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Database: UniProt
Entry: V8PG40_OPHHA
LinkDB: V8PG40_OPHHA
Original site: V8PG40_OPHHA 
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
//
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