ID A9V1S8_MONBE Unreviewed; 381 AA.
AC A9V1S8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=MONBRDRAFT_32800 {ECO:0000313|EMBL:EDQ88496.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ88496.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ88496.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CH991554; EDQ88496.1; -; Genomic_DNA.
DR RefSeq; XP_001746600.1; XM_001746548.1.
DR AlphaFoldDB; A9V1S8; -.
DR STRING; 81824.A9V1S8; -.
DR EnsemblProtists; EDQ88496; EDQ88496; MONBRDRAFT_32800.
DR GeneID; 5891796; -.
DR KEGG; mbr:MONBRDRAFT_32800; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; A9V1S8; -.
DR OMA; KYDHDAS; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
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 PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..381
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002745177"
FT DOMAIN 63..378
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 81
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 94..101
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 300..337
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 381 AA; 40718 MW; F39EFFC70A803AEF CRC64;
MMRTAVLLLA LVAAAAALSK VTLHGMERTR DSLRRQGAML TTKYQNIMAG TNVPLSNYED
AQYFGEISIG TPAQKFKVIF DTGSSNLWVP SSQCPKTNIA CDVHAKYDSS ASSTYKANGT
KFAIQYGTGS LSGFLSTDTA CIGDLCVKDQ TFAEALEEPG VTFVAAKFDG ILGMGFSTIS
VDHVVPVWYN MVQQQVVEQN MYSFYLNRNP NGVSGGELTL GGYDESHFAG PIHWTDVTVD
GYWQFTMTGL SIENTPYCTN CKAIADTGTS LLAGPTDVVK QINKAIGATT IAAGEAIVDC
NKIPHMPNVT IVINGIQYSL SAEQYVLQVT AEGETECISG FAGIDVPAPE GPLWILGDVF
IGAYTTVFDM GNNRVGFGAS A
//
