ID A0A0D2WX44_CAPO3 Unreviewed; 986 AA.
AC A0A0D2WX44;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
GN ORFNames=CAOG_007773 {ECO:0000313|EMBL:KJE97665.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE97665.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; KE346375; KJE97665.1; -; Genomic_DNA.
DR RefSeq; XP_004342846.1; XM_004342797.2.
DR AlphaFoldDB; A0A0D2WX44; -.
DR STRING; 595528.A0A0D2WX44; -.
DR MEROPS; S16.003; -.
DR EnsemblProtists; KJE97665; KJE97665; CAOG_007773.
DR GeneID; 14895041; -.
DR eggNOG; KOG2004; Eukaryota.
DR InParanoid; A0A0D2WX44; -.
DR OrthoDB; 1103874at2759; -.
DR PhylomeDB; A0A0D2WX44; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
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:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|RuleBase:RU000591};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000256|RuleBase:RU000591};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 15..359
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 777..974
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 76..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 880
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 923
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 986 AA; 104958 MW; 49487169C73C7CAD CRC64;
MAASSEIPSA VLDALPLLTV GQRVLLPGAL MQVFISRPAG VRLVTDRLWR SDGAQSVFVG
VLPVAIADAT ATAAALGSDR DPQASQTASI HQKENGAPRD ADADAERQSQ RQPSANSASV
SSLPTRMPRT AHDHDHDQHP PKGDKPTAAG SAGSAAGGSG GATRGGSDDD ASRPIAKFKA
PNADPATLTV PAIPAVPKLE ISATPDAAFA PLSQLVGEVG TIGRVVRLAR IKVGSKMVYN
LLLEGQCRFG VVAVRMDPFM VAQACQLELV FTPSQGALPP PTPGVEAMLY DSIRQLLKLL
ASRAPTLAGF DRIVDQVPLA RIVDLLMANM DLSFVDRVST LRELNVPLRF ERALALIQRQ
VSRLQTALEV PAPRGSLVGQ LVKMARNAKD GKTDDEGNNS SSTPPSIGDA NKDQDDADVE
ALETRIKALN LPEEVAPVVM RELAKLKRLH PQSSERQVYF SYLEVIADLP WNTLTEDVLD
LQKAQADLDH DHHGLAKVKK RILECLAVRK LRNDMKGPII CLVGPPGVGK TSLGRSIAST
LGRKFQRIAL GGMHDEAEIR GHRLTYVGAM PGRVMQAIRR SGSKNPVLLL DEIDKLGKDV
RGDPASALLE VLDPEQNCQF SDHYLHVPFD LSKALFICTA NRMSSIPAPL LDRMEVIELP
GYTLDEKAHI ATRHLIPKQL KEHGLVPQNL DIPSDIVQTI IQRYTREAGV RNLEREIAAV
CRATAVRIVQ ASTTAPASVG SHPASPTDSV QPLVVDDALL EDVLGAPKFD DEIHERVSVP
GVATGLVWTA NGGGILFVEA TSMGGKGRLT LTGQLGDVIK ESAQIALTWL KAHATALPPN
SPAVFPTSAQ PGTAVVRNLL ENTDIHVHFP AGAIPKDGPS AGITLVTVMV SLMSGKVVRA
DTAMTGEVTL SGLVLPVGGI KEKVIAAHRA GIKRVILPHR NSKDLAEIPA TVKSSLDIVL
VKTVQEVLDA AFDGGSPLVG VFSSRL
//
