ID A0A443SGD0_9ACAR Unreviewed; 677 AA.
AC A0A443SGD0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Proprotein convertase type 2-like protein {ECO:0000313|EMBL:RWS26566.1};
GN ORFNames=B4U80_02828 {ECO:0000313|EMBL:RWS26566.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS26566.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS26566.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS26566.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS26566.1}.
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DR EMBL; NCKV01002647; RWS26566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443SGD0; -.
DR STRING; 299467.A0A443SGD0; -.
DR EnsemblMetazoa; LDEU005474-RA; LDEU005474-PA; LDEU005474.
DR VEuPathDB; VectorBase:LDEU005474; -.
DR Proteomes; UP000288716; 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:UP000288716};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 497..650
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 202
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 418
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 677 AA; 75041 MW; 6E303750232255FA CRC64;
MVRLFSKQNG IGISAKCAVG GHSIRNASTF SLNIFLVVVT YLICVTGVTN SKSNDVYTNS
FYVRLTENHG PHVAHTIAKR YGFVNLGPVL KSGNEYHFVH RALPHARTKR SVSRTRLLLT
DPKVEVAVQQ KGFKRVKRGY NKLNVGTEHL LLNKEPTDPY FPFQWYLKNV GQNGGKPKLD
LNVEAAWAQG YTGKNVTTAI MDDGVDYMHP DIRDNYNAKA SYDFSSNDPF PYPRYTDDWF
NSHGTRCAGE VAAKRDNGIC GVGVAYDSKV AGIRMLDQPY MTDLIEANSM GHEPNLIDIY
SASWGPTDDG KTVDGPRNAT MRAIVRGVNE GRNGLGNIYV WASGDGGQDD DCNCDGYAAS
MWTISINSAI NNGENAHYDE SCSSTLASTF SNGAKDPHTG VATTDLYGKC TKTHSGTSAA
APEAAGVFAL ALEANPKLTW RDVQHLTVLT SKRNSLYDSK NRFHWNMNGV GLEFNHLFGY
GVLDAGAMVG LAKIWKSVPP RFHCDSGTFD KLSKIPANES LFLKLDTKAC ANTETEVNYV
EHVQAVITLN STRRGDVTLY LISPMGTRLV AIKIARPLIF VRANRSMILS RRPKDDDSRD
GFTKWPFMTT HTWGEDPKGR WKLEVRFESE QPQSGFIKEW TLMIHGTKQP PYKDLPAHDK
NSKLAIVKKA HESALKM
//
