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Database: UniProt
Entry: R1FRX5_EMIHU
LinkDB: R1FRX5_EMIHU
Original site: R1FRX5_EMIHU 
ID   R1FRX5_EMIHU            Unreviewed;       956 AA.
AC   R1FRX5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:EOD38401.1};
GN   ORFNames=EMIHUDRAFT_471473 {ECO:0000313|EMBL:EOD38401.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD38401.1};
RN   [1] {ECO:0000313|EMBL:EOD38401.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD38401.1};
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:EOD38401}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; KB864032; EOD38401.1; -; Genomic_DNA.
DR   RefSeq; XP_005790830.1; XM_005790773.1.
DR   STRING; 2903.R1FRX5; -.
DR   MEROPS; M16.A09; -.
DR   PaxDb; 2903-EOD38401; -.
DR   EnsemblProtists; EOD38401; EOD38401; EMIHUDRAFT_471473.
DR   GeneID; 17283672; -.
DR   KEGG; ehx:EMIHUDRAFT_471473; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   OMA; VGHQWLE; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..956
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014593153"
FT   DOMAIN          66..199
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          226..314
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          405..690
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
SQ   SEQUENCE   956 AA;  103739 MW;  1EEA68A7ECF9FDFF CRC64;
     MRAATESASR RALLSLCSAL LATPTPSPAA AAAAAAAARG LQTFDIAASD LDRRSFRGMQ
     LSNGLRVLLC SDPEAGKAAA SMNVAVGSMS NPVEWPGLAH FCEHMLFLGT KRFPGEGEFE
     RFIAANAGSN NAFTGSEETN YFFSVNGDAL PGALTRFADF FTAPLFSESG TTREVDAIDA
     EHAKNLQSDF WRSDAVLRLR ARPDHPYSRF FTGNRQTLRG GDADARAALF AFHRAFYRAP
     QMALAVAGPQ SLDALQRLVQ ANFGALPPGP APPASAAYDA LPPPFDTQPQ AEPPVATVLV
     PVREQRSVTV TWCLPVEDPD EWWRAKPDST VLLKAKGLAS SVDGSIDEFT RSFVVLTAYI
     GLTPQGLQRW PEVVSALFSY LALLREEGVP PHVYAEERRM RELAFAFAEP APPSSFVQSA
     SGNLFLFPPR EWLRGPLLAG EGAEPLVRSI LEGLTPQAAV VKLTARELAP LATRVEPVYS
     ASYGEMPIGR EVAAWSAAPR LDGLAVPPPN RFIPTDLSIK ALSIKARGAS TAQGGGGAAR
     RVKPALLLNT DSDERFGRPK AFAFVSLRTP QLYESAAAAA QAELYAALLS DALQDVTYQA
     ARAGLSAGAS VGWQGLSLSL SGYDQRLPEL AALVADSLRT FDVAPLAFER QRDGLLRQLR
     GADKRQPVEQ AAYRRNLALE TPRYTNEQLA AGLEKATLPQ VLGLQRRLLP EVEVEALLCG
     NVAEGQATQL VLKLLNALGS RPLPVARRPV RRVRVLPAGE RTLQQFVAAS QAEVNSATEV
     YFQVGGDEAD DWVLLTLLSQ LMQQLGYIVQ CSANEIDGVR GLSFLVQSKV AAPEAVEERI
     EAFLRLFRGT LLLLGEAEVQ SYAASIAAQF TDAGRLWAEC TRRRYDFERP WRSAEKVKRL
     TREQLIAFFD RHVASGSPTR RQLSTHVYAQ SMAPPQLRVQ LPGDDFYPAP RDLLLV
//
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