ID I1C562_RHIO9 Unreviewed; 515 AA.
AC I1C562;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIE83592.1};
GN ORFNames=RO3G_08297 {ECO:0000313|EMBL:EIE83592.1};
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:EIE83592.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE83592.1, 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:PIRSR634015-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; CH476737; EIE83592.1; -; Genomic_DNA.
DR AlphaFoldDB; I1C562; -.
DR STRING; 246409.I1C562; -.
DR MEROPS; M01.004; -.
DR VEuPathDB; FungiDB:RO3G_08297; -.
DR eggNOG; KOG1047; Eukaryota.
DR InParanoid; I1C562; -.
DR OMA; FPGNHHP; -.
DR OrthoDB; 443480at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd09599; M1_LTA4H; 1.
DR Gene3D; 3.30.2010.30; -; 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; IPR034015; M1_LTA4H.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634015-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 25..201
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 238..434
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 384
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 515 AA; 57533 MW; A1976BDC6E96326A CRC64;
MCVPAATIDL STQANIDQVK TTHVHLNWNV DFVGQILFGN VVLNLITLVD QVDKVILDTS
YLNIQSVSLE EHDLKFTVAE RYASLGSALT IDLPKAVATS GTKFQIKIKY ATTEKCTAVQ
FLQPEQTLGK KHPYLFSQSE PIHGRAMIPC QDSPSIKVTY SASVTSPLPV VMSALRTGDE
EAGDGLKTYH FEQRTTIPSY LIAIAVGNLV GREIGPRSTV WCEPQMIEQA AWEFSDTESF
IATGEALLTP YEWGRYDLLV LPPSFPYGGM ENPCLTFVTP TLLAGDKSAV NVIAHEIAHS
WMGNLVTTNS WKHYWLNEGW TVFIERKILG RLHGEATRQF EALSGLKALK ESVDLFGSDS
PKTVLNPDLR EGADPDDFFS KVPYEKGFNF LYQIEKVVGG PSVFEPYMKA YVENFASTSI
STEDWKNFLF QYMEKVHGPS MIEKLNTIDF DAWINQPGMP PVDNAFDTTL ADACLDLADR
WNKARDEQSL AQFSSKDTVH PCLTMRSSRW THSIN
//
