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Database: UniProt
Entry: A0A2J6Q3Z3_9HELO
LinkDB: A0A2J6Q3Z3_9HELO
Original site: A0A2J6Q3Z3_9HELO 
ID   A0A2J6Q3Z3_9HELO        Unreviewed;       841 AA.
AC   A0A2J6Q3Z3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN   ORFNames=NA56DRAFT_600866 {ECO:0000313|EMBL:PMD20914.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD20914.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD20914.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD20914.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) 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; KZ613483; PMD20914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6Q3Z3; -.
DR   STRING; 1745343.A0A2J6Q3Z3; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
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:UP000235672};
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..841
FT                   /note="P/Homo B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014410318"
FT   TRANSMEM        713..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          480..615
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          109..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          784..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..801
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..819
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..834
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        232
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        404
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   841 AA;  92048 MW;  8179A7AFEC7DFD18 CRC64;
     MRLHSVLGLI GLGYLASASN LRARDYDAQD YYVLHLDSTT PPSQVALQLG LAHEGQLGEL
     EDHHIFSCHK QEVDVVHTAL KERRRRKRSF GGSDILDGVK FAQKQKIKAR MEKRGPLPPP
     PEGYAAPVEE RQESPSEAVL AKQAAVAAAL DIQDPIFHEQ WHLLNPVQVG HDVNVTDVWM
     QGITGHNATV AIVDDGLDMY SDDLKDNYYA EGSYDFNDNV LEPKPRLADD RHGTRCAGEV
     SAVKNNVCGV GVAWDSKIAG IRILSKLITD ADEAVAMNYA YQHNQIYSCS WGPPDDGRSM
     DAPGILIKRA MLNAVQNGRG GLGSIYVFAS GNGAANEDNC NFDGYTNSIY SITVGAIDRK
     GLHPYYSEKC SAQLVVTYSS GSGDAIHTTD VGTNACYNGH GGTSAAAPLA AGIFALVLQI
     RPDLTWRDMQ YLVMQTALPV DLDTGDWQDT TMGLKYSHTF GYGKIDSWAT IEAAKTFKNV
     KPQAWYYSPW IHVNQAIPQG LEGLAVSFEV YPEMLKAANL ERLEHVTVTM NVAHTRRGDL
     SVDLVSPDKV LSHLSASRKL DNAPEGYDDW TFMSVVHWGE SGIGTWTIVV KDTNVNEFNG
     TFIDWHLKLW GEAIDPAAAT LLPMPSEHDD DNHDQIISTT SIAGTTTTLA PVSTQTSLMA
     NPTDHPDRPV NAKPTGTTED ENTPTNTPAA TGIPSSWLPS FFPTFGASPK TQIWIYGSAA
     LIVIFCSAVG IYLFMARRKR LRNNPRDEWE FDLLEEDEAE GLNGGGKVGG KKGGKRRAGE
     LYDAFAAGSE DESDGEYVDG VEGGDEQEKR LYEDSDDEGR HVIGEDEDEE EVVNEKFSSV
     E
//
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