ID A0A023AZ43_GRENI Unreviewed; 894 AA.
AC A0A023AZ43;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=GNI_155610 {ECO:0000313|EMBL:EZG43919.1};
OS Gregarina niphandrodes (Septate eugregarine).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC Eugregarinorida; Gregarinidae; Gregarina.
OX NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG43919.1, ECO:0000313|Proteomes:UP000019763};
RN [1] {ECO:0000313|EMBL:EZG43919.1, ECO:0000313|Proteomes:UP000019763}
RP NUCLEOTIDE SEQUENCE.
RA Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA Brunk B., Roos D., Caler E., Lorenzi H.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:EZG43919.1}.
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DR EMBL; AFNH02001162; EZG43919.1; -; Genomic_DNA.
DR RefSeq; XP_011132890.1; XM_011134588.1.
DR AlphaFoldDB; A0A023AZ43; -.
DR EnsemblProtists; EZG43919; EZG43919; GNI_155610.
DR GeneID; 22915383; -.
DR VEuPathDB; CryptoDB:GNI_155610; -.
DR eggNOG; KOG3525; Eukaryota.
DR OrthoDB; 1330511at2759; -.
DR Proteomes; UP000019763; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
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:UP000019763};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..894
FT /note="subtilisin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012475089"
FT DOMAIN 616..878
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 214..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..461
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 623
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 670
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 832
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 894 AA; 97842 MW; 6D4C6790522FF874 CRC64;
MLLSHLTQLA TLALSWRLGD LSTADYAPTL IHTRTHTNRE QLSYLQYLHE PPPPLLQAHD
AQYDELVDDE LLDGHSRDDQ SLDDQLLADQ SLEDHSLDLE DDLEDDLEWP PRRTHFTPAE
VIAAAEAAHR NGSLRAQDAS GESPVIFTAS QLEALLGVLS VDPPALLFTI NEGGRHRLGF
GLFRDIAQHY VNNPVYQKIF QALNKLLRDV ARRKGGNNQA GDPATLDHLD HQAGDQDAEN
HDPGADDATS LNTPLSNRKT ALSLAGAEVE AKAEADEPVG HAWLSNVLTG TDEMQGFESN
YREDGALWDD LDAALKEDHR QIDRLGILDL KAVYEAALSL PRSESTTGAM AAGADDLAVY
DLVSGEDEFP TEKDWIEDDE DLFTPPPRFR PPDLAQERAA LLRQTPVHAD RPRPLSGNDH
RSASPDPETA LGGVERSEVE RSEVEPSEEA EPSEEAEPFE EAEPSTSQNR DSATQGVFNL
CDWYQYPAVC RAHFDHACLH QMVKRWKGRR KDFSLLPHLS IGHIALPRRP VRALKAIIDV
ACNPWIKDLH ADIILRSHGS GEVIPFDPVS LRGPARRELM LRGLGSPVND PKYRDQWHIP
DQKVEQAWQT TQGDVNVAVM VADTGVDINH EDLRDNFWQN NQPSREFNGQ DVHGINPIRK
NGDLSDEGGH GTHMSGVACA ATNNNRGVAG VGYRVRLAGC KFMQGASGSL GKLCDCVNYA
ADKRIKVVSM SFGGDTDMPA FSQSMKKATQ NNVIVVCSAG NSGHNNDQQH TYPAQYATNQ
DLAVVSVGGH DQKQAWLDYA SYGANTVLVS APGDYVLSTA QGNDYEFRGG TSPAAPSIAG
ILALGFSANP RLSALTAKQL LQQAVEPMNG FKAKCSWGGK INAQKFVSLA KNAN
//
