ID A0A1X7RC24_ZYMTR Unreviewed; 684 AA.
AC A0A1X7RC24;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=ZT3D7_G118 {ECO:0000313|EMBL:SMQ44974.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ44974.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ44974.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; LT853692; SMQ44974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RC24; -.
DR STRING; 1276538.A0A1X7RC24; -.
DR Proteomes; UP000215127; Chromosome 1.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 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; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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:UP000215127};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 200..539
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 483
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 684 AA; 73706 MW; B5FBA8251B4DD709 CRC64;
MSLVTVNGNT LNLSTSPILS QPTAEHSNFI LVQGYDAFTP DQKSALSGLG VEIMEYVSEN
TYLCRYPPRD LEVVRRVEGV RSVVVYDPAL KQTISLSEMV ETQPDQTEYE IDLILHDIPN
VTANQLAPFI ATAARIPIAE LEVVPGKVRL TVHQDRLADL AALDSVNRIE EVQPKTWYND
RARAVLLGEE EICVSTKYQG NGQIVCVADT GIDEGFVAGA EDGILHPAFK GRIEQVLDLW
DEDNGRDHIG HGTHVCGSIV GSGMCIDPES GKEVVVRGTA PGARLIVQSM LNWNTNLKEY
ILKQPLDLQK LWSAPYALGA RIHSNSWGDK WKQTQLGYES DATTIDSFVH GNPDFIILIA
AGNDANKGKV PLAQIGDNSA AKNCITVGAT GSTRANDGQR FFRGTLGTTI AQAAAFSSRG
PTLSTKNTQG QDLVGRIKPD VVAPGVAVLS PAAKGLDLFT RLDIEKKCGK SGDPNWLFMS
GTSMATPLVA GCGAILREAL ERRGKKHPSA ALIKALLING AVNHSAPAGQ VFDYAQGFGR
VDVQRSIEMI EGKNPLCGFV DGGNPFEATE FDVSALRREV GNSWESADIA IPKGRNMVVV
TLAYSDAPGT LLQNDINLIV QAGGQERHGN VGDSPGFDST NNVEKVIWEN VQSATMRIFV
RCNGFAKDLT SGFAVAWRVE TGLD
//
