ID A0A0C2QL94_9CYAN Unreviewed; 359 AA.
AC A0A0C2QL94;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=SD80_24360 {ECO:0000313|EMBL:KIJ80848.1};
OS Scytonema tolypothrichoides VB-61278.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ80848.1};
RN [1] {ECO:0000313|EMBL:KIJ80848.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ80848.1};
RA Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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:KIJ80848.1}.
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DR EMBL; JXCA01000014; KIJ80848.1; -; Genomic_DNA.
DR STRING; 1233231.SD80_24360; -.
DR MEROPS; M04.023; -.
DR OrthoDB; 291295at2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 80..187
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 190..358
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
SQ SEQUENCE 359 AA; 39738 MW; 4F90EF9A19285B82 CRC64;
MARKKKKSVM SECEHLLDTR CPICCIVPPH MLEHVAVNGN QQQREWAFRT LNVSAQFRGR
RNVAGAVNFA VSPGQKRRTI FDAKNSEQLP GVLVRGEGDP PSQDTAVNEA YDAAGATYDL
FKEVFERNSV DDKGLRLDST VHYNVKYDNA FWNGDQMVYG DGDGEIFQCF TKSIDVIGHE
LTHGVTQHEA GLIYFEEPGA LNESFSDVFG SLVKQRVKNQ TADQADWIIG EGLLTPKTKG
IGIRSMKAPG TAYDDPLLGK DPQPAHMKNK YTGTDDNGGV HINSGIPNHA FYLAAVEIGG
YAWEKAGKIW YITLRDRLKS KANFKQAANI TIKVAGELYD QGSKEQKAVQ NAWQKVGVL
//
