ID A0A372RRF5_9GLOM Unreviewed; 878 AA.
AC A0A372RRF5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=C1646_732775 {ECO:0000313|EMBL:RGB43191.1};
OS Rhizophagus sp. MUCL 43196.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB43191.1, ECO:0000313|Proteomes:UP000263633};
RN [1] {ECO:0000313|EMBL:RGB43191.1, ECO:0000313|Proteomes:UP000263633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB43191.1,
RC ECO:0000313|Proteomes:UP000263633};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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:RGB43191.1}.
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DR EMBL; QKKE01000012; RGB43191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372RRF5; -.
DR STRING; 1803374.A0A372RRF5; -.
DR InParanoid; A0A372RRF5; -.
DR Proteomes; UP000263633; 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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
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; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
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:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 17..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..450
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 527..855
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 391
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 878 AA; 100011 MW; 00D2CCFE1FD13D90 CRC64;
MSKEEDKRVL LPTNVRPTHY TLTITPDLVN FTFKGSEVVN LNINENTNVI TLHANDIEIK
SAKLVNSALK TNQGFRTVNI AKNAETQTVT LTFPQEISAK TTATLHIEYT GILDDKMLGF
YRSSYKDQDG KTRYMASTQF EATEARRAFP SWDEPAIKST FDITLIVPAE MTALSNMNVV
SETRLGDGKK ELVAFVVGDL GYVESFTTGK HNGGKSVTVR VYAPKGEERH GDFALKIATD
TLEYFAEVFG IPYPLPKCDM VAIPDFEAGA MENWGLITYR TTAVLYDPKA SDAKFKQRIA
YTVSHELAHQ WFGNLVTMEW WTDLWLNEGF ATWVGYLAVD KLFPDWEIWN QYVTEGFQRG
LQLDALRSSH PIEVPVNDSS EIHQIFDAIS YYKGANVIRM LSAFLGEKVF LSGVKRYLMR
HKFSNASTDD LWKALTEESG NDVSKFMTLW TKMAGHPVLT VEEPGNTLKI RQCRFLSSGV
ASPEEDNTVW WVPLGVDLGP TETHHEIRSV VLTQKEMTLV LPEKYDFYQL NARKTGVFRV
NYTPERLSKL GQAVKKGLLG TSDRIGIMAD AGALAASGYG KTSGLLNFIK NFEDEEQYIV
WIEINSRLSN LLNVWFEQPD HIYQGLLKFQ RQLVSKLVAK LGWEYSDNDD YLTTMLRSLV
IKMAGRANDP DTVKEAHRKF HSFTKRNEES ALHPNIRGVV FEIVLSYGGG NEEFDSILKY
YSEARTADQK VVALTGLGFA QSDELIQRAL KFSTSEEVRN QDIIYAFNGL QSNRKSRRAL
WNFVKENFYM VRLILFDLLH ERYAKSLALF EHIIKFGTEL FASEDDIKDV EKFFSNKNCK
EFERPLQQSI ENIRANAAWV ERDAKDVEEW LKINGYIQ
//
