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Database: UniProt
Entry: A0A0L0SVL1_ALLM3
LinkDB: A0A0L0SVL1_ALLM3
Original site: A0A0L0SVL1_ALLM3 
ID   A0A0L0SVL1_ALLM3        Unreviewed;       854 AA.
AC   A0A0L0SVL1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN   ORFNames=AMAG_11741 {ECO:0000313|EMBL:KNE66623.1};
OS   Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS   macrogynus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE66623.1, ECO:0000313|Proteomes:UP000054350};
RN   [1] {ECO:0000313|EMBL:KNE66623.1, ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE66623.1,
RC   ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Allomyces macrogynus ATCC 38327.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA   Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA   Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA   Lander E., Nusbaum C.;
RT   "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL   Submitted (NOV-2009) 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; GG745350; KNE66623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0SVL1; -.
DR   STRING; 578462.A0A0L0SVL1; -.
DR   EnsemblFungi; KNE66623; KNE66623; AMAG_11741.
DR   VEuPathDB; FungiDB:AMAG_11741; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   OMA; QIKDPIF; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000054350; 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:UP000054350};
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..48
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           49..854
FT                   /note="P/Homo B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005548194"
FT   TRANSMEM        736..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          513..659
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          661..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..704
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        218
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        256
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        430
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   854 AA;  90870 MW;  6202C625B4872683 CRC64;
     MSVPSRAAAC RAVPALRRRH APLSAPAALL IAALALLLAA VPPAPVLADP APPHRMDHAN
     YHYFAARVHD GADPRLAARD VAAAVDCPVA QSVELVGPVG NLPRHFLYRA PAECTTALAK
     RNPDASLHSH LVRRALEEHD GVVYVEQQIP TRRLHKRAPT AITQADAQAI FDSANIRDPG
     FPQQWHLYNQ VNPRSDINVT GVWAQGVFGH NVTVALVDDG LDFDAADLRD QFDLQGSYDF
     NDHGKEPRPR LSDDYHGTRC AGEVAAARND ACGVGVAFGA RVAGIRILSG QLTTADEAAA
     YTYAHETNHI YSCSFGPEDN GAVVEGPSEL VHDAFRHGVE QGRGGLGSIY VFASGNGGRQ
     DDDCNADGYA NSNYTITIGA VDRNDQVPWY AENCAAQLAV TYSGGSHGAA GIFTTDVGAS
     KCTDNHSGTS AAAPIGAGIF ALVLSVRPDL TWRTLQHLVV ETAVPFDLDI PSHAWSALPS
     GRYFSHHFGY GKLDAYALVS AARTRPNVAH AVAVESAWHA LELPISAMAK RDRFVSAVAG
     SGLGAVNHTI TVEPGQVEAV GARRNGTEYV MATVWIDHEQ RGDLELDLVS PHGVVSHLLV
     RRPYDYSDKG FQNWTMSTVQ HWGEDPTGNW TLVVMDKSNP KAGGTLRGWS LQVYMEANAT
     TAAVPPPPRP PSSRPIPPAS TSTLAVPTPP SSSAPAPPAS SLPPAPSTSS DAESSSLPDT
     RPTTDPVAEE VSAAHVLGVL ITCTLSAGAF LGTLTFLVRT GHWKKCVPRS WRGDRGSGGN
     DDYEFMKLGP DSGGRLADHE VLFDSFLDDE DEEGDEEAQR GRVAVHVEDD DGAEGENVVL
     FGASTSPGLR PVAR
//
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