ID Q6VGA7_9ALVE Unreviewed; 341 AA. AC Q6VGA7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 24-JUL-2024, entry version 68. DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619}; DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619}; DE Flags: Fragment; OS Perkinsus marinus. OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae; OC Perkinsus. OX NCBI_TaxID=31276 {ECO:0000313|EMBL:AAQ54744.1}; RN [1] {ECO:0000313|EMBL:AAQ54744.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=14735929; RA Brown G.D., Reece K.S.; RT "Isolation and characterization of serine protease gene(s) from Perkinsus RT marinus."; RL Dis. Aquat. Organ. 57:117-126(2003). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins with broad specificity for peptide CC bonds, and a preference for a large uncharged residue in P1. CC Hydrolyzes peptide amides.; EC=3.4.21.62; CC Evidence={ECO:0000256|ARBA:ARBA00023529}; CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE- CC ProRule:PRU01240}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY340226; AAQ54744.1; -; mRNA. DR AlphaFoldDB; Q6VGA7; -. DR MEROPS; S08.041; -. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd07473; Peptidases_S8_Subtilisin_like; 1. DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1. DR InterPro; IPR000209; Peptidase_S8/S53_dom. DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf. DR InterPro; IPR051048; Peptidase_S8/S53_subtilisin. DR InterPro; IPR022398; Peptidase_S8_His-AS. DR InterPro; IPR023828; Peptidase_S8_Ser-AS. DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel. DR InterPro; IPR034204; PfSUB1-like_cat_dom. DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1. DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR SUPFAM; SSF52743; Subtilisin-like; 1. DR PROSITE; PS51892; SUBTILASE; 1. DR PROSITE; PS00137; SUBTILASE_HIS; 1. DR PROSITE; PS00138; SUBTILASE_SER; 1. PE 2: Evidence at transcript level; 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 36..261 FT /note="Peptidase S8/S53" FT /evidence="ECO:0000259|Pfam:PF00082" FT ACT_SITE 43 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 83 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 247 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAQ54744.1" SQ SEQUENCE 341 AA; 34937 MW; B112A818FC44A838 CRC64; LLGTNDPGSS CQGNLEIIRF RGAQEAVRSV SRGLRNVVLA IVDSGVDVSH PDLINQFWKN PDDGSIGFNF LDDNTNVTDE NGHGTHCAGI AGAQTNNSLG IAGVADVKLM ILKFVGSDRT GPLSGALKAL DYAVGMGAAV SSHSYGGNVP SRIFENAIRN AANAGHIVVA ASGNEGMNLD ETPTYPCSYS RSIPSMLCVG ASSSTPTSPV SLASFSNIGS VVNIVAPGVN ILSTYLSGSY AFLSGTSMAT PQVAGVAAVL ATLGLAGQSI TDSITRSRTA SLRNALSLQN LGELDALNAV NEGLGQPTSP PRQPSSARLS SSVCLWSVGL LFVIITGHSA F //