ID   A0A0K9Q3G9_ZOSMR        Unreviewed;       468 AA.
AC   A0A0K9Q3G9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   03-MAY-2023, entry version 24.
DE   SubName: Full=Aspartyl aminopeptidase, putative, expressed {ECO:0000313|EMBL:KMZ75010.1};
GN   ORFNames=ZOSMA_11G00310 {ECO:0000313|EMBL:KMZ75010.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ75010.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMZ75010.1}.
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DR   EMBL; LFYR01000216; KMZ75010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9Q3G9; -.
DR   STRING; 29655.A0A0K9Q3G9; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF16; ASPARTYL AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  51852 MW;  5FAF864C91283D4E CRC64;
     MAAANSVASD FLDFLNASPT AFHAVDEAKK RLKKEGYEQL SERDDWSLEA GKKYFFARNH
     STIIAFAIGK RFVAGNGFHI VGAHTDSPCL KVKPNSKITK GGYVEVGVQT YGGGLWHTWF
     DRDLTVAGRV IVKSENDGSI QYSNKLVRMR EPILRIPTLA IHLDRNVSES FKFNNQAHLL
     PVLATSVKAE LQKQTEENDC RNDKNHHSIL MQLISNQVNS KSTEICDFEL QICDTQPSVF
     GGSQKEFIFS GRLDNLCMSF CSLKALIDST SSENCLDSEP GVRMVALFDN EEVGSNSAQG
     AGSPVLLDAL TRVTESFSSP NSKVLLKAIQ KSFIVSADMA HALHPNYMDK HEEHHQPKLH
     GGLVIKHNAN QRYATSMVTA MIFREIAKQH NLPIQDFVVR NDMPCGSTIG PILASGIGIR
     TVDVGAPQLS MHSIREMCAV DDVKHSYEHL KAYFEDFSLI DAKIHSEA
//