ID A0A0D2E1L9_9EURO Unreviewed; 847 AA.
AC A0A0D2E1L9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN ORFNames=PV06_01243 {ECO:0000313|EMBL:KIW48675.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW48675.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW48675.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW48675.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) 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; KN847332; KIW48675.1; -; Genomic_DNA.
DR RefSeq; XP_016268891.1; XM_016401838.1.
DR AlphaFoldDB; A0A0D2E1L9; -.
DR STRING; 215243.A0A0D2E1L9; -.
DR GeneID; 27353317; -.
DR VEuPathDB; FungiDB:PV06_01243; -.
DR HOGENOM; CLU_002976_2_1_1; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000053342; 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:UP000053342};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..847
FT /note="P/Homo B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002251906"
FT TRANSMEM 733..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 491..626
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 124..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..823
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 415
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 847 AA; 92664 MW; 0717B5444D64AD50 CRC64;
MRLPSWLSLF LLASHAVAAQ RDYEKNDYFA VHLGPTADIQ EVARLFGVKH EGQIGELSDH
HTFSCSKGSC PDFEASLHEL KLRKKRWRRG DIGLQKRDSW RQLSIELGGI LWAEQQHLRH
RHVKRIPPPG PLVSRQDKAD GGTDAEQQEA IQRLNSIAET LDISDPIFKE QWHLFNPLQL
GHDLNVTGVW LDGITGNGTI SAVIDDGLDM DSNDLKDNYY AAGSYDFNDK GPDPKPRLFD
DKHGTRCAGE IAAVKNNVCG VGMAYDSKVA GLRILSKPIS DEDEATAINY HYQENDIYSC
SWGPPDDGAT MEAPGILIQR AMVNGIQSGR GGLGSVFVFA AGNGAASEDN CNFDGYTNSI
YSITVGGIDR AGNHPYYSEA CSAQLVVTYS SGHNDAIHTT DVGVDKCYTG HGGTSAAGPL
VVGTVALALS ARPDLSWRDL QYLCVETAIP IHLDDGSWQN TTIGKKFSHT YGYGKVDAYL
FVEAAKSFVP VKAQAWFHSP WLSVQHAIPE GDQGLAASFN VTQQMLDEAN LERLEHVTVT
MNVKHGKRGD LSADLISPDG VVSHLAVTRR PDVADTGYDD WTFMSVAHWG ESGIGKWTVV
VKDTRENEFN GTFIDWRLNL WGESINEQIQ GLHPLPDEHD DDHETATAIV STTSVDAAPS
PTSLAAKPTD HIDRPTKPKP GDDSDTTATA PTTSTGSEAA ATTTGAVEPT HTYSDSFLPS
FFPTFGVSKR TQIWIYGSIG LIIVFCAGLG VYFVLQRRKR LRNNPRDAYE FEMVGDADDD
EQQGLNNRRT RTGKGRARRG GELYDAFAGE SDDDDDDLYS EDDTYQDTPS NDTSTGSRGD
SPAGREK
//
