ID   V7CFZ1_PHAVU            Unreviewed;      1247 AA.
AC   V7CFZ1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHAVU_002G040800g {ECO:0000313|EMBL:ESW29069.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW29069.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; CM002289; ESW29069.1; -; Genomic_DNA.
DR   RefSeq; XP_007157075.1; XM_007157013.1.
DR   AlphaFoldDB; V7CFZ1; -.
DR   STRING; 3885.V7CFZ1; -.
DR   MEROPS; M16.004; -.
DR   EnsemblPlants; ESW29069; ESW29069; PHAVU_002G040800g.
DR   GeneID; 18636894; -.
DR   Gramene; ESW29069; ESW29069; PHAVU_002G040800g.
DR   KEGG; pvu:PHAVU_002G040800g; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   OMA; VEIHCSN; -.
DR   OrthoDB; 1087103at2759; -.
DR   Proteomes; UP000000226; Chromosome 2.
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; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF33; STROMAL PROCESSING PEPTIDASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
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:UP000000226};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          198..330
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          349..583
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          914..1138
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          135..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1247 AA;  139132 MW;  112F35FE128E277F CRC64;
     MAMAMAASTS TSLSVVGSGL AFPHHHLNPP APSSTRFRTQ FRNNSLFLSS LPSERRRLKA
     LCGGLGLRRN KPRGHAFGVG EPSFLLPQQS CASCCLARKR RSNLATFVPG AFLDKSCFRL
     SNSKLHRSTV QIPRATVGPD EPHAASTTWP DGIAEKQDSS VYDNELERIE GFLSSELPSH
     PKLHRGQLKN GLRYLILPNK VPPKRFEAHL EVHAGSIDEE EDEQGIAHMI EHVAFLGSKK
     REKLLGTGAR SNAYTDFHHT VFHIHAPTST KDSDGDLLPF VLDALNEIAF HPKFLASRIE
     KERRAILSEL QMMNTIEYRV DCQLLQHLHS ENKLSKRFPI GLEEQIKKWD ADKIRKFHER
     WYFPANATLY IVGDIDNISK TVYQIEAVFG QTGVDNEKGS VATPSAFGAM ASFLVPKLSV
     GLGGNSIERS VMDQSKIFNK ERQAVRPPVK HNWSLPGSGA DLKAPQIFQH ELLQNFSINM
     FCKIPVNKVQ TYRDLRQVLM KRIFLSALHF RINTRYKSSN PPFTSVELDH SDSGREGCTV
     TTLTITAEPK NWHNAIRVAV QEVRRLKEFG VTQGELTRYL DALLKDSEHL AAMIDNVSSV
     DNLDFIMESD VLGHKVMDQR QGHESLLAVA GTVTLEEVNS VGAKVLEFIA EFAKPTAPLP
     AAIVACVPKN VHIEGAGETE FKISSTEITD AIKAGLDEPI QPEPELEVPK ELIQSSKLEE
     LKKLRKPAFI PVNPEADSTK LLDEETGITQ RRLSNGIPVN YKISKTETQS GVMRLIVGGG
     RAAESSDSRG SVIVGVRTLS EGGRVGNFSR EQVELFCVNH LINCSLESTE EFISMEFRFT
     LRDNGMRAAF QLLHMVLEHS VWVDDAFDRA RQLYLSYYRS IPKSLERSTA HKLMVAMLDG
     DERFIEPTPK SLENLTLQSV KDAVMNQFFG DNMEVCIVGD FTEEDIESCI LDYLGTAQAT
     RNHGREQEFN PPIFRPSPSE LQFQEVFLKD TDERACAYIA GPAPNRWGFT VDGKYLLESI
     NNASTTNDDQ SNSDAQQTQG LQKSLRGHPL FFGITMGLLS EIINSRLFTT VRDSLGLTYD
     VSFELNLFDR LKLGWYVISV TSTPSKVHKA VDACKNVLRG LHSNKITERE LDRAKRTLLM
     RHEAEIKSNA YWLGLLAHLQ ASSVPRKDLS CIKDLTFLYE VATIEDIYLA YEQLKVDENS
     LYSCIGIAGA QDAQDIAAPI EEEVAGDVYP GVIPVGRGLS TMTRPTT
//