ID A0A168EGC3_9HYPO Unreviewed; 819 AA.
AC A0A168EGC3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Subtilisin-like serine protease PR1C {ECO:0000313|EMBL:KZZ98766.1};
GN ORFNames=AAL_02317 {ECO:0000313|EMBL:KZZ98766.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ98766.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ98766.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ98766.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ98766.1}.
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DR EMBL; AZGY01000004; KZZ98766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168EGC3; -.
DR STRING; 1081109.A0A168EGC3; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000078544; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034187; Peptidases_S8_5.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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:UP000078544};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 57..498
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 307..372
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 533..661
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 66
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 456
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 819 AA; 89000 MW; 8EDB895B8F64E7AF CRC64;
MVSPPGEHLR PYKPSPRSLS RRWCNWWGTC VNTVVHGVYE PHRMTQVDQL HAKGITGSGL
KVAVIDTGID FKHPVLGTTI GSCLKSECGS CFGKGCLVEY GYDFVGNDFN GENTPIPDKD
PMDCNGHGTH VAGIISARKN DLGFIGAAPG VKLGAYKVFG CSGDTPNDIL VAASLQAFED
GSDIITASIG AANGWNEHPW GTVINRITAQ GVPFICSAGN EGSSGLFYAN GGAASKAVTA
IGSMENRVIP KIMIKSTWRE NKGLVGTDFH LLAGEPKIWG VDKMRLWATS LDYDYIEDCC
KPLPEDYRDL SKYVVLVRAS NCPFNIQVIN IMQKGAKYMI IYNHRDETFT PTPTPIPEGL
LAVGMVEYKL GKKWIRIMNE GKKVHVTIPH PYKAFQHSTT AKMEPNDKEG GLISLFTSWG
PTWQMLMKPQ FTAPGGNILS TWPMAKGGYS VQSGTSMATP LVASIMALMY QVRGRIGLPA
LTDLLSSTAK PQIFYNGTKR FGMLAPPAQQ GGGLVQAFDA AYTTTRLYPS SLSFNDTVHL
APELNFTIMN YGKSSVIYTL GHRPALTMYT LANGTNMTMN FPNEIVDDAH ATLSFHHGRL
RVADPFHHMQ PVKRVTIEAG NRAIITVRAK PPKVEKPERL AVWGGYITIN GTDKSALSMP
YQGLAGNLTN VTVLEPGNAA WVVSVKKSQF VVPPPDTPVP LPSGGSHEDQ EVVLKVACFL
NLGTANLSID IVPQGGAPPA DKVKDVFGLQ TLGQMYGFPM LWVGRGYGYY KWDGKLASGD
FAPAGRYIAN VRALKLNGDP VKENNWETAK TNTIDLSYE
//
