ID A0A0D9P133_METAN Unreviewed; 802 AA.
AC A0A0D9P133;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN ORFNames=H634G_04203 {ECO:0000313|EMBL:KJK79964.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK79964.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; KE384729; KJK79964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9P133; -.
DR STRING; 1291518.A0A0D9P133; -.
DR MEROPS; S08.070; -.
DR Proteomes; UP000054544; 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:UP000054544};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..802
FT /note="P/Homo B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002341672"
FT TRANSMEM 675..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 479..614
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 631..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 403
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 802 AA; 88003 MW; 1BBE68DEAAB0D51A CRC64;
MRVALFAGLI GLASLSYAGH APRDYKDNDY YVIQIERSVP PEEIASRLHL RHEGTVGALS
DHHVFRSRKT EHDVVRRELL ESKRKKRTPE EYDVLDKVLF SAKQELRRHL HKRVIPPPPP
GAHKPRAVAE PALSAVKKQQ TIMDTLSIKD PIFTAQWHLF NSVEVGNDVN VTGVWMEGIT
GKNATVAIVD DGLDMHSEDL RENYFAEGSY DFNDHDPEPA PVLSDDHHGT RCAGEVAAVR
NDVCGIGVAY ESKVAGIRIL SAVISDEDEA EALMYKNDKN QIYSCSWGPS DDGRTMEAPS
VLIRRAMLKS IQEGRNKLGS IFVFASGNGA KSGDNCNFDG YTNSIFSITV GAVSRDNQQT
YYSEPCSAQL AVTYSSGGSA SDGFIHTTDV GSNKCTDRHG GTSAAAPLAA GIFALVLEVD
PELSWRDMQY LVMDTAKPFS APGVVWNQTG IGKQFSHAFG YGKIDTYDLV QKAKTWNKVK
PQAWFFSPRL EVNGAIPEGP TGISANFTVT KDMLKEANLE RLEHVTVFMN VNHTRRGDIS
VDLISPSNMV SQIATTRSGD EHYAGYVNWT FMSVAHWGES GVGTWTLVVR DTEQNEHNGS
FVDWRLKLWG ESIDAKKATE LGMPTEDEYV DLPVTQSPTP TASPTPTATA SPTTTATATS
TVPPSWFPGF GSKTAMLWVI GAAVLIVLFC IGLCIYLFIA RKRRNTPRDD YEFELLDEEE
ADGLNSNEKG GEGRRTRGGE LYDAFAGASD DEEEFDEYRD PPTERLAGNG YEEDQYVVGE
ESDDEGSSGA AETMPLGGGS RS
//
