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Database: UniProt
Entry: G6FMD0_9CYAN
LinkDB: G6FMD0_9CYAN
Original site: G6FMD0_9CYAN 
ID   G6FMD0_9CYAN            Unreviewed;       426 AA.
AC   G6FMD0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Processing peptidase {ECO:0000313|EMBL:EHC19210.1};
DE            EC=3.4.24.64 {ECO:0000313|EMBL:EHC19210.1};
GN   ORFNames=FJSC11DRAFT_0027 {ECO:0000313|EMBL:EHC19210.1};
OS   Fischerella thermalis JSC-11.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Fischerella.
OX   NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC19210.1, ECO:0000313|Proteomes:UP000004344};
RN   [1] {ECO:0000313|EMBL:EHC19210.1, ECO:0000313|Proteomes:UP000004344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-11 {ECO:0000313|EMBL:EHC19210.1,
RC   ECO:0000313|Proteomes:UP000004344};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA   Woyke T.J.;
RT   "The draft genome of Fischerella sp. JSC-11.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:EHC19210.1}.
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DR   EMBL; AGIZ01000001; EHC19210.1; -; Genomic_DNA.
DR   RefSeq; WP_009453688.1; NZ_AGIZ01000001.1.
DR   AlphaFoldDB; G6FMD0; -.
DR   GeneID; 60764311; -.
DR   PATRIC; fig|741277.3.peg.30; -.
DR   Proteomes; UP000004344; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 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   Hydrolase {ECO:0000313|EMBL:EHC19210.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004344}.
FT   DOMAIN          27..169
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          177..358
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   426 AA;  48136 MW;  7F6368D1142AB781 CRC64;
     MTSTLVKFPR LNAPKLHRLP NGLTIIAEQM PIDAVNLSLW INVGSAVEAD AINGMAHFLE
     HMIFKGTEQL ISGEFERRIE ERGAVTNAAT SQDYTHYYIT TAPKDFADLA PLQIDVVANA
     SIPDDAFERE RLVVLEEIRR SEDNPRRRTY KRAMEMAFAQ LPYRRPVLGA EEVISHLKPQ
     QMRDFHASWY QPPSITAVAV GNLAVEELIE IIAEGFSKSH NHQSTINKQP PKFVCELPFS
     EIVRQEFTDE SLQQARLVMV WRVPGLDKLD ETYALDVLAA ILGHGRTSRL VRELREERGL
     ASHISVSNMT HKLQGTFYIS AHCPVENLGL VEEAIAQHIR TLQTEFVQES EIARVRKRVA
     NRFIFGNETP SDRAGLYGYY QTLIGDLEPA FDYPSHIEAQ DATKLMQAAQ KYLTPNAYGV
     VVMKPV
//
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