ID I1BSD4_RHIO9 Unreviewed; 539 AA.
AC I1BSD4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=RO3G_03819 {ECO:0000313|EMBL:EIE79114.1};
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:EIE79114.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE79114.1, 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 -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000256|ARBA:ARBA00002123}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CH476733; EIE79114.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BSD4; -.
DR STRING; 246409.I1BSD4; -.
DR VEuPathDB; FungiDB:RO3G_03819; -.
DR eggNOG; KOG2067; Eukaryota.
DR InParanoid; I1BSD4; -.
DR OMA; LKYHHSP; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT DOMAIN 67..213
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 220..444
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 539 AA; 59270 MW; 49F522A1C25A0DF9 CRC64;
MTSRILTAPL KNPLYKKAIS SVLKRSESTF SQNAEKITVN GFPTIVQEYS KASTGLCKIT
TLPNGIRVTS ENTPGHFSAV GVYVDAGSRY ETAKVRGVSH ILDRLAFKST KNRSADEIVA
ELESLGGNIM CSSSRESIMY QSAIFSQDLS RVLSLFSDVV CHPTIDPLEV EEQRQTAMYE
IEEIWSKPEM ILPEILHTAA YKGNTLGNPL LCPPENLQTM TPELIHDYKN TWYRPERMVI
AACGTEHEQV VDLAMRYFGD IPKSKENLDS VMTHLEILKK QQKPAKSSLI STLLSSSGKT
PLEIATQPAH YTGGMEFLEL EYEAPLNHVY VAFEGVSIDD PDIYALTTLQ ILLGGGGSFS
AGGPGKGMYS RLFTNVLNQH YWVESCQAFN HCYTDSGLFG IAGSCQPEYT NALVEVICRE
LDTVARSGRW GVTDVELNRA KNQLKSSLLM NLESRMVQLE DLGRQVQVHG KKTGIDEMLA
KIDQVDMDEL RRVASRVVRG AVSVTSGGTG RATIVAQGNL AGVTDFNKVV EKYGLGSGK
//
