ID T1HZ79_RHOPR Unreviewed; 636 AA.
AC T1HZ79;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
DE Flags: Fragment;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC009349-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC009349-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; ACPB03016132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1HZ79; -.
DR STRING; 13249.T1HZ79; -.
DR EnsemblMetazoa; RPRC009349-RA; RPRC009349-PA; RPRC009349.
DR VEuPathDB; VectorBase:RPRC009349; -.
DR eggNOG; KOG3526; Eukaryota.
DR HOGENOM; CLU_002976_4_4_1; -.
DR InParanoid; T1HZ79; -.
DR OMA; LAKQWHS; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016486; P:peptide hormone processing; IEA:UniProt.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 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 InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 467..603
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 388
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 636 AA; 70358 MW; 9F2216F93A853522 CRC64;
GGWSLILGAW ILVLITSYSC TALVFTNSFY VRLRGDGGQE AASLVAKRTG FDNFGPVLGS
QNEFHFVHRG LQEARTKRSI PHTRRLKVDP LVHMAVQMAG FKRVKRGYKP LVVENLVGEM
KPGRDPTDPY FQLQWYLKNT GQNGGKARLD LNVEAAWAQG VTGKNVTTAI MDDGVDYMHQ
DLKFNYNAKA SYDFSSNDQF PYPRYTDDWF NSHGTRCAGE VAAARDNDIC GVGVAYDSKI
AGIRMLDQPY MTDLIEANSM GHEPNLIDIY SASWGPTDDG KTVDGPRNAT MRAIVKGVNE
GRNGLGNIYV WASGDGGEED DCNCDGYAAS MWTISINSAI NDGQNAHYDE SCSSTLASTF
SNGAKDPNTG VATTDLYGKC TTTHSGTSAA APEAAGVFAL ALEANTQLTW RDIQHLTVLT
SKRNSLFDAK GRFHWTMNGV GLEFNHLFGF GVLDAGAMVA LAKQWRTVPA RYHCEAGSIN
RLQKISSNQP LFLKIETTAC QGTDTQVNFL EHVQAVITLN STRRGDVELF LTSPMGTRSM
ILSRRVNDND HRDGFTKWPF MTTHTWGEYP QGTWTLEVSF NSENVQSGFI KEWRLMLHGT
SDPPYTGLPV SDHHSKLAIV KKAHEERNSR SKHVYY
//
