGRSVAKTL GREFHRIALG GVRTYVGSMP GRIINGLKTV GVNNPVFLLD
EVDKLGKSLQ GDPAAALLEV LDPEQNHNFT DHYLNVAFDL SQVLFIATAN TTATIPAALL
DRMEIIQVPG YTQEEKIEIA HRHLIPKQLE QHGLTPQQVQ IPQEATLVII TRYTREAGVR
SLDRKLGAIC RAVAVKVAES QHKETRLDRS EGTEGALPPE MPILIDFHAL KDILGPPMYE
LEVSVRLNQP GVAIGLAWTP LGGEIMFVEA SRMDGEGQLT LTGQLGDVMK ESAHLAISWL
RSNAKRYQLT NASGSFDLLD NTDIHLHFPA GAVTKDGPSA GVTIVTCLAS LFSGRLVRSD
VAMTGEITLR GLVLPVGGIK DKVLAVHRAG LKSVIIPQRN EKDLEEIPAN VRQDLNFVMA
STLDDVLNSA FDGGFSTQAR LDHLNSKL
//