ID R1CIF0_EMIHU Unreviewed; 591 AA.
AC R1CIF0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=ATP-dependent protease La {ECO:0000313|EMBL:EOD22337.1};
GN ORFNames=EMIHUDRAFT_450768 {ECO:0000313|EMBL:EOD22337.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD22337.1};
RN [1] {ECO:0000313|EMBL:EOD22337.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD22337.1};
RG DOE Joint Genome Institute;
RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT "Genome variability drives Emilianias global distribution.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [3] {ECO:0000313|EnsemblProtists:EOD22337}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; KB865754; EOD22337.1; -; Genomic_DNA.
DR RefSeq; XP_005774766.1; XM_005774709.1.
DR STRING; 2903.R1CIF0; -.
DR PaxDb; 2903-EOD22337; -.
DR EnsemblProtists; EOD22337; EOD22337; EMIHUDRAFT_450768.
DR GeneID; 17267884; -.
DR KEGG; ehx:EMIHUDRAFT_450768; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_2_1_1; -.
DR OMA; ANCVIML; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
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: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 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; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
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 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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 365..550
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 499
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 591 AA; 63083 MW; 481C001C9A3B3585 CRC64;
MISGLISEIE RQVAREPRPK RGSAGNSSEA PVHFRIYTSK PPFPGGLPPP IGLPFMPGGP
SGGDDEDGEV PTLERRLRAA GLPAEAEEVV TRELRRLRRM SPMHSEYSTL VDYLEWMAEL
PWAPPESPQP PVPLSQARAQ LEEDHYAMDK VKQRILEFLA VCHLRGDTKG SILCMLGPPG
IGKTSLGKSV AAALGRPFHR VSVGGIHSEA EVRGHRRTYV GALPGLILQA VKKCGAANCV
IMLDEVDKLG RNSYNGDPSS ALLEVLDPEQ NGAFRDHFLA VPFNLSQAAL RLASADDGGM
HGPVIELTGY TVDDKVAIAA RHLLPKQAGV RELERKLGAV CRAIAANRVL GPPRFEPRRD
VARRITKPGI ALGLAATVFG GETLFVEVEQ VAGKGAVQMT GNIKEVMQES VKAALTWIRA
NVAELGLAKT ASEALLNTTD LHIHFPEGAT PKDGPSAGVT ITTALTSLLT GRLVRNDVAM
TGEITLRGLV LPVGGIKEKV VAAHRAGVRT VLLPQANEKD LRELPQKVLE EMQFELVSDV
REVIRAALVP ADVTEAEAAG SASGDGSEPA TDDGRQVPLS HPLPSVPTGV P
//
