ID A0A0F7ZG50_9HYPO Unreviewed; 765 AA.
AC A0A0F7ZG50;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=SWIM-type domain-containing protein {ECO:0000259|PROSITE:PS50966};
GN ORFNames=HIM_10320 {ECO:0000313|EMBL:KJZ70276.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ70276.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ70276.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ70276.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KQ030635; KJZ70276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZG50; -.
DR OrthoDB; 380531at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
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; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF69; PROTEINASE T; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054481};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 120..158
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT REGION 209..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 538
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 553
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 708
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 765 AA; 82964 MW; 1AA01563D1C6FB74 CRC64;
MKAEFPIGLL LLLCFFFLFS DYLLLLADYL ILPIECLLQS LEFRTILFQQ LPDLLDRRHF
LVTAADALVP RYPRTFFITC LFSCRPCRTR DPFRLPLYNK VSEKASYRSL ELVQKQARAA
TASLLYPEER ALPECTNSFT SQYGLPCKHI IASFLAVEGD GPNRRVTTKE ALPLAFWDNH
WLLRDDLADT DPYRRIRDPR VVARRRGTIR VATTSSPTTN NTSSRASRSR SQQQQLQRST
APRRRLIVPP EVPQASQASR SVPLPDLESA GMAAQATITT IVKQLETIQN CLGICNAELK
SSRPPADITI EQSPIEPRSY RQPRSFPRSA RATQEMRRLP SAFEEFEPTS ASQGGARRGY
RERARQFTLN TSSKPLSNAL PSIQGGFGQP QALEPANTVA EGAIGHSPSR RRGAGALRPY
ESILYLAISS LCIVKFKEGT STASFNDALG IANQTVDRIY NHVFQGFASR LDNSVLHILR
SRSDIDFIEA DGVISVNGYI EQPDAPWGLG RISYRRPGSA PYVYHTSAGQ GTCSYVIDTG
IEDNHPTTDG NGHGTHVAGI IGSKSYGVAK ETTIYGIKVL NNTGGGSYSS VIAGMDFVSR
DAKRRRCPKG SMANMSIGGG YSKSINIAAA ALVRSGVFVS VSAGGSNSDA ANFSPASEPL
VCTVGATTSS DSRSGSSNYG KLVDVFAPGS HVKSTWINAA SNTVSGSSMS AGHITGLGAY
LAAWEGYPGA QELCTRIQSL ATKGALTNVP SDTQNLLAFN GNPSG
//
