ID A0A2C9W258_MANES Unreviewed; 504 AA.
AC A0A2C9W258;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAY53095.1};
GN ORFNames=MANES_04G135300 {ECO:0000313|EMBL:OAY53095.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY53095.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY53095.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY53095.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CM004390; OAY53095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9W258; -.
DR STRING; 3983.A0A2C9W258; -.
DR EnsemblPlants; OAY53095; OAY53095; MANES_04G135300.
DR Gramene; OAY53095; OAY53095; MANES_04G135300.
DR OMA; LKYHHSP; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000091857; Chromosome lg4.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:SF203; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA-1, MITOCHONDRIAL-RELATED; 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:UP000091857}.
FT DOMAIN 86..232
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 243..421
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 504 AA; 54713 MW; 3ABC56A04B20D786 CRC64;
MYRTAGSRLR ALKSYAGILG ATRYATSSAV ASTTSSPGFF SWLTGEHSAS LSPLDSPIPG
VSLPPPLPDY VEPSKVKSKT LENGFRIVSE ASPNPAASIG LYLDCGSIYE TPLSCGATHL
LERMAFKSTR NRSHLRIVRE VEAIGGSVAA SASREQIAYT FDALKTHVPE MVELLIDSVR
NPVFLDWEVN EELKKIKDEL GQLSNNPQGL LLEAIHSAGY SGALANPLLA PESALNRLDS
VILEEFVSEH YTPSRMVLAA SGVELEEIIS VAEPLLSDLP LVQRPEEPKS LYVGGDYRRQ
ADSPMTHVAL AFEVPGGWHN EKEAIVLTVL QMLMGGGGSF SAGGPGKGMH SRLYLRVLNE
YHQLQSFSAF NSIFNKTGLF GIYASTTSDF VAKAVDVAVG ELIAIAQPGQ VTKLQLDRAK
ESTRSAVLMN LESRMIVTED IGRQFLTYGE RKPVEHFLKA LDEITAKDIT NIAQKMLSSP
LTMASYGDVV NVPSYEYVSS KFHA
//
