ID A0A2G4SJ14_RHIZD Unreviewed; 1007 AA.
AC A0A2G4SJ14;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Putative Metalloprotease {ECO:0000313|EMBL:PHZ08760.1};
GN ORFNames=RHIMIDRAFT_247464 {ECO:0000313|EMBL:PHZ08760.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ08760.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ08760.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ08760.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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DR EMBL; KZ303862; PHZ08760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4SJ14; -.
DR STRING; 1340429.A0A2G4SJ14; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000242254; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PHZ08760.1};
KW Metalloprotease {ECO:0000313|EMBL:PHZ08760.1};
KW Protease {ECO:0000313|EMBL:PHZ08760.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242254}.
FT DOMAIN 54..135
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 192..374
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 1007 AA; 113739 MW; F208E9E38C47F13B CRC64;
MSSFKEICTV PTNFGVTFTK LKSDKTGLTV VLADVEAPIV NGYFALATEA FDDFGCPHTL
EHLIFLGSEQ YPYKGVLDSL ANRAFAQGTN AWTDVDHTCY TILTAGPKGF LNLLPIYLDH
ILYPTLTDSG FYTEVHHING KGENAGVVYS EMQGYQCTGD ERIHHRMQQL MYPETCGYRS
VTGGLMERLR EISVDQIRQY HKSYYRPDNL CLIITGKVDK DELLKALEPV EESIIKKGPL
PEMQRPWVST GNFPNLEKNI EDTVLFADED ESMGTLLIAW NGPMCNDFLS QKELEVLNVY
LTDSSVSVLQ KEFVETEDPL CTDVDFYISD HLKSTLTFTA SSVPIEEMER LPVEFFKTLN
RLVEEEDIDM KRMATVIEKE ILQLLKSAET DAHDTAAAVA VFDFLYGSPD GDSLKESVKD
VEYLNALAKY STRDWLNILK KWYIDAPHII LYGKPSAEFA KQQSEEESQR VEKQRADLGP
EKLKELQKRL DGATAKNDVK IPRELLESFK IPPTSSIRFI DVVTARNNET SINKVQDYIN
QDNEADVPLF IQYDHVKSQF VSLSAYICGS SVPDHLLPYT RLFLQAIFSL PIEKDGKLIS
YEDVVKGLEE DTILYKADLG TNYYRFKELV SIKLKGKISK FENIVQWLKD ILWNTRFTAE
RIKIVATQIL SDIPQAKRDG YSMTDSAMKA LELDPKKSLY ASYNILYQSE FLQNVIDRLE
KNPESVLAEL NEYRAALCAP ENIRIHVISD VLKLENPRSV FKKLAPKKVI GPPTPITLAK
DVMSFAGKTP GNQGLLVSLP AIESSYSYHS TKGPSKFDDP DIAPTLVLME LLDSMEGIFW
KFIRGKGLAY STKVYNNIEL GSIYFTIYNS PDAFKAFEQA KLVIEQLCDG RMDIDPSAVD
GARSAVIYSL VYEEGIMERA ARLSFEYQVL MGMPASYNHD MMAAVQNVTM DDLQRVLNKY
FMNLFKPDAS NVVTVSSPSK VADIQQGFQS LGFNMKTIGL NDIKLNL
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