ID A0A0C1RH79_9CYAN Unreviewed; 415 AA.
AC A0A0C1RH79;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Insulinase family protein {ECO:0000313|EMBL:KAF3887471.1};
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KIE11405.1};
GN ORFNames=DA73_0223895 {ECO:0000313|EMBL:KIE11405.1}, DA73_0400019755
GN {ECO:0000313|EMBL:KAF3887471.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE11405.1};
RN [1] {ECO:0000313|EMBL:KIE11405.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE11405.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3887471.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3887471.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) 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:KIE11405.1}.
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DR EMBL; JHEG04000001; KAF3887471.1; -; Genomic_DNA.
DR EMBL; JHEG02000048; KIE11405.1; -; Genomic_DNA.
DR RefSeq; WP_038086109.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1RH79; -.
DR STRING; 1479485.DA73_0223895; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000029738; 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: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; 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.
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:UP000029738};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 18..160
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 170..348
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 415 AA; 46853 MW; 39B976E143E9B030 CRC64;
MFSASVFKLD NSLTLIHQEI PTTPVVVADI WVRAGANVEP EPLFGMAHFL EHLIFKGTAT
LPPGVFDQKI ENQGGVTNAA TSHDYAHYSL TTASGYLKET LPYLGELLLN AAIPEDEFVR
ERDVVFEEIR QSYDDPDWIG FQSLISSIYQ QHPYGRSVLG GEEELMQTSP EIVRCFHRNH
YQPENMTVVI VGGIATEQAI EIVNNTFVDF ADRCCECPKS PKEVVEPILA GVRRQELHLP
RLEQARLLMG WTGPGVDRLR TSYGLDLLSV LLAEGRTSRL VRDLREEQQL VQGICSHFSL
QRDASLFTIT AWLEPENLER VESLIRLHLN DLQTNGMSEQ ELIRGQRLLC NDYAFSTEAP
NQLAGLYGYY NTIAQAELAV TYPHQIKSYS TQELQQLARE YLSPNHYAVT VLKPC
//
