ID A0A068S2W8_9FUNG Unreviewed; 857 AA.
AC A0A068S2W8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Probable kex2-endoproteinase of late golgicompartment {ECO:0000313|EMBL:CDH56202.1};
GN ORFNames=LCOR_07277.1 {ECO:0000313|EMBL:CDH56202.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH56202.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH56202.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-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:CDH56202.1}.
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DR EMBL; CBTN010000035; CDH56202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S2W8; -.
DR STRING; 1263082.A0A068S2W8; -.
DR VEuPathDB; FungiDB:LCOR_07277.1; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000027586; 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: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; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..857
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001652848"
FT DOMAIN 498..637
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 653..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 250
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 422
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 857 AA; 93555 MW; 702C28676C2E674F CRC64;
MKASATLVLV AGFLAASCLG SSQPVKRSPD RRYYTLHIPS SEAHLAVQAA DALGVQYEGP
VGELTTYYLV STLDHEQLYK RDQAVAAATA AVHDPILEAF HAHKERRWLG KRDTENNDWW
DRVHAMDAQV PRQRVKRAVL PEHHVKREPP FVEINQGKLT LEDAQETLGI QDPGFPRQWH
LVNQENVGND INVTGVWKQG ITGEGSIVAI LDDGLDYESH DLQDNFFAEG SYDFNDHVDL
PKPKLFDDTH GTRCAGQIAA VKNDVCGIGI AYDAKVAGVR ILSAEITDSD EAAALNYKYQ
ENQIFSCSWG PPDNGETMEA PTGILAEAFV NGIKNGRDGK GSIYVFATGN GAISGDNCNF
DGYTNSIYTI TVGALDHTNS HPPYSESCSA QMVVAYSSGG GEFIYTTNVG ENVCSDRHGG
TSAAAPTAAG IFALVLSVRP ELTWRDLQHL CVQTAIPVDL EDEDWKELPS GRKYNHKFGY
GKLDAYAIVE AAKTFEHVNE QTYLELPVDV GGKIIPESTQ VKKVPLKSTI KVTQDMVKNA
GLKRLEHVTA TVNIEHKRRG DIVITLQSPN NVESELATMR PGDKSPDGIR NWKFMSVKHW
DEDPLGDWSL LVYDVTHPES NGTMLNWTLT LWGEMDPEFE GEPVHAPLAE HNTTVSDHHS
TIVSSASATS TTTSEHVPAR PTRLKSTTTA TPATTTTTTA TTTTTTSSST TTEEEEEEED
EDTTTSTTTT TATAENDSTD TQTSTPESIS PAADAAKQED EDEDDSTSQS PGSGSTVVYA
LVGTGAIVAL ATGLYVQKRK SWQPPAGSET ERHRQAASDY EFSVLRRSEE DEAEDDDITS
DRHALLPDND PSRRNRS
//
