ID W9XDE4_9EURO Unreviewed; 846 AA.
AC W9XDE4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Kexin {ECO:0000313|EMBL:EXJ78243.1};
GN ORFNames=A1O3_09404 {ECO:0000313|EMBL:EXJ78243.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ78243.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ78243.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ78243.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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:EXJ78243.1}.
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DR EMBL; AMGY01000009; EXJ78243.1; -; Genomic_DNA.
DR RefSeq; XP_007737688.1; XM_007739498.1.
DR AlphaFoldDB; W9XDE4; -.
DR STRING; 1182542.W9XDE4; -.
DR GeneID; 19173488; -.
DR eggNOG; KOG3525; Eukaryota.
DR HOGENOM; CLU_002976_2_1_1; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
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:UP000019478};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..846
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004931841"
FT TRANSMEM 736..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 494..629
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 126..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 246
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 418
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 846 AA; 93138 MW; EBBB88E732CD2154 CRC64;
MRLPSWLSIL LLARAVSASP RDYERYDYFA VHLDSAVVPQ EVAQRLGMQY EGLVGELSHH
YTFSCLKDSC LDVEESLEEL RRRKKRRRRR SDGSEPHNLR REIPLDLNGI LWSEKQQLRH
RHVKRIPPSP LLNGRAGQKA ADSDIHQAAD QEAVRRLDSI AETLDIKDPI FKEQWHLFNT
RQLGHDLNVT GVWLDGITGN GSISAVIDDG LDLYSNDLKD NYFAEGSYDF NEKEPEPRPR
LFDDHHGTRC AGEIAAVRNN VCGVGMAYDS KVAGIRILSK PISDEDEATA INYHFQENQI
YSCSWGPPDD GATMEAPGIL IQRALVNGVQ SGRNGLGSVF VFAAGNGASN EDNCNFDGYT
NSIYSITVGG IDRDGNHPYY SEHCSAQLVV TYSSGEQDAI HTTDVGTDKC FNGHGGTSAA
GPLVVGTVAL ALSVRPDLSW RDLQYLCVET AVPIHLDDGG WQNTTIGKKF SHTYGYGKVD
AYRFVEAAKS FESVKPQAWF HSPWISVQHA IPEGDLGLAA SFQVTEGMLR DANLERLEHV
TVTMNVEHGR RGDLSADLIS PTGVVSRIAT ARGPDSAAAG YDDWTFMSVV HWGESGIGNW
TVVVKDTTEN EFNGTFIDWR LNLWGECIDP QIQGLHPLPD EHDDDHVTAT AIVSTTSVAP
GSSPTSLPAI PTSHIERPTK PKPSDATDTT ATATATDITS VPAATTTLVP EPTHTYSDSF
LPSFFPTFGV SKRTQIWIYG SIGLIVIFCS GLGVYFLVQR RKRLRNNPRD AYEFEMVGDA
DEDEQQSLNT RGGRGKARAR RGGELYDAFA GESEDDLYSD DEAYQDTPSN DTGTGSRSDS
LEGQEK
//
