ID I1BI00_RHIO9 Unreviewed; 938 AA.
AC I1BI00;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=RO3G_00534 {ECO:0000313|EMBL:EIE75830.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE75830.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE75830.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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}.
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DR EMBL; CH476732; EIE75830.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BI00; -.
DR STRING; 246409.I1BI00; -.
DR MEROPS; M01.A25; -.
DR VEuPathDB; FungiDB:RO3G_00534; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; I1BI00; -.
DR OMA; MMEYVAI; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000009138; 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; 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 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|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634016-3,
KW ECO:0000256|RuleBase:RU364040};
KW Metalloprotease {ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW Zinc {ECO:0000256|PIRSR:PIRSR634016-3, ECO:0000256|RuleBase:RU364040}.
FT DOMAIN 19..190
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 297..513
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 585..913
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 454
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 938 AA; 105770 MW; E767404D0E227E2B CRC64;
MCTSSVDNPN RQVLPTNVKP THYDLTLEPN LKTFKFDGQV KVNLNVNEDT TTIVLNTRDI
KIKSAFLSSE GLKTDSKQAA IDIKYDEKKD LATLSFKEVV VANTKALLEI YFEGELNDQM
AGFYRSSYKD VDGNTQYLAT TQFESTDARR AFPCWDEPSL KATFDVTLIV PAHLVALSNM
DVISEEPFNE KYSLHGKTET GKFEGKTEAG KFEGKIEAGK VEGKTEIGKV EGKTETKSTS
LKQVKYSTTP LMSTYLLAFC VGPFEYIEAF TSGEYNGKPI RSRVYTLPGS VEQGRHALNV
CTLALEYFAK VFGEPYPLPK VDMIAIPDFE AGAMENWGLI TYRTVALLFD EKSSSIAFKK
STAYTVCHEL AHQWFGNLVT MEWWDHLWLN EGFATWVGWL AVDQIFPDWE VWTSFVNEDM
PRALNLDALR SSHPIEVTVN DPAEIHQIFD AISYYKGASV IRMLSSWLGV DTFLAGVRRY
LRRHKLGNAS TNDLWIALSE EAKVDVSKFM TLWTRCVGYP VLTVKKTGND TINVTQSRYL
STGDLTKEED STVWWVPLGI LVSEKTESYT LTDKSQNFTI PSDGLFKLNA GQTSVYRVNY
PIETIRKLSE EIKKGKNGLL ANTSDRVGLV ADAGNLCVSG EQNTAAFLEL AQAFVNEDNY
FVWSQLSSHL SNILSVWSEQ PEEVRNGLKA LRRSLFAPVA HKLGWEFAET DDYLTNILRV
LAISNAGRSN HTETIQEAKK RFWQFVEGNT NVLHPNLRGP VYSIVLKAAE SEEEEEKVWS
EIFKIYRDEA LPSDQRLTAL SSLGGASHAH LIQKYLDMCL DERLVRGQDS IYVFRSLASN
PKARDILWKF FTDNYDVLFA KFSKSLSLFG SAVRSAVGSF VSFDKIAEVE AFFSTKDTKE
YARPLQQALE SARVNAKWIE RDEHVVAEWV HSNANNFA
//
