ID A0A2K8SIJ9_9NOSO Unreviewed; 662 AA.
AC A0A2K8SIJ9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:AUB34665.1};
GN ORFNames=COO91_00494 {ECO:0000313|EMBL:AUB34665.1};
OS Nostoc flagelliforme CCNUN1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB34665.1, ECO:0000313|Proteomes:UP000232003};
RN [1] {ECO:0000313|EMBL:AUB34665.1, ECO:0000313|Proteomes:UP000232003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB34665.1,
RC ECO:0000313|Proteomes:UP000232003};
RA Shang J.;
RT "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT its photosynthetic adaptation to extreme terrestrial habitat.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP024785; AUB34665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8SIJ9; -.
DR KEGG; nfl:COO91_00494; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000232003; 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; IPR023827; Peptidase_S8_Asp-AS.
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; PS00136; SUBTILASE_ASP; 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}; Reference proteome {ECO:0000313|Proteomes:UP000232003};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 533..662
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 662 AA; 71968 MW; BCA713669A8BF432 CRC64;
MVQFRYGGQN GQQYELAISD EHLVVRTENR SALVGARPFE VAPVSPTARS ILNEFELATR
FRQAGVEILR TKGPTEGVAL RDRAREILNQ EPEVQFAGRV LVDPVSQQPI IYTENLFLKF
HSEEELTVCQ EVLRRYDLTI KRQLEYAPNA YFVSASANTG IAIFDIAERL LNEESVDLCH
PELVRELRQR QVFPQQWHLK QTTINGKVIN AHANAEAAWK LSDGTGTIIA IVDDGVDLDH
EEFRSSGKIV APRDVTRKTD NPRPGNDNNH GTGCAGVACA NGNFGASGVA PGAKLMPIRL
ASALGSQDEA DAFVWAAQNG ADVISCSWGP SDGVWFERND PVHNQKVPLP DSTRLAIEFA
INKGRNGKGC VILFAAGNGN ESVDNDGYAS YQKVIAVAAC NDYGTRSAYS DFGQAVWCAF
PSNNGESSQT TGIWTTDRSG VVGYNSGSRN LGDAPGNYTN QFGGTSSACP GAAGVAALII
ARNPNLRWDE VRDIIKRSCD RIDQAGGKYD ANGRSPFYGY GRMNALKAVE LAKPPETSPI
SRFQAVQDIP INDLQISTLS LAIASTNLIK SIKVNVDIEH TFIGDLIVTL LPPVQTGIPP
VILHDRQGGA TDNIKTTYDE INTLKLAAFK GKNPQGTWTL EVADKAEGDT GKIRRFTIEM
GF
//
