ID   A0A1Z4UXG5_9CYAN        Unreviewed;       703 AA.
AC   A0A1Z4UXG5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Subtilase family peptidase {ECO:0000313|EMBL:BAZ83883.1};
GN   ORFNames=NIES806_00630 {ECO:0000313|EMBL:BAZ83883.1};
OS   Dolichospermum compactum NIES-806.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Dolichospermum; Dolichospermum compactum.
OX   NCBI_TaxID=1973481 {ECO:0000313|EMBL:BAZ83883.1, ECO:0000313|Proteomes:UP000218702};
RN   [1] {ECO:0000313|EMBL:BAZ83883.1, ECO:0000313|Proteomes:UP000218702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-806 {ECO:0000313|EMBL:BAZ83883.1,
RC   ECO:0000313|Proteomes:UP000218702};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; AP018316; BAZ83883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4UXG5; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000218702; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07498; Peptidases_S8_15; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR034054; Pep_S8_PrcA.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          564..703
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        239
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        277
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        491
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   703 AA;  76624 MW;  7678DD8417EB05DF CRC64;
     MSDNINPADF PESDVANNGE SLTLQRGGEE LTLEKTLYRF TIRPNANFPH EKLTQIPGSV
     WRRSIPQAKL ELYTVFPNQL DAVMSQLRAD ENVDFVSHVY TLENNPGTFV YLSDQITIQF
     ATWVDNTKIN TITSTLNLVQ DKPVFGIPNT FIFLVNKQAT QNPVKITNYL QTLPEVLAAE
     PNILIQQEPH YKPKDSLYSQ QWYLNHNSSN QLVAGSHISV EQAWDTTRGV RSIVVAVVDD
     SFDLKHPDFQ GTGKIVAPRD LKENDFLPLP GEKETSHGTA CAGLAVAEEN GSGIVGVAPG
     CAMMPIRTTG FLDDQSIEDI FDWAVEKGAS VISCSWGASA VYFPLSIRQK AAINRAATNG
     RRGKGCVIVF AAGNANRPIN GTVNEQNWPK NIVQGKTNWL SGFAVHPDVI TVSASTSLNK
     KAAYSNWGGN VSVCAPSNNA PPGMWFQETG FVYTQPAIVS SLFGLGVFTT DQIGAAGYDA
     GNFTKNFGGT SSATPVVAGV AALVLSANPD LTAQQVKRIL QDTADKIVDN NPDLQLGVRG
     GTYDSNGHSQ WFGYGKVNAA KAVRLAQQMG AVAKITNKQI QFKNSQVVDI PDNNRQGIKS
     MIGINEAVNV TDIQVTVNIT HDFLGDLEVY LIAPNNQRIL LQSRTLGRRN QLQNTYTVRS
     HPALKQLLSL PAKGNWQLQV IDYAALDVGK LNNWELVIGV GNK
//