ID A0A1V6RIZ5_9EURO Unreviewed; 842 AA.
AC A0A1V6RIZ5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN ORFNames=PENSOL_c003G08536 {ECO:0000313|EMBL:OQE01801.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQE01801.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:OQE01801.1}.
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DR EMBL; MDYO01000003; OQE01801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RIZ5; -.
DR STRING; 60172.A0A1V6RIZ5; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000191612; 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; IPR023827; Peptidase_S8_Asp-AS.
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; PS00136; SUBTILASE_ASP; 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:UP000191612};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 486..621
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 646..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 410
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 842 AA; 91944 MW; C4312DCCBA3E09AE CRC64;
MRIVSGITAT LGLAGAASAN LHPRSQETRD FFALHLDDTT SPSHIAQVLG ARHEGQIGQL
DGHHTFSLPR EQTAQFDTLL SDLRTRRKLR RRSDGGIDSR GTSDDPLDKI LWSHKIAPAR
QRLQKRLPPV SVPYKTLDKR ENAQAVAFQK NAMSSLGITD PIFREQWHLL NTLQPGNDLN
VTGLWLEGIT GKGVATAVVD DGLDMDSNDL KPNYLPEGSW DFNEGLPDPR PLLLDDKHGT
RCCGEIAAAK NDVCGVGVAY DSKIAGIRIL SKPIDDVDEA AAINFAYQKN DIYSCSWGPM
DDGATMDAPG ILIKRAMANG IQKGRGGKGS VYVFAAGNGA ASGDNCNFDG YTNSIYSITV
GAIDREGNHP SYSESCSAQL VVAYSSGSGD YIHTTDVGAN KCFSGHGGTS AAGPLAAGSV
ALALSARPEL TWRDLQYLMV ETAIPVSEDD GSWQVLPSGR KFSHDWGFGK VDTYTMVQLA
KTWDLVKPQA WLHSPWLRVH QDIPQGNQGL LSRYTVNADQ LKEANVAKLE HVTVTMNVNH
TRRGDISVEL RSPGGIVSYL SVAREKDNMP VGYEDWTFMS VAHWGESPIG EWSIIVKDSD
VNEHSGTFID WRLNLWGEAA DAAKQKLHPL PDEHDDDHTY EDAPVATTSI TSAPTKTATP
ANPDNHHDRP VNAKPKPTST KPTPVEPTPI EDLKQPTNTT GSEAATSSPS SADSGYISSW
LPTFGASKRT QIWIYASLAM IITFFIGLGV YFQLQRIKRR RTTAHDDYEF EMIEDEDEMQ
PMTGASGRTQ RRGGELYNAF AGESDEEMFS DDDEPYRDGL ANTQEKDGQD GTSHGGPHQE
KP
//
