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Database: UniProt
Entry: A0A5D0NNZ1_9ACTN
LinkDB: A0A5D0NNZ1_9ACTN
Original site: A0A5D0NNZ1_9ACTN 
ID   A0A5D0NNZ1_9ACTN        Unreviewed;       418 AA.
AC   A0A5D0NNZ1;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Insulinase family protein {ECO:0000313|EMBL:TYB46187.1};
GN   ORFNames=FXF69_12940 {ECO:0000313|EMBL:TYB46187.1};
OS   Actinomadura chibensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=392828 {ECO:0000313|EMBL:TYB46187.1, ECO:0000313|Proteomes:UP000323380};
RN   [1] {ECO:0000313|EMBL:TYB46187.1, ECO:0000313|Proteomes:UP000323380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14158 {ECO:0000313|EMBL:TYB46187.1,
RC   ECO:0000313|Proteomes:UP000323380};
RA   Songsumanus A., Kuncharoen N., Kudo T., Yuki M., Igarashi Y.,
RA   Tanasupawat S.;
RT   "Actinomadura sp. nov. CYP1-5 isolated from mountain soil.";
RL   Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TYB46187.1}.
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DR   EMBL; VSFG01000002; TYB46187.1; -; Genomic_DNA.
DR   RefSeq; WP_067895231.1; NZ_VSFG01000002.1.
DR   AlphaFoldDB; A0A5D0NNZ1; -.
DR   STRING; 1220554.GCA_001552135_04767; -.
DR   Proteomes; UP000323380; 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; 2.
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:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
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:UP000323380};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          17..143
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          175..349
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          214..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  44724 MW;  E474AF266F5429F1 CRC64;
     MAEQPLHEHT LGNGLRVVVC EDHVVPLAAV NIWYGVGSRH ERAGRTGLAH LFEHLMFQGS
     ANVAEGEHAA LLESAGAAFN ASTSFERTNY YETVPVSHLE LALWLEADRM GTLPAALTQA
     NLDNQRDVVK NERRQRYDNQ PYGTAFERLC DLTFPAGHPY AHTPIGSMED LDATTLEDCA
     DFFATWYAPG NAVLSVVGDV DPAKTIEAVE RYFGGLPTGP EKPPTRPGEL GPLSGVREEA
     LDEEVPSPAY FAMFTLPTDG GDDVEAAELA VEILGGGSGS RLYDRMVRRD EIATEVWAGV
     TRLASGPSLA IVDAIGPEPD KIAAVLDEEL ERFAADGPDA DETARATAQA ERGFLEQTET
     VTGLANALSQ NATQFDDPAR VFTAPGRAAA VTGDAIKEMA GRWLAPGART ALTYGGTS
//
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