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Database: UniProt
Entry: A0A2V3J012_9FLOR
LinkDB: A0A2V3J012_9FLOR
Original site: A0A2V3J012_9FLOR 
ID   A0A2V3J012_9FLOR        Unreviewed;       811 AA.
AC   A0A2V3J012;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Aminopeptidase M1-D {ECO:0000313|EMBL:PXF47643.1};
GN   ORFNames=BWQ96_02622 {ECO:0000313|EMBL:PXF47643.1};
OS   Gracilariopsis chorda.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Gracilariopsis.
OX   NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF47643.1, ECO:0000313|Proteomes:UP000247409};
RN   [1] {ECO:0000313|EMBL:PXF47643.1, ECO:0000313|Proteomes:UP000247409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF47643.1,
RC   ECO:0000313|Proteomes:UP000247409};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PXF47643.1};
RX   PubMed=29688518; DOI=10.1093/molbev/msy081;
RA   Lee J., Yang E.C., Graf L., Yang J.H., Qiu H., Zel Zion U., Chan C.X.,
RA   Stephens T.G., Weber A.P.M., Boo G.H., Boo S.M., Kim K.M., Shin Y.,
RA   Jung M., Lee S.J., Yim H.S., Lee J.H., Bhattacharya D., Yoon H.S.;
RT   "Analysis of the draft genome of the red seaweed Gracilariopsis chorda
RT   provides insights into genome size evolution in Rhodophyta.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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:PXF47643.1}.
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DR   EMBL; NBIV01000022; PXF47643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3J012; -.
DR   STRING; 448386.A0A2V3J012; -.
DR   Proteomes; UP000247409; 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; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:PXF47643.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247409};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          33..205
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          245..455
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   811 AA;  92077 MW;  11146A9622B98DE1 CRC64;
     MPCGGTHLDA RLADPFTDSY AKPHYQPRLP LRPTHIALEH HFSIAERTIQ GTVTHTLVAQ
     WPGAHVITLH AEDFDQVQVT SPDDDKLSFT YDGHLIQAVF SFPLANDEKV SLVISYHVID
     PIDGVLFSIE REGHWVVSDH ETERARYWLP VIDHPSVRTT LTFKLHTPAE DNLIALANGE
     LISEQTVGSE KVSHWEMKQL TPSYLICVAI GRFVVADGGE HHGKPIKFFG VKGGRHPYTE
     EDLAFTFGRT KEMIEFMENK VHFELPWPKY YQFCVGDVGG AMENSSLVSY DEWYMLDERS
     ASERSHRVDS TVVHELAHTW FGDTVVCSDF CHSFLKESFA TLISAEWYHH KDGEEEFQST
     LTRYAEASFS ETAEYVRPIV WRSYESSWSL FDRHLYTNGA WRLHMLRNKL GNDTFWSGVS
     RYLHKRAWQT VETDDFRRDL EDYAHEELCS FFDQWFYSKG HPVLEISFSY DASKSGLATI
     TITQVQRDEK KGVGLFDITI DVAMEVGSGV WETHTLTMEN GSTFAQLVEK VPSKPLQVVI
     DPEKKVLYEI SKVNGLGDDM CVRSLAHAPT FAGRHQALEL LFQSGSRRAR AALKDALKKD
     NHWNIRSTIA KRMGNSKRKD YLEVLIDAAF TEHDARATPT ILAAIGEFRE PEAEKALLKF
     IQDGCDMMRP YGAMGMAISS LGKMRNIEHL ELITSFLEEF RKGGKSFEIP RAAAMGLGHL
     RDWKATEVLM RNSYPPNLNL PNRVRCGLLD AMAKSAVYET RGNRIKLFDF IERVCMSDEA
     KMVAMVAGRA LVSLSDVGNP IKALNELEKT S
//
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