ID A0A0L9VSM4_PHAAN Unreviewed; 1015 AA.
AC A0A0L9VSM4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan11g090000 {ECO:0000313|EMBL:KOM57867.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM57867.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003381; KOM57867.1; -; Genomic_DNA.
DR RefSeq; XP_017442338.1; XM_017586849.1.
DR AlphaFoldDB; A0A0L9VSM4; -.
DR STRING; 3914.A0A0L9VSM4; -.
DR EnsemblPlants; KOM57867; KOM57867; LR48_Vigan11g090000.
DR Gramene; KOM57867; KOM57867; LR48_Vigan11g090000.
DR KEGG; var:108347539; -.
DR OMA; ICYKCTD; -.
DR OrthoDB; 448605at2759; -.
DR Proteomes; UP000053144; Chromosome 11.
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: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; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 55..172
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 210..390
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 695..879
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 1015 AA; 114009 MW; BE4C05F7D50AEA3E CRC64;
MELLPAAVPP ISKKQGFRSL KLVNADMEQL LSDQPVGVDY GTLDNGLRYY VRCNSKPRMR
AALALAVRAG SILEEEDERG VAHIVEHLAF SATKKYTNHD IVKFLESIGA EFGACQNAVT
SADDTVYELL VPVDKPELLS QAISVLAEFS SEIRVSKDDL AKERGAVMEE YRGSRNATGR
LQDAHWMLMM EGSKYAERLP IGLEKVIRTV SSETVKHFYK KWYHLCNMAV IAVGDFSDTQ
DVVELIKTHF GQKIPDPDPP LIPTFQVPSH DEPRFSCFIE SEAAGSAVMI SYKTPVDELK
TVKDYRNLLA ESMFLYALNQ RFFKIARRND PPYFSCSAAA DVLVRPLKAN IMTSSCKRKG
TIEALESMLI EVARVRLHGF SDREISVVRA LLMSEIESAY LERDQIQSTS LRDEYLQHFL
HAEPVVGIEY EAQLQKTLLP HISTSEISKC SEKLRTSCSC VIKTIEPQPF AVLDDLKNVV
KKVNLMEEEG RISYWDDEHV PEEIVTTKPN MGHVVQELEY SNIGATELVL SNGMRICYKR
TDFLDDQVIF TGYSYGGLSE LPESEYFSCS MGPTIAGEIG VFGYRPSVLM DMLAGKRAEV
GTKIGAYMRT FYGDCSPSDL ETALQLVYQL FTTNLTPGEE DVKIVMQMAE EAVSAQDRDP
YTAFTNRVKE LNYGNSYFFR PIRKSDLQKV DPRKACEFFS TCFKDPSTFT VVIVGNIDPA
IAMPLILQYL GGIPKPPEPI MHFNRDELKG LPFNFPTEIH REVVRSPMVE AQCLVQICFP
VELRNGTMVE EIHFVGFLSK LLETKIMQVL RFKHGQIYSV GVSVFLGGNK PSRIGDVRGD
VSINFSCDPD ISSKLVDIAL DEMLRLQEEG PSGQDVSTIL EIEQRAHENG LQENYYWLDR
ILHSYQSRVY AGDVGISFEV QDEGRSKVRS SLTPSTAQLA LKRILPFPCK NKYTVVILMP
KSSPFKLLKS VFQSARTNYG KEAKILAGVA SLAVLAFSLW RQGRSNSRLL SRAVN
//