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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//