ID A0A2H5SD48_RHIID Unreviewed; 882 AA.
AC A0A2H5SD48;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=GLOIN_2v1541065 {ECO:0000313|EMBL:POG78008.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:POG78008.1, ECO:0000313|Proteomes:UP000018888};
RN [1] {ECO:0000313|EMBL:POG78008.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=24277808; DOI=10.1073/pnas.1313452110;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei Dit Frey N., Gianinazzi-Pearson V.,
RA Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M.,
RA Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E.,
RA Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P.,
RA Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G.,
RA Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young P.W.,
RA Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N.,
RA Roux C., Martin F.;
RT "Genome of an arbuscular mycorrhizal fungus provides insight into the
RT oldest plant symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013).
RN [2] {ECO:0000313|EMBL:POG78008.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=29355972;
RA Chen E.C.H., Morin E., Beaudet D., Noel J., Yildirir G., Ndikumana S.,
RA Charron P., St-Onge C., Giorgi J., Kruger M., Marton T., Ropars J.,
RA Grigoriev I.V., Hainaut M., Henrissat B., Roux C., Martin F., Corradi N.;
RT "High intraspecific genome diversity in the model arbuscular mycorrhizal
RT symbiont Rhizophagus irregularis.";
RL New Phytol. 0:0-0(2018).
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:POG78008.1}.
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DR EMBL; AUPC02000035; POG78008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5SD48; -.
DR STRING; 747089.A0A2H5SD48; -.
DR VEuPathDB; FungiDB:GLOIN_2v1541065; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000018888; 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:UP000018888};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 17..204
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 245..462
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 539..859
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 403
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 882 AA; 100327 MW; B7D0CF7067C0973A CRC64;
MSKEEDKRVL LPTNVRPTHY TLTITPDLVN FTFKGSEVVN LNINENTNVI TLHANDIEIK
SAKLVNSALK TNQGFRTVNI AKNAETQTVT LTFPQEISAK TTATLHIEYT GILDDKMLGF
YRSSYKDQDG KTRYMASTQF EATEARRAFP SWDEPAIKST FDITLIVPAE MTALSNMNVV
SETRLGDGKK EVKFARTPIM STYLVAFVVG DLGYVESFTT GKHNGGKSVT VRVYAPKGEE
RHGDFALKIA TDTLEYFAEV FGIPYPLPKC DMVAIPDFEA GAMENWGLIT YRTTAVLYDP
KASDAKFKQR IAYTVSHELA HQWFGNLVTM EWWTDLWLNE GFATWVGYLA VDKLFPDWEI
WNQYVTEGFQ RGLQLDALRS SHPIEVPVND SSEIHQIFDA ISYYKGANVI RMLSAFLGEK
VFLSGVKRYL MRHKFSNAST DDLWKALTEE SGNDVSKFMT LWTKMAGHPV LTVEETGNTL
KIRQCRFLSS GVASPEEDNT VWWVPLGVDL GPTETHHEIG SVVLTQKEMT LVLPEKYDFY
QLNARKTGVF RVNYTPERLS KLGQAVKKGL IGTSDRIGIM ADAGALAASG YGKTSGLLNF
IKNFEDEEQY IVWIEINSRL SNLLNVWFEQ PDHIYQGLLK FQRQLVSKLV AKLGWEYSDN
DDYLTTMLRS LVIKMAGRAN DPDTVKEAHR RFHSFTKRNE ESALHPNIRG VVFEIVLSYG
GGNEEFDSIL KYYSEARTAD QKVVALTGLG FAQSDDLIQR ALKFSTSEEV RNQDIIYAFN
GLQANRKSRR ALWNFVKENF YMLHERYAKS LALFEHIIKF GTELFASEDD IKDVEKFFSN
KNCKEFERPL QQSIENIRAN AAWVERDAKD VEEWLKTNGY IQ
//
