ID A0A0P7YZ79_9CYAN Unreviewed; 583 AA.
AC A0A0P7YZ79;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Zn-dependent peptidase {ECO:0000313|EMBL:KPQ35718.1};
GN ORFNames=HLUCCA11_09125 {ECO:0000313|EMBL:KPQ35718.1};
OS Phormidesmis priestleyi Ana.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Phormidesmis.
OX NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ35718.1, ECO:0000313|Proteomes:UP000050465};
RN [1] {ECO:0000313|EMBL:KPQ35718.1, ECO:0000313|Proteomes:UP000050465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ana {ECO:0000313|EMBL:KPQ35718.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPQ35718.1}.
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DR EMBL; LJZR01000010; KPQ35718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7YZ79; -.
DR STRING; 1666911.HLUCCA11_09125; -.
DR PATRIC; fig|1666911.3.peg.616; -.
DR Proteomes; UP000050465; 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; 3.
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; 2.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..583
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006146782"
FT DOMAIN 72..117
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 151..266
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 275..451
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 512..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 63941 MW; 2BC8EFC6C682EEEB CRC64;
MICWFGISAI APPALAFPSG SSQIPATPIT IAQRLSQNPT QPEPGNSIQP YLDRVAEEVS
EFTLDNGMKF IVLEQHDTPV VSMMLYANVG ASNEIDGQTG IAHYLEHLAF KGTTRIGTTN
YAAEKPVLDQ LDEVFDQMLA AEEAGDDAAL AELSERFAVL QAEAASYVEQ NKFGQIIEQA
GGTGLNATTS ADATRYFYNL PSNKLELWFS LESERFLDPV FREFYKEKEV ILEERRMRVD
NSPIGQMVER FSEVAYTSNP YRRPVIGYQE DLRKATRADI QAFFNTYYGP SNLIAAIVGD
VDPDQAKELA KIYFGRYQLR TQAPKLVVNE PVQEAPREFS LELVSQPWYL EGYHRPGIND
PDHVVYSMID SVLTGGRTAR LYKALVEPQI ALDVGSANGF PGDKQSTVLL LYGLTAPGNT
VEDIAEGIGE QLERLKTELV DEATLERVKT QARAGLLGVL DSNNGMASLL AEYQAKTGDW
RNVFVELQAI ESVTAADVQR VARETFRPEN RTVGKLISAS TEAPTEAPTE APTEAPTEMP
AEGEPGDSPE GPTQTPDESP SMPENSSSKA LSAQPIKAQP VEA
//
