ID C1N1K1_MICPC Unreviewed; 647 AA.
AC C1N1K1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEH54466.1};
GN ORFNames=MICPUCDRAFT_51434 {ECO:0000313|EMBL:EEH54466.1};
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN [1] {ECO:0000313|EMBL:EEH54466.1, ECO:0000313|Proteomes:UP000001876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH54466.1,
RC ECO:0000313|Proteomes:UP000001876};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GG663744; EEH54466.1; -; Genomic_DNA.
DR RefSeq; XP_003061836.1; XM_003061790.1.
DR AlphaFoldDB; C1N1K1; -.
DR STRING; 564608.C1N1K1; -.
DR MEROPS; A01.096; -.
DR GeneID; 9687012; -.
DR KEGG; mpp:MICPUCDRAFT_51434; -.
DR eggNOG; KOG1339; Eukaryota.
DR OMA; GVECANL; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000001876; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
DR Gene3D; 1.10.225.10; Saposin-like; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 2.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF47862; Saposin; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001876};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..647
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002912319"
FT DOMAIN 107..644
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 342..381
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 436..477
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 317
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 138..145
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 647 AA; 69521 MW; 99BCE7FB692605F3 CRC64;
MNARVVALLC ALVALLSLAS VPVAVRADDD GVDNDDDDAD AMRSSSVASS SSRLPRVSLS
KRVVDARAVH ARVVATRANE ANARLNSMYG ADADARVSIT NYMDAQYFGA VSIGTPPQSF
DVVFDTGSSN LWVPSSKCKF TQIPCDLHHK YDAKASSTHA QNGTDFAIQY GSGSLSGFLS
ADVVGWGGLE IASQTFAEAT REPGLAFMFA KFDGILGMGW DTISVDKVVP PFYNAYAQGL
VPDDVFSFWL NRDESHPDGP GGELVLGGVD PAHYVGEHAW LPVTREGYWQ VRMDDVIVDG
ASAGECDETD GCAAILDTGT SLLAGPKDVI EKINAKIGAR PILNEECRVM IEQYGEELID
DVKKFGPKAI CVSAGLCHEK TERQPPQRPA SSSPFDILGR LAKKSRARAS VTRRVLEGRR
GRLWADAAAD ADAASQPASC RACEMAVAYA QSLIKTNVTR ALILNELKSL CDHIPSKGGE
AVRRLPVRPS FVRHVSLTDT RAPDSSSKGV DCDAVDAMPD VSFVLGGKAW TLTPRQYVLR
VTSGGGGDDD DETERERADE EDADAMDEEG RGRHHHHHKR PRPPTHAPPE PPKPKPKPSA
EQCVSGFMGL DVPPPAGPLW ILGDVFIGPY HTVFDHGNAR VGIAEAR
//