ID R0HXL8_9BRAS Unreviewed; 561 AA.
AC R0HXL8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CARUB_v10013366mg {ECO:0000313|EMBL:EOA30245.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA30245.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; KB870807; EOA30245.1; -; Genomic_DNA.
DR RefSeq; XP_006297347.1; XM_006297285.1.
DR AlphaFoldDB; R0HXL8; -.
DR STRING; 81985.R0HXL8; -.
DR MEROPS; M16.003; -.
DR eggNOG; KOG0960; Eukaryota.
DR Proteomes; UP000029121; 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:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 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:UP000029121}.
FT DOMAIN 107..254
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 310..476
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 18..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 62544 MW; 1530CFB5C1E10E70 CRC64;
MAMKNLLSLA RRSQRRLSLN QVTRSSSSFS AIDSAPASTS PATPSPPPPH LMPYDHAAEL
IKNKIKKLEN PDKRFLKYAS PIPILASHNH ILSAPETRVT TLPNGLRVAT ESNLSAKTAT
VGVWIDAGSR FESDETNGTA HFLEHMIFKG TGKRTVRALE EEIEDIGGHL NAYTSREQTT
YYAKVMDSNV NQALDVLADI LQNSKFEEDR INRERDVILR EMQEVEGQTD EVVLDHLHAT
AFQYTPLGRT ILGPAQNVKS ITREDLQNYI KTHYTASRMV LILVTSYHFL QSAIEFVRIL
MLAYPKYIQV IAAAGAVNHE EVVEQVKKLF TKLSSDPTST SQLVANEPAS FTGSEVRMID
DDLPLAQFAV AFEGASWTDP DSVALMVMQT MLGSWNKNVG GGKHVGSDLT QRVAINEIAE
SIMAFNTNYK DTGLFGVYAV AKADCLDDLS YAIMYEVTKL AYRVSDADVT RARNQLKSSL
LLHMDGTSPI AEDIGRQLLT YGRRIPIAEL FARIDAVDAS TVKRVANKYV YDKDIAISAI
GPIQDLPDYN KFRRRTYWNR Y
//