ID A0A1G4MIY6_LACFM Unreviewed; 824 AA.
AC A0A1G4MIY6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=LAFE_0H00782g1_1 {ECO:0000313|EMBL:SCW03867.1};
GN ORFNames=LAFE_0H00782G {ECO:0000313|EMBL:SCW03867.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW03867.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|EMBL:SCW03867.1, ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6772 {ECO:0000313|EMBL:SCW03867.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; LT598491; SCW03867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MIY6; -.
DR STRING; 4955.A0A1G4MIY6; -.
DR OMA; AYEFDII; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000190831; Chromosome h.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
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 PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 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; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000190831};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..824
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009237417"
FT TRANSMEM 690..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 459..593
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 655..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 383
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 824 AA; 91178 MW; 829A65FEF9DE9E8A CRC64;
MNCIKNGPLW CLLMILTKVS ESKRVPAKDH SERLYFAIET DLNMTSVIGM HPDWNYEHEV
RGLDNHYVFS KSLTDVQKRE FDDNVLLDGI TAFHNLPPKR LHKRLPVPDL PAEMPSDSSL
IPMSLAKEKL EISDPAFDQQ WHLINTNFPG NDVNVSNLWF QNITGFNVVA AIVDDGLDYE
SEDLRDNFSP EGSWDFNNNE PLPKPRLNDD YHGTRCAGEI AAVKNDVCGI GVAYNAKVSG
IRILSGEITS EDEAASLIYG LDVNDIYSCS WGPSDDGRTL QGPDELVKKA LVKGVLDGRN
KKGAVYVFAS GNGGMFDDNC NYDGYTNSIY SITVGAIDHK GLHPPYSEAC SAVMVVTYSS
GSGEYIHSTD IKGKCSNTHG GTSAAAPLAA GVFALVLEAN PDLTWRDMQY LVILSSVEIN
EGDGNWQHGA LGKRYSHRYG YGKLDAYRIV DMARSWTNVN PQSWYYSNEE VTDQFTNSTD
TTLESTIEIT DMDLSDANLK RVEHITVTVD IETDFRGHTL IDLISPEGIT SNLGVLRRMD
KSKEGFRDWT FMSVAHWGEK GAGEWKLQVR TTNEGDGVKL NRWNLKIFGE SLEASRAQTF
SYGDDKDETS IATVSTQASE TESLTQIMTS SATDSESSIR TSSLLTAEPT VSTSAASSYL
QTSSPSPIPT HDGDDYDTNQ ANRLSRPADA MHYFVALFIL GSAFFLLYFV FFVRSRRRIR
RSRAEAYEFD IIDSDSEYDS SMDNATNASA NMLGDSIPED FDFDLSDEEL LAASAATSST
PDNKKASNTL DEIIEDAYDD RAPLNASSEQ TQSLEKTSGD IKPK
//
